Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light
Open accessAbstract
The leaf of kidney bean (Phaseolus vulgaris) moves in response to blue light. The movement is induced by a decrease in the turgor pressure of pulvinar motor cells on the irradiated side. In this study, we investigated the initial event of the movement with respect to function of phototropin and the plasma membrane H+-ATPase in the motor cells. The results indicated that, in dark conditions, phototropin existed in a dephosphorylated state and the H+-ATPase existed in a phosphorylated state. A pulse of blue light (30 s) induced the phosphorylation of phototropin and the dephosphorylation of the H+-ATPase as determined by the binding behavior of 14-3-3 protein. Phototropin phosphorylation occurred rapidly, followed by the transient gradual dephosphorylation of the H+-ATPase. When the specific flavoprotein inhibitor diphenyleneiodonium and the protein kinase inhibitors K-252a and staurosporine were administered to pulvinar cells, both phototropin phosphorylation and H+-ATPase dephosphorylation were inhibited. The phosphorylation and dephosphorylation exhibited similar fluence rate dependencies to blue light. These results indicated that phototropin may function upstream of the plasma membrane H+-ATPase and decrease the activity of H+-ATPase by dephosphorylation. We provide evidence for the existence of three kinds of phototropins in pulvinar motor cells.
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TL;DR
Blue light induces kidney bean leaf movement via pulvinar bending, and this study provides biochemical evidence that phototropin phosphorylation precedes blue-light-induced dephosphorylation/inactivation of the plasma membrane H⁺-ATPase in pulvinar motor cells. The authors propose phototropin acts upstream of the H⁺-ATPase, opposite to its activating role in stomatal guard cells.
Key findings
- Continuous blue light at 100 µmol m⁻² s⁻¹ for 120 min caused dark-adapted kidney bean leaves to rise, reaching their highest position at 90 min; side irradiation oriented leaves toward the light source.
- A 30-s blue light pulse rapidly induced phototropin phosphorylation, detected by 14-3-3 binding that peaked within 1 min, followed by transient H⁺-ATPase dephosphorylation, detected by 14-3-3 dissociation that fell to less than 40% of initial level at 5 min and recovered by 10 min.
- Phototropin binding and H⁺-ATPase dissociation had similar fluence-rate dependencies, with half-saturation values of 7.4 and 11.2 µmol m⁻² s⁻¹, respectively, and both saturated near 50 µmol m⁻² s⁻¹.
- Inhibitors suppressed both responses: DPI (100 µM) inhibited phototropin binding by 57% and H⁺-ATPase dissociation by 53%; K-252a (10 µM) inhibited them by 69% and 70%; staurosporine (10 µM) inhibited them by 47% and 49%. Three phototropin cDNAs, PvPHOT1a, PvPHOT1b, and PvPHOT2, were cloned from pulvini.
Methods
- Kidney bean (Phaseolus vulgaris cv Kentucky Wonder) plants were grown for 2 weeks; excised laminar pulvini were dark-adapted and irradiated with blue light pulses or continuous blue light.
- Microsomal membranes from pulvini were analyzed by immunoblotting and protein-blot analysis using GST-14-3-3 as a probe, plus immunoprecipitation and CNBr digestion to assess H⁺-ATPase C-terminal phosphorylation.
- Phototropin cDNAs were cloned by RT-PCR and RACE, and tissue-specific/light-regulated expression was examined by RT-PCR.
Limitations
- The paper states that the three phototropin isoproteins could not be distinguished from each other because of their similar molecular masses.
- The paper states that radiolabeling the H⁺-ATPase with ³²Pi was unsuccessful, probably due to insufficient incorporation into motor cells, so phosphorylation status was inferred from mobility shifts and 14-3-3 binding.
- Evident from the text: phototropin involvement is supported by pharmacological inhibition and correlative timing/fluence dependencies, not by genetic loss-of-function in Phaseolus; the direct causal link between these molecular events and leaf movement is not tested.
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- Findingown data§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1
In darkness, phototropin exists in a dephosphorylated state in pulvinar motor cells.
“The results indicated that, in dark conditions, phototropin existed in a dephosphorylated state and the H 1 -ATPase existed in a phosphorylated state.”
Quote in the paperSubstantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
- Findingown data§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1
Kidney bean leaves move in response to blue light.
“The leaf of kidney bean ( Phaseolus vulgaris ) moves in response to blue light.”
- Also stated in: § Blue Light Induces Pulvinar Bending of Kidney Bean · p. 2 · plain
“Blue Light Induces Pulvinar Bending of Kidney Bean”
Quote in the paperSubstantial claim - Also stated in: § Blue Light Induces Pulvinar Bending of Kidney Bean · p. 2 · plain
- Findingown data§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1
In darkness, the plasma membrane H+-ATPase exists in a phosphorylated state in pulvinar motor cells.
“The results indicated that, in dark conditions, phototropin existed in a dephosphorylated state and the H 1 -ATPase existed in a phosphorylated state.”
- Also stated in: § The Plasma Membrane H 1 -ATPase Was Dephosphorylated by Blue Light in Pulvini · p. 3 · hedged
“The results suggest that the H 1 -ATPase exists in a phosphorylated state with high activity in the motor cells under darkness”
Quote in the paperSubstantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
- Also stated in: § The Plasma Membrane H 1 -ATPase Was Dephosphorylated by Blue Light in Pulvini · p. 3 · hedged
- Findingown data§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1
A 30-s pulse of blue light induces phosphorylation of phototropin in pulvinar motor cells.
“A pulse of blue light (30 s) inducedthephosphorylationof phototropin and the dephosphorylation of the H 1 -ATPaseasdeterminedbythebindingbehavior of 14-3-3 protein.”
- Also stated in: § Phosphorylation of Phototropin Precedes Dephosphorylation of the H 1 -ATPase in Response to Blue Light in Pulvini · p. 3 · plain
“When the pulvini were irradiated with a pulse of blue light, 14-3-3 protein rapidly bound to phototropin and reached a maximum within 1 min after the pulse began”
Quote in the paperSubstantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
- Also stated in: § Phosphorylation of Phototropin Precedes Dephosphorylation of the H 1 -ATPase in Response to Blue Light in Pulvini · p. 3 · plain
- Findingown data§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1
A 30-s pulse of blue light induces dephosphorylation of the plasma membrane H+-ATPase in pulvinar motor cells.
“A pulse of blue light (30 s) inducedthephosphorylationof phototropin and the dephosphorylation of the H 1 -ATPaseasdeterminedbythebindingbehavior of 14-3-3 protein.”
- Also stated in: § The Plasma Membrane H 1 -ATPase Was Dephosphorylated by Blue Light in Pulvini · p. 3 · plain
“The amount of 14-3-3 protein started to decrease between 1 and 2.5 min after the initiation of a pulse of blue light and reached the minimum, less than 40% of initial level, at 5 min after the pulse began”
Quote in the paperSubstantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
- Also stated in: § The Plasma Membrane H 1 -ATPase Was Dephosphorylated by Blue Light in Pulvini · p. 3 · plain
- Findingown data§ The Plasma Membrane H 1 -ATPase Was Dephosphorylated by Blue Light in Pulvini · p. 3
Blue light does not affect the amount of H+-ATPase.
“The blue light did not affect the amount of the H 1 -ATPase (Fig. 2B).”
Quote in the paperSubstantial claim - Findingown data§ The Plasma Membrane H 1 -ATPase Was Dephosphorylated by Blue Light in Pulvini · p. 3
In dark-adapted pulvini, 14-3-3 protein is already bound to the H+-ATPase.
“As shown in Figure 2A, 14-3-3 protein was already bound to the H 1 -ATPase in the dark.”
Quote in the paperSubstantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
- Findingnone given§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1
Three kinds of phototropins exist in pulvinar motor cells of kidney bean.
“We provide evidence for the existence of three kinds of phototropins in pulvinar motor cells.”
Quote in the paperNot a substantial claim - Findingown data§ Blue Light Induces Pulvinar Bending of Kidney Bean · p. 2
Leaf movements are brought about by bending of a laminar pulvinus at the base of each leaf blade.
“These leaf movements were brought about by the bending of a laminar pulvinus located on the base of each leaf blade (Fig. 1F).”
Quote in the paperNot a substantial claim - Findingown data§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1
Phototropin phosphorylation and H+-ATPase dephosphorylation have similar fluence rate dependencies to blue light.
“The phosphorylation and dephosphorylation exhibited similar fluence rate dependencies to blue light.”
Quote in the paperSubstantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
- Findingown data§ Phosphorylation of Phototropin Precedes Dephosphorylation of the H 1 -ATPase in Response to Blue Light in Pulvini · p. 3
Maximum 14-3-3 binding to phototropin occurs earlier (1 min) than maximum dissociation from H+-ATPase (5 min).
“According to the time courses of 14-3-3 protein binding to phototropin, the maximum binding occurred earlier (at 1 min) than the maximum dissociation of 14-3-3 protein from the H 1 -ATPase (5 min; Fig. 2E).”
Quote in the paperSubstantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
- Findingown data§ Phosphorylation of Phototropin Precedes Dephosphorylation of the H 1 -ATPase in Response to Blue Light in Pulvini · p. 3
A second blue light pulse 20 min after the first causes 14-3-3 protein to bind again to phototropin.
“When the pulvini were irradiated with a second blue light pulse 20 min after the first pulse start, 14-3-3 protein bound again (data not shown).”
Quote in the paperNot a substantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
- Findingcitation§ Phosphorylation of Phototropin Precedes Dephosphorylation of the H 1 -ATPase in Response to Blue Light in Pulvini · p. 3
Phototropin shows a mobility shift to the upper side after blue light.
“The phototropin also exhibited a mobility shift to the upper side of the nonirradiated position, suggesting that the phototropin was phosphorylated in response to blue light as described previously (Short et al., 1993; Salomon et al., 2003; Knieb et al., 2004; Fig. 2, C and D).”
Quote in the paperSubstantial claim0 of 3 sources checked- cites Short et al., 1993
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- cites Salomon et al., 2003
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- cites Knieb et al., 2004
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- Findingown data§ Expression of PvPHOT s · p. 6
PvPHOT2 transcripts are detected only in green tissue, such as leaves and pulvini.
“PvPHOT2 transcripts were detected only in green tissue, such as leaves and pulvini.”
Quote in the paperNot a substantial claim - Findingown data§ Evidence for Dissociation of 14-3-3 Protein from the H 1 -ATPase and Binding of 14-3-3 Protein to Phototropin in Vivo · p. 5
Phototropin coprecipitates with 14-3-3 protein only when pulvini are irradiated with blue light.
“We found that phototropin was coprecipitated together with 14-3-3 protein only when the pulvini were irradiated by blue light (Fig. 5C).”
Quote in the paperSubstantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
- Findingown data§ Phosphorylation Levels of the H 1 -ATPase and Phototropin in Response to Blue Light in Pulvini · p. 4
K-252a inhibits binding of 14-3-3 protein to phototropin.
“The binding of 14-3-3 protein to phototropin was inhibited by K-252a in the same way (Fig. 4D).”
Quote in the paperSubstantial claim- Rests on an assumption: The inhibitors DPI, K-252a, and staurosporine act specifically on the targeted phototropin/kinase pathways in pulvinar cells without relevant off-target effects.
- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
- Findingown data§ Phosphorylation of Phototropin Precedes Dephosphorylation of the H 1 -ATPase in Response to Blue Light in Pulvini · p. 3
Blue light irradiation does not affect the amount of phototropin.
“The blue light irradiation did not affect the amount of phototropin (Fig. 2D).”
Quote in the paperNot a substantial claim - Findingown data§ Phosphorylation of Phototropin Precedes Dephosphorylation of the H 1 -ATPase in Response to Blue Light in Pulvini · p. 3
A phototropin with molecular mass 118 kD is present in pulvinar motor cells.
“Using the antibodies for Vicia phototropins, we found initially that phototropin with molecular mass of 118 kD was present in the motor cells (Fig. 2D).”
Quote in the paperSubstantial claim- Rests on an assumption: The anti-Vicia phototropin and anti-Vicia H+-ATPase antibodies used recognize the corresponding Phaseolus proteins.
- Findingcitation§ Light Dependencies of Dissociation of 14-3-3 Protein from the H 1 -ATPase and Binding of 14-3-3 Protein to Phototropin · p. 3
Phototropin mobility on SDS-PAGE decreases with increasing fluence rate, suggesting increased phosphorylation.
“The mobility of phototropin on SDS-PAGE decreased with increase in the fluence rate (Fig. 3D), suggesting that the levels of phototropin phosphorylation increased by blue light (Kinoshita et al., 2003; Salomon et al., 2003).”
Quote in the paperSubstantial claim0 of 2 sources checked- cites Kinoshita et al., 2003
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- cites Salomon et al., 2003
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- Findingown data§ Expression of PvPHOT s · p. 6
PvPHOT1a transcripts are found in etiolated seedlings, leaves, and pulvini.
“PvPHOT1a transcripts were found in etiolated seedlings, leaves, and pulvini.”
Quote in the paperNot a substantial claim - Findingown data§ Expression of PvPHOT s · p. 6
White light irradiation of etiolated seedlings increases PvPHOT2 mRNA with no detectable change in PvPHOT1a and PvPHOT1b mRNAs.
“Etiolated seedlings of 4-d-old plants, which were irradiated with white light at 75 m mol m 2 2 s 2 1 for 180 min, revealed an increase in PvPHOT2 mRNA with no detectable change in PvPHOT1a and PvPHOT1b mRNAs.”
Quote in the paperSubstantial claim - Findingown data§ Phosphorylation Levels of the H 1 -ATPase and Phototropin in Response to Blue Light in Pulvini · p. 4
CNBr digestion of Phaseolus H+-ATPase yields two peptides of 16 and 16.5 kD recognized by antibodies against the C terminus.
“We obtained two peptides with molecular masses of 16 and 16.5 kDs, both of which were recognized by the antibodies against the C terminus (Fig. 4A, left)”
Quote in the paperSubstantial claim - Findingown data§ Phosphorylation Levels of the H 1 -ATPase and Phototropin in Response to Blue Light in Pulvini · p. 4
The blue-light-induced mobility shift of phototropin is strongly suppressed by K-252a.
“We confirmed the mobility shift of phototropin by blue light and that the shift was strongly suppressed by a Ser/Thr kinase inhibitor K-252a (Fig. 4C).”
Quote in the paperSubstantial claim- Rests on an assumption: The inhibitors DPI, K-252a, and staurosporine act specifically on the targeted phototropin/kinase pathways in pulvinar cells without relevant off-target effects.
- Findingown data§ Cloning of Phototropins from Pulvini of Kidney Bean · p. 5
All Pvphots contain LOV1, LOV2, and Ser/Thr kinase domains.
“All Pvphots contained LOV1, LOV2, and Ser/Thr kinase domains, which were typically conserved in phototropins of other plants (Fig. 7A).”
Quote in the paperNot a substantial claim - Findingcitation§ Evidence for Dissociation of 14-3-3 Protein from the H 1 -ATPase and Binding of 14-3-3 Protein to Phototropin in Vivo · p. 5
Immunoprecipitation with antibodies against phototropin did not recover 14-3-3 protein in Phaseolus pulvini, as previously shown in Vicia guard cells.
“If we did the immunoprecipitation using antibodies against phototropin, we could not find 14-3-3 protein in the immunoprecipitate in Phaseolus pulvini as shown previously in Vicia guard cells (Kinoshita et al., 2003).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Kinoshita et al., 2003
Not checked in the free run.
- Rests on an assumption: The anti-Vicia phototropin and anti-Vicia H+-ATPase antibodies used recognize the corresponding Phaseolus proteins.
- Findingnone given§ Cloning of Phototropins from Pulvini of Kidney Bean · p. 5
A phototropin placed in the phot2 group had not been identified in leguminous plants before this study.
“A phototropin placed in the phot2 group had not been identified in leguminous plants thus far.”
Quote in the paperNot a substantial claim - Findingown data§ Expression of PvPHOT s · p. 6
PvPHOT1b transcripts are found in all tissues investigated.
“PvPHOT1b transcripts were found in all tissues investigated.”
Quote in the paperNot a substantial claim - Findingown data§ Light Dependencies of Dissociation of 14-3-3 Protein from the H 1 -ATPase and Binding of 14-3-3 Protein to Phototropin · p. 3
Both reactions saturate near 50 μmol m-2 s-1 with a 30-s pulse.
“Both reactions were saturated near 50 m mol m 2 2 s 2 1 when the pulse duration was 30 s (Fig. 3E).”
Quote in the paperNot a substantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
- Findingown data§ Biochemical Evidence for the Inactivation of the Plasma Membrane H 1 -ATPase by Blue Light in Pulvinar Motor Cells · p. 8
The degree to which 14-3-3 protein dissociated from the H+-ATPase depended on the intensity of the blue light.
“and that the degree of dissociation depended on the intensity of the light (Fig. 3A).”
Quote in the paperSubstantial claim - Findingown data§ Involvement of Phototropin in Blue Light-Induced Inactivation of the H 1 -ATPase · p. 8
In kidney bean, the light-capturing area of the leaf greatly increased in response to blue light.
“and that the lightcapturing area of the leaf was greatly increased in response to blue light (Fig. 1, A-D).”
Quote in the paperSubstantial claim - Findingown data§ Involvement of Phototropin in Blue Light-Induced Inactivation of the H 1 -ATPase · p. 8
Binding of 14-3-3 protein to phototropin and dissociation of 14-3-3 protein from the H+-ATPase had similar fluence rate dependencies.
“Second, the binding of 14-3-3 protein to phototropin and the dissociation of the protein from the H 1 -ATPase had similar fluence rate dependencies (Fig. 3E).”
Quote in the paperSubstantial claim - Findingown data§ Involvement of Phototropin in Blue Light-Induced Inactivation of the H 1 -ATPase · p. 8
In kidney bean, the leaf surface was oriented perpendicular to the direction of the light.
“we found that the leaf surface of kidney bean was oriented perpendicular to the light direction”
Quote in the paperSubstantial claim - Findingown data§ Phototropin-Mediated Blue Light Signal Transduction to the Plasma Membrane H 1 -ATPase · p. 8
In pulvinar motor cells, the greater portion of the H+-ATPase was phosphorylated on the C terminus in the dark.
“In pulvinar motor cells, the greater portion of the H 1 -ATPase was phosphorylated on the C terminus in the dark (Fig. 4A)”
Quote in the paperSubstantial claim - Findingown data§ Involvement of Phototropin in Blue Light-Induced Inactivation of the H 1 -ATPase · p. 8
A flavoprotein inhibitor and protein kinase inhibitors that inhibit phototropin activity also suppressed dephosphorylation of the H+-ATPase.
“Third, the flavoprotein inhibitor and protein kinase inhibitors, which inhibit the activity of phototropin, also suppressed dephosphorylation of the H 1 -ATPase (Fig. 6).”
Quote in the paperSubstantial claim - Findingown data§ Involvement of Phototropin in Blue Light-Induced Inactivation of the H 1 -ATPase · p. 8
Phosphorylation of phototropin preceded dephosphorylation of the H+-ATPase in response to blue light.
“First, the phosphorylation of phototropin preceded the dephosphorylation of the H 1 -ATPase in response to blue light (Fig. 2E).”
Quote in the paperSubstantial claim - Findingown data§ Biochemical Evidence for the Inactivation of the Plasma Membrane H 1 -ATPase by Blue Light in Pulvinar Motor Cells · p. 8
In pulvinar motor cells, 14-3-3 protein bound to the H+-ATPase transiently dissociated after a pulse of blue light.
“We found that the bound 14-3-3 protein transiently dissociated in response to a pulse of blue light (Fig. 2A)”
Quote in the paperSubstantial claim - Findingown data§ Involvement of Phototropin in Blue Light-Induced Inactivation of the H 1 -ATPase · p. 8
Three PvPHOT cDNAs were identified in pulvini.
“and identified three PvPHOT cDNAs (Fig. 7C) in pulvini.”
Quote in the paperNot a substantial claim - Findingown data§ Phototropin-Mediated Blue Light Signal Transduction to the Plasma Membrane H 1 -ATPase · p. 8
Activation of phototropin resulted in dephosphorylation of the H+-ATPase in motor cells.
“In this study, we found that the activation of phototropin resulted in dephosphorylation of the H 1 -ATPase in motor cells (Figs. 2, 3, and 6).”
Quote in the paperSubstantial claim - Premisecitation§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1
The leaf movement is induced by a decrease in turgor pressure of pulvinar motor cells on the irradiated side.
“The movement is induced by a decrease in the turgor pressure of pulvinar motor cells on the irradiated side.”
- Also stated in: § Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1 · plain
“This bending is mediated by a decrease in turgor pressure of pulvinar motor cells, which results in a decrease in cell volume on the irradiated side of the pulvinus (Wang et al., 2001).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites Wang et al., 2001
Not checked in the free run.
- Also stated in: § Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1 · plain
- Premisecitation§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1
Net K+ salt efflux is driven by depolarization-activated K+ channels in the plasma membrane.
“This net K 1 -salt efflux is driven by depolarization-activated K 1 channels in the plasma membrane (Moran et al., 1988; Moran, 1996; Suh et al., 2000)”
Quote in the paperNot a substantial claim0 of 3 sources checked- cites Moran et al., 1988
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- cites Moran, 1996
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- cites Suh et al., 2000
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- Premisecitation§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1
Depolarization is likely triggered by inactivation of the plasma membrane H+-ATPase in response to blue light.
“the depolarization is likely triggered by inactivation of the plasma membrane H 1 -ATPase in response to blue light (Kim et al., 1992; Nishizaki, 1994; Okazaki et al., 1995; Wang et al., 2001).”
Quote in the paperSubstantial claim0 of 3 sources checked- cites Kim et al., 1992
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- cites Nishizaki, 1994
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- cites Okazaki et al., 1995
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- Premisecitation§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1
Many leguminous plants orient their leaves in response to blue light independently of circadian leaf movement.
“Many leguminous plants orient their leaves in response to blue light, and this response is independent of leaf movement by circadian rhythms (Koller, 1990; Cote ´, 1995; Nishizaki, 1996).”
Quote in the paperNot a substantial claim0 of 3 sources checked- cites Koller, 1990
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- cites Cote ´, 1995
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- cites Nishizaki, 1996
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- Interpretationcitation§ Blue Light Induces Pulvinar Bending of Kidney Bean · p. 2
The properties of leaf movement may account for solar tracking in Phaseolus.
“The properties of leaf movement may account for those of solar tracking in Phaseolus plant (Ritter and Koller, 1994; Briggs and Christie, 2002).”
Quote in the paperNot a substantial claim0 of 2 sources checked- cites Ritter and Koller, 1994
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- cites Briggs and Christie, 2002
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- Interpretationcitation§ The Plasma Membrane H 1 -ATPase Was Dephosphorylated by Blue Light in Pulvini · p. 3
The amounts of 14-3-3 protein bound to H+-ATPase are closely related to ATP hydrolytic activity in response to blue light as shown by Okazaki (2002).
“The amounts of 14-3-3 protein bound to the H 1 -ATPase shown here were closely related to the levels of ATP hydrolytic activity in response to blue light as shown by Okazaki (2002).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites Okazaki (2002)
Not checked in the free run.
- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
- Premisecitation§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1
Okazaki (2002) demonstrated that blue light decreased ATP hydrolysis by inactivating the H+-ATPase in Phaseolus pulvinar protoplasts.
“Recently, Okazaki (2002) used pulvinar protoplasts from Phaseolus to demonstrate that blue light decreased ATP hydrolysis by inactivating the H 1 -ATPase.”
Quote in the paperSubstantial claim0 of 1 sources checked- cites Okazaki (2002)
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- Interpretationown data§ Evidence for Dissociation of 14-3-3 Protein from the H 1 -ATPase and Binding of 14-3-3 Protein to Phototropin in Vivo · p. 4
14-3-3 protein dissociates from H+-ATPase in vivo in response to blue light.
“The result indicates that the 14-3-3 protein dissociated from the H 1 -ATPase in vivo by blue light.”
Quote in the paperSubstantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
- Interpretationown data§ Phosphorylation Levels of the H 1 -ATPase and Phototropin in Response to Blue Light in Pulvini · p. 4
Dissociation of 14-3-3 protein from H+-ATPase by blue light is closely related to dephosphorylation of the C terminus of H+-ATPase.
“These results indicate that dissociation of 14-3-3 protein from the H 1 -ATPase by blue light is closely related to dephosphorylation of the C terminus of H 1 -ATPase.”
Quote in the paperSubstantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
- Interpretationown data§ Phosphorylation Levels of the H 1 -ATPase and Phototropin in Response to Blue Light in Pulvini · p. 4
Binding of 14-3-3 protein to phototropin depends on phosphorylation levels of phototropin.
“The results suggest that the binding of 14-3-3 protein to phototropin depends on the phosphorylation levels of phototropin.”
Quote in the paperSubstantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
- Interpretationown data§ Evidence for Dissociation of 14-3-3 Protein from the H 1 -ATPase and Binding of 14-3-3 Protein to Phototropin in Vivo · p. 5
14-3-3 protein binds to phototropin in vivo in response to blue light.
“The result demonstrates that the 14-3-3 protein bound to phototropin in vivo by blue light.”
Quote in the paperSubstantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
- Interpretationown data§ Requirement of Phototropin Phosphorylation for the Dephosphorylation of the Plasma Membrane H 1 -ATPase · p. 5
Phosphorylation of phototropin is required for dephosphorylation of H+-ATPase.
“They also suggest that phosphorylation of phototropin is required for dephosphorylation of the H 1 -ATPase.”
Quote in the paperSubstantial claim- Rests on an assumption: The inhibitors DPI, K-252a, and staurosporine act specifically on the targeted phototropin/kinase pathways in pulvinar cells without relevant off-target effects.
- Interpretationcitation§ Biochemical Evidence for the Inactivation of the Plasma Membrane H 1 -ATPase by Blue Light in Pulvinar Motor Cells · p. 8
Membrane depolarization in motor cells can also be induced by activation of an anion channel.
“However, the membrane depolarization can be induced also by the activation of an anion channel in the motor cells.”
Quote in the paperNot a substantial claim - Interpretationreasoning§ Involvement of Phototropin in Blue Light-Induced Inactivation of the H 1 -ATPase · p. 8
Phototropins most likely play a role in kidney bean leaf movement.
“Therefore, phototropins most likely play a role in kidney bean leaf movement.”
Quote in the paperSubstantial claim- Rests on an assumption: Photoreceptors mediating blue light-induced leaf movement in leguminous plants have not been identified.
- Premisecitation§ Biochemical Evidence for the Inactivation of the Plasma Membrane H 1 -ATPase by Blue Light in Pulvinar Motor Cells · p. 8
Inactivation of the H+-ATPase by blue light causes depolarization of the plasma membrane.
“Inactivation of the H 1 -ATPase by blue light causes the depolarization of the plasma membrane (Nishizaki, 1994; Okazaki, 2002)”
Quote in the paperSubstantial claim0 of 2 sources checked- cites Nishizaki, 1994
Not checked in the free run.
- cites Okazaki, 2002
Not checked in the free run.
- Premisecitation§ Phototropin-Mediated Blue Light Signal Transduction to the Plasma Membrane H 1 -ATPase · p. 9
Similar transient growth inhibition mediated by phototropin was found in rice coleoptiles in response to blue light.
“Very recently, similar transient growth inhibition mediated by phototropin was also found in coleoptiles of rice ( Oryza sativa ) in response to blue light (Haga et al., 2005).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Haga et al., 2005
Not checked in the free run.
- Premisecitation§ Plant Materials and Growth Conditions · p. 9
Blue light induces membrane depolarization in motor cells on both the flexor and extensor sides.
“We used these whole pulvini without dividing them into flexor and extensor cells because blue light induces membrane depolarization in motor cells on both the flexor and extensor sides (Nishizaki, 1988).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites Nishizaki, 1988
Not checked in the free run.
- Premisecitation§ Phototropin-Mediated Blue Light Signal Transduction to the Plasma Membrane H 1 -ATPase · p. 9
This growth inhibition was not inhibited by 5-nitro-2-(3-phenylpropylamino)-benzoic, an anion channel blocker.
“This growth inhibition was not inhibited by 5-nitro-2-(3-phenylpropylamino)-benzoic, an anion channel blocker (Parks et al., 1998).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites Parks et al., 1998
Not checked in the free run.
- Premisecitation§ Biochemical Evidence for the Inactivation of the Plasma Membrane H 1 -ATPase by Blue Light in Pulvinar Motor Cells · p. 8
Membrane depolarization leads to efflux of K+ salt through depolarization-activated K+ channels.
“leading to the efflux of K 1 -salt through the depolarization-activated K 1 channels (Moran, 1996; Suh et al., 2000).”
Quote in the paperSubstantial claim0 of 2 sources checked- cites Moran, 1996
Not checked in the free run.
- cites Suh et al., 2000
Not checked in the free run.
- Interpretationcitation§ Biochemical Evidence for the Inactivation of the Plasma Membrane H 1 -ATPase by Blue Light in Pulvinar Motor Cells · p. 8
Membrane depolarization in motor cells is likely caused mainly by inactivation of the plasma membrane H+-ATPase, because vanadate completely inhibits the depolarization.
“The membrane depolarization is likely elicited mainly by the inactivation of the plasma membrane H 1 -ATPase because the depolarization is completely inhibited by the addition of vanadate, a specific inhibitor of the H 1 -ATPase (Nishizaki, 1994).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites Nishizaki, 1994
Not checked in the free run.
- Interpretationreasoning§ Phototropin-Mediated Blue Light Signal Transduction to the Plasma Membrane H 1 -ATPase · p. 8
The difference in response between motor cells and guard cells seems to be generated by downstream components in these distinct cell types.
“This difference in response between motor cells and guard cells seems to be generated by the downstream components in these distinct cell types.”
Quote in the paperSubstantial claim - Interpretationown data§ Involvement of Phototropin in Blue Light-Induced Inactivation of the H 1 -ATPase · p. 8
Three separate lines of evidence support the function of phototropin in pulvinar motor cells as a photoreceptor in the leaf movement response.
“In this study, we obtained three separate lines of evidence supporting the function of phototropin in the pulvinar motor cells as a photoreceptor in the leaf movement response (Figs. 2, 3, and 6).”
Quote in the paperSubstantial claim - Premisecitation§ Phototropin-Mediated Blue Light Signal Transduction to the Plasma Membrane H 1 -ATPase · p. 8
In stomatal guard cells, most of the H+-ATPase was dephosphorylated under dark conditions.
“but in stomatal guard cells most of the H 1 -ATPase were dephosphorylated under the same condition (Kinoshita and Shimazaki, 1999).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites Kinoshita and Shimazaki, 1999
Not checked in the free run.
- Interpretationreasoning§ Phototropin-Mediated Blue Light Signal Transduction to the Plasma Membrane H 1 -ATPase · p. 9
The early phase growth inhibition might be caused by inactivation of the H+-ATPase by blue light.
“Therefore, the early phase growth inhibition might be caused by inactivation of the H 1 -ATPase by blue light.”
Quote in the paperSubstantial claim
- May combine two claims. 34
- The quote only partly states this claim. 3
- Classified as probably not a substantial claim. 26
May combine two claims.
Findingown data§ The Plasma Membrane H 1 -ATPase Was Dephosphorylated by Blue Light in Pulvini · p. 3After a blue light pulse, the amount of 14-3-3 protein bound to H+-ATPase decreases between 1 and 2.5 min, reaches less than 40% of initial at 5 min, and returns to original in another 5 min.
“The amount of 14-3-3 protein started to decrease between 1 and 2.5 min after the initiation of a pulse of blue light and reached the minimum, less than 40% of initial level, at 5 min after the pulse began, and then returned to the original level in another 5 min.”
Quote in the paperSubstantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
May combine two claims.
Findingown data§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1K-252a inhibits blue-light-induced phototropin phosphorylation and H+-ATPase dephosphorylation in pulvinar cells.
“When the specific flavoprotein inhibitor diphenyleneiodonium and the protein kinase inhibitors K-252a and staurosporine were administered to pulvinar cells, both phototropin phosphorylation and H 1 -ATPase dephosphorylation were inhibited.”
- Also stated in: § Requirement of Phototropin Phosphorylation for the Dephosphorylation of the Plasma Membrane H 1 -ATPase · p. 5 · plain
“K-252a at 10 m M inhibited the binding to phototropin by 69% and the dissociation from the H 1 -ATPase by 70% (Fig. 6, C and D).”
Quote in the paperSubstantial claim- Rests on an assumption: The inhibitors DPI, K-252a, and staurosporine act specifically on the targeted phototropin/kinase pathways in pulvinar cells without relevant off-target effects.
- Also stated in: § Requirement of Phototropin Phosphorylation for the Dephosphorylation of the Plasma Membrane H 1 -ATPase · p. 5 · plain
May combine two claims.
Findingown data§ Blue Light Induces Pulvinar Bending of Kidney Bean · p. 2Side irradiation with blue light causes leaves to orient to the light source, limited by contact of two leaves.
“When the dark-adapted plant was irradiated at the same intensity of blue light from the side, the leaves oriented to the source of light, although the orientation was limited by the contact of two leaves (Fig. 1D).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown data§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1DPI inhibits blue-light-induced phototropin phosphorylation and H+-ATPase dephosphorylation in pulvinar cells.
“When the specific flavoprotein inhibitor diphenyleneiodonium and the protein kinase inhibitors K-252a and staurosporine were administered to pulvinar cells, both phototropin phosphorylation and H 1 -ATPase dephosphorylation were inhibited.”
- Also stated in: § Requirement of Phototropin Phosphorylation for the Dephosphorylation of the Plasma Membrane H 1 -ATPase · p. 5 · plain
“DPI at 100 m M inhibited the binding of 14-3-3 protein to phototropin by 57% and the dissociation of 14-3-3 protein from the H 1 -ATPase by 53% (Fig. 6, A and B).”
Quote in the paperSubstantial claim- Rests on an assumption: The inhibitors DPI, K-252a, and staurosporine act specifically on the targeted phototropin/kinase pathways in pulvinar cells without relevant off-target effects.
- Also stated in: § Requirement of Phototropin Phosphorylation for the Dephosphorylation of the Plasma Membrane H 1 -ATPase · p. 5 · plain
May combine two claims.
Findingown data§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1Phototropin phosphorylation occurs rapidly and precedes the transient gradual dephosphorylation of the H+-ATPase.
“Phototropin phosphorylation occurred rapidly, followed by the transient gradual dephosphorylation of the H 1 -ATPase.”
- Also stated in: § Phosphorylation of Phototropin Precedes Dephosphorylation of the H 1 -ATPase in Response to Blue Light in Pulvini · p. 3 · plain
“the maximum binding occurred earlier (at 1 min) than the maximum dissociation of 14-3-3 protein from the H 1 -ATPase (5 min; Fig. 2E).”
Quote in the paperSubstantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
- Also stated in: § Phosphorylation of Phototropin Precedes Dephosphorylation of the H 1 -ATPase in Response to Blue Light in Pulvini · p. 3 · plain
May combine two claims.
Findingown data§ Blue Light Induces Pulvinar Bending of Kidney Bean · p. 2Continuous blue light at 100 μmol m-2 s-1 for 120 min from above causes dark-adapted kidney bean leaves to rise from pointing down to horizontal, reaching highest at 90 min.
“Before the irradiation, the leaves were closed and pointing completely down (Fig. 1A, 0 min) and rose to the horizontal position in response to the blue light, greatly increasing the lightreceptive area (Fig. 1, A and B, 120 min). The leaf reached its highest position at 90 min of blue light, and this position was maintained for the rest of the irradiation period (Fig. 1E).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown data§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1Staurosporine inhibits blue-light-induced phototropin phosphorylation and H+-ATPase dephosphorylation in pulvinar cells.
“When the specific flavoprotein inhibitor diphenyleneiodonium and the protein kinase inhibitors K-252a and staurosporine were administered to pulvinar cells, both phototropin phosphorylation and H 1 -ATPase dephosphorylation were inhibited.”
- Also stated in: § Requirement of Phototropin Phosphorylation for the Dephosphorylation of the Plasma Membrane H 1 -ATPase · p. 5 · plain
“staurosporine, a Ser/Thr protein kinase inhibitor, at 10 m M inhibited the binding of 14-3-3 protein to phototropin by 47% and its dissociation from the H 1 -ATPase by 49% (Fig. 6, E and F).”
Quote in the paperSubstantial claim- Rests on an assumption: The inhibitors DPI, K-252a, and staurosporine act specifically on the targeted phototropin/kinase pathways in pulvinar cells without relevant off-target effects.
- Also stated in: § Requirement of Phototropin Phosphorylation for the Dephosphorylation of the Plasma Membrane H 1 -ATPase · p. 5 · plain
May combine two claims.
Findingown data§ Phosphorylation of Phototropin Precedes Dephosphorylation of the H 1 -ATPase in Response to Blue Light in Pulvini · p. 3A blue light pulse causes 14-3-3 protein to bind rapidly to phototropin, reaching maximum within 1 min, then decreasing to basal levels within 10 min.
“When the pulvini were irradiated with a pulse of blue light, 14-3-3 protein rapidly bound to phototropin and reached a maximum within 1 min after the pulse began, after which the binding decreased gradually, returning to the basal levels within 10 min (Fig. 2C).”
Quote in the paperSubstantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
May combine two claims. The quote only partly states this claim.
Findingown data§ Requirement of Phototropin Phosphorylation for the Dephosphorylation of the Plasma Membrane H 1 -ATPase · p. 5Staurosporine at 10 μM inhibits binding to phototropin by 47% and dissociation from H+-ATPase by 49%.
“staurosporine, a Ser/Thr protein kinase inhibitor, at 10 m M inhibited the binding of 14-3-3 protein to phototropin by 47% and its dissociation from the H 1 -ATPase by 49% (Fig. 6, E and F).”
Quote in the paperSubstantial claim- Rests on an assumption: The inhibitors DPI, K-252a, and staurosporine act specifically on the targeted phototropin/kinase pathways in pulvinar cells without relevant off-target effects.
- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
May combine two claims. The quote only partly states this claim.
Findingown data§ Requirement of Phototropin Phosphorylation for the Dephosphorylation of the Plasma Membrane H 1 -ATPase · p. 5K-252a at 10 μM inhibits binding to phototropin by 69% and dissociation from H+-ATPase by 70%.
“K-252a at 10 m M inhibited the binding to phototropin by 69% and the dissociation from the H 1 -ATPase by 70% (Fig. 6, C and D).”
Quote in the paperNot a substantial claim- Rests on an assumption: The inhibitors DPI, K-252a, and staurosporine act specifically on the targeted phototropin/kinase pathways in pulvinar cells without relevant off-target effects.
- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
May combine two claims. The quote only partly states this claim.
Findingown data§ Requirement of Phototropin Phosphorylation for the Dephosphorylation of the Plasma Membrane H 1 -ATPase · p. 5DPI at 100 μM inhibits binding of 14-3-3 protein to phototropin by 57% and dissociation from H+-ATPase by 53%.
“DPI at 100 m M inhibited the binding of 14-3-3 protein to phototropin by 57% and the dissociation of 14-3-3 protein from the H 1 -ATPase by 53% (Fig. 6, A and B).”
Quote in the paperSubstantial claim- Rests on an assumption: The inhibitors DPI, K-252a, and staurosporine act specifically on the targeted phototropin/kinase pathways in pulvinar cells without relevant off-target effects.
- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
May combine two claims.
Findingown data§ Phosphorylation Levels of the H 1 -ATPase and Phototropin in Response to Blue Light in Pulvini · p. 4Only the 16.5-kD peptide binds 14-3-3 protein, and blue light decreases this binding.
“we indicated that only the 16.5-kD peptide had the binding ability to 14-3-3 protein and that the amount of this binding decreased by blue light (Fig. 4B).”
Quote in the paperSubstantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
May combine two claims.
Findingown data§ Phosphorylation Levels of the H 1 -ATPase and Phototropin in Response to Blue Light in Pulvini · p. 4Blue light decreases the amount of the upper 16.5-kD peptide and slightly increases the 16-kD peptide.
“found that the amount of upper 16.5-kD protein decreased by blue light with a slight increase in the amount of 16-kD peptide (Fig. 4A, right).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown data§ Cloning of Phototropins from Pulvini of Kidney Bean · p. 5Deduced Pvphot1a, Pvphot1b, and Pvphot2 proteins consist of 976, 987, and 996 amino acids and have molecular masses of 110, 111, and 112 kD.
“The deduced protein sequences of Pvphot1a, Pvphot1b, and Pvphot2 consisted of 976, 987, and 996 amino acids, respectively, and had molecular masses of 110, 111, and 112 kD, respectively.”
Quote in the paperNot a substantial claimMay combine two claims.
Findingown data§ Evidence for Dissociation of 14-3-3 Protein from the H 1 -ATPase and Binding of 14-3-3 Protein to Phototropin in Vivo · p. 4In vivo, 14-3-3 protein coprecipitates with H+-ATPase, and the amount decreases by 58% in response to blue light.
“As shown in Figure 5A, 14-3-3 protein was coprecipitated with the H 1 -ATPase, and the amount of the 14-3-3 protein decreased by 58% in response to blue light.”
Quote in the paperSubstantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
May combine two claims.
Findingown data§ Cloning of Phototropins from Pulvini of Kidney Bean · p. 5Pvphot1a and Pvphot1b belong to the phot1 group, and Pvphot2 belongs to the phot2 group.
“Therefore, Pvphot1a and Pvphot1b were placed into a phot1 group, and Pvphot2 was placed into a phot2 group.”
Quote in the paperNot a substantial claimMay combine two claims.
Findingown data§ Cloning of Phototropins from Pulvini of Kidney Bean · p. 5Pvphot1a and Pvphot1b have high identities (77%) to Vfphots and Psphot1 in leguminous plants but lower (about 68%) identities to phot1 in Arabidopsis.
“Pvphot1a and Pvphot1b have high (77%) identities to Vfphots and Psphot1 in leguminous plants, but lower (about 68%) identities to phot1 in Arabidopsis (Fig. 7B).”
Quote in the paperNot a substantial claimMay combine two claims.
Findingown data§ Light Dependencies of Dissociation of 14-3-3 Protein from the H 1 -ATPase and Binding of 14-3-3 Protein to Phototropin · p. 3As blue light fluence rate increases, 14-3-3 protein bound to H+-ATPase decreases and bound to phototropin increases.
“As the fluence rate of blue light increased, the amount of 14-3-3 protein bound to the H 1 -ATPase decreased (Fig. 3A), whereas the amount bound to phototropin increased (Fig. 3A).”
Quote in the paperSubstantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
Probably not a substantial claim: may not pass S3 (load-bearing).
Premisecitation§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1Phototropin phosphorylation occurs on multiple Ser residues.
“Phototropins undergo autophosphorylation in response to blue light (Christie et al., 1998; Sakai et al., 2001), and the phosphorylation occurs on multiple Ser residues (Short et al., 1994; Salomon et al., 2003).”
Quote in the paperNot a substantial claim0 of 2 sources checked- cites Short et al., 1994
Not checked in the free run.
- cites Salomon et al., 2003
Not checked in the free run.
May combine two claims.
Interpretationreasoning§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1Because Phaseolus pulvinar motor cells respond to blue light via protein components similar to guard cells, including H+-ATPase and K+ channels, phototropins most likely function in these cells.
“Since Phaseolus pulvinar motor cells respond to blue light via protein components similar to those in guard cells, including the H 1 -ATPase and K 1 channels, it is most likely that phototropins function also in these cells.”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
Premisecitation§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1Phototropins undergo autophosphorylation in response to blue light.
“Phototropins undergo autophosphorylation in response to blue light (Christie et al., 1998; Sakai et al., 2001), and the phosphorylation occurs on multiple Ser residues (Short et al., 1994; Salomon et al., 2003).”
Quote in the paperNot a substantial claim0 of 2 sources checked- cites Christie et al., 1998
Not checked in the free run.
- cites Sakai et al., 2001
Not checked in the free run.
May combine two claims.
Premisecitation§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1In kidney bean, blue light is absorbed by the laminar pulvinus and induces leaf movement through pulvinar bending.
“In kidney bean ( Phaseolus vulgaris ), blue light is absorbed by the laminar pulvinus, the leaf-moving site located between the petiole and leaf blade (Fig. 1F), and induces leaf movement through pulvinar bending (Koller, 1990; Cote ´, 1995).”
Quote in the paperSubstantial claim0 of 2 sources checked- cites Koller, 1990
Not checked in the free run.
- cites Cote ´, 1995
Not checked in the free run.
Probably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.
Premisecitation§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 114-3-3 protein binds to the hinge region between LOV1 and LOV2 in Vicia phototropins upon their phosphorylation in Vicia guard cells, and this binding is a key step in phototropin-mediated responses.
“Recently, Kinoshita et al. (2003) found that 14-3-3 protein bound to the hinge region between LOV1 and LOV2 in broad bean ( Vicia faba ) phototropins (Vfphots) upon their phosphorylation in Vicia guard cells and suggested that the binding of 14-3-3 protein to phototropins is a key step in phototropinmediated responses.”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Kinoshita et al. (2003)
Not checked in the free run.
Probably not a substantial claim: may not pass S3 (load-bearing).
Premisecitation§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1In guard cells, blue light activates the H+-ATPase via phosphorylation of the C terminus with subsequent binding of 14-3-3 protein.
“In guard cells, blue light activates the H 1 -ATPase via phosphorylation of the C terminus with subsequent binding of 14-3-3 protein to the H 1 -ATPase (Assmann and Shimazaki, 1999; Kinoshita and Shimazaki, 1999; Palmgren, 2001).”
Quote in the paperNot a substantial claim0 of 3 sources checked- cites Assmann and Shimazaki, 1999
Not checked in the free run.
- cites Kinoshita and Shimazaki, 1999
Not checked in the free run.
- cites Palmgren, 2001
Not checked in the free run.
Probably not a substantial claim: may not pass S3 (load-bearing).
Premisenone given§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1Stomatal opening is driven by increased turgor pressure in guard cells.
“Stomatal opening, which facilitates gas exchanges between the leaf and the atmosphere, is driven by increased turgor pressure in guard cells.”
Quote in the paperNot a substantial claimMay combine two claims.
Interpretationown data§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1Phototropin may function upstream of the plasma membrane H+-ATPase and decrease H+-ATPase activity by dephosphorylation.
“These results indicated that phototropin may function upstream of the plasma membrane H 1 -ATPase and decrease the activity of H 1 -ATPase by dephosphorylation.”
Quote in the paperSubstantial claim- Rests on an assumption: The inhibitors DPI, K-252a, and staurosporine act specifically on the targeted phototropin/kinase pathways in pulvinar cells without relevant off-target effects.
- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
Classified as probably not a substantial claim. May combine two claims.
Premisecitation§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1Phototropins are blue light receptors in guard cells, identified using Arabidopsis mutants.
“In recent studies using Arabidopsis ( Arabidopsis thaliana ) mutant plants, phototropins, which are receptor-type protein kinases with two light, oxygen, and voltage (LOV) domains (Huala et al., 1997; Briggs and Christie, 2002), were identified as blue light receptors in guard cells (Kinoshita et al., 2001; Doi et al., 2004).”
Quote in the paperSubstantial claim0 of 2 sources checked- cites Kinoshita et al., 2001
Not checked in the free run.
- cites Doi et al., 2004
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Probably not a substantial claim: may not pass S3 (load-bearing).
Premisecitation§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1The increase in guard cell turgor is induced by membrane hyperpolarization through activation of the plasma membrane H+-ATPase and subsequent K+ influx via hyperpolarization-activated K+ channels.
“This increase is induced by membrane hyperpolarization through the activation of the plasma membrane H 1 -ATPase and the subsequent influx of K 1 via hyperpolarizationactivated K 1 channels (Hedrich and Schroeder, 1989; Schroeder et al., 2001).”
Quote in the paperNot a substantial claim0 of 2 sources checked- cites Hedrich and Schroeder, 1989
Not checked in the free run.
- cites Schroeder et al., 2001
Not checked in the free run.
May combine two claims.
Premisecitation§ Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light 1 · p. 1The decrease in turgor pressure is caused by water efflux from motor cells, brought about by effluxes of K+ and Cl-.
“The decrease in turgor pressure is caused by water efflux from the motor cells, which is brought about by effluxes of K 1 and Cl 2 (Lowen and Satter, 1989; Okazaki et al., 2000).”
Quote in the paperNot a substantial claim0 of 2 sources checked- cites Lowen and Satter, 1989
Not checked in the free run.
- cites Okazaki et al., 2000
Not checked in the free run.
Probably not a substantial claim: may not pass S3 (load-bearing).
Study design and conductown data§ Phosphorylation of Phototropin Precedes Dephosphorylation of the H 1 -ATPase in Response to Blue Light in Pulvini · p. 3Values presented are means of three independent experiments with SEs.
“Values presented are means of three independent experiments with SEs.”
Quote in the paperNot a substantial claimClassified as probably not a substantial claim.
Premisecitation§ Biochemical Evidence for the Inactivation of the Plasma Membrane H 1 -ATPase by Blue Light in Pulvinar Motor Cells · p. 8Activation of the plasma membrane H+-ATPase requires phosphorylation of the penultimate threonine in its C-terminal region and subsequent binding of a 14-3-3 protein at that site.
“The plasma membrane H 1 -ATPase is known to be activated by phosphorylation of the penultimate Thr in the C terminus followed by 14-3-3 protein binding on this site (Fuglsang et al., 1999; Kinoshita and Shimazaki, 1999, 2002; Svennelid et al., 1999).”
Quote in the paperSubstantial claim0 of 3 sources checked- cites Fuglsang et al., 1999
Not checked in the free run.
- cites Kinoshita and Shimazaki, 1999, 2002
Not checked in the free run.
- cites Svennelid et al., 1999
Not checked in the free run.
May combine two claims.
Interpretationown data§ Phosphorylation Levels of the H 1 -ATPase and Phototropin in Response to Blue Light in Pulvini · p. 4The 16.5-kD peptide is the phosphorylated C terminus of Phaseolus H+-ATPase, and blue light decreases this phosphorylated peptide.
“The result suggests that 16.5-kD peptide is the phosphorylated C terminus of Phaseolus H 1 -ATPase and that the phosphorylated peptide was decreased by blue light.”
Quote in the paperSubstantial claimMay combine two claims.
Interpretationown data§ Requirement of Phototropin Phosphorylation for the Dephosphorylation of the Plasma Membrane H 1 -ATPase · p. 5These inhibitors inhibit phototropin function, thereby interrupting signaling to H+-ATPase in pulvinar motor cells.
“These observations indicate that these three lines of inhibitors inhibit phototropin function, thereby interrupting the signaling to the H 1 -ATPase in pulvinar motor cells.”
Quote in the paperSubstantial claim- Rests on an assumption: The inhibitors DPI, K-252a, and staurosporine act specifically on the targeted phototropin/kinase pathways in pulvinar cells without relevant off-target effects.
Classified as probably not a substantial claim.
Study design and conductown data§ Evidence for Dissociation of 14-3-3 Protein from the H 1 -ATPase and Binding of 14-3-3 Protein to Phototropin in Vivo · p. 5The same amounts of 14-3-3 protein were used for immunoprecipitation.
“The same amounts of 14-3-3 protein were used for the immunoprecipitation (Fig. 5D).”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.
Study design and conductown data§ Cloning of Phototropins from Pulvini of Kidney Bean · p. 6Experiments were repeated three times on different occasions and gave similar results.
“Experiments repeated three times on different occasions gave similar results.”
Quote in the paperNot a substantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
Interpretationcitation§ Expression of PvPHOT s · p. 6This result agrees with previous observations that light induces expression of the phot2 group.
“This result agrees with the previous observations that light induces the expression of the phot2 group (Kanegae et al., 2000; Jarillo et al., 2001; Kagawa et al., 2001).”
Quote in the paperNot a substantial claim0 of 3 sources checked- cites Kanegae et al., 2000
Not checked in the free run.
- cites Jarillo et al., 2001
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- cites Kagawa et al., 2001
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Classified as probably not a substantial claim.
Study design and conductown data§ Evidence for Dissociation of 14-3-3 Protein from the H 1 -ATPase and Binding of 14-3-3 Protein to Phototropin in Vivo · p. 4The same amount of H+-ATPase was used in the immunoprecipitation experiment.
“We confirmed that the same amount of H 1 -ATPase was used in this experiment (Fig. 5B).”
Quote in the paperSubstantial claimMay combine two claims.
Study design and conductown data§ Phosphorylation of Phototropin Precedes Dephosphorylation of the H 1 -ATPase in Response to Blue Light in Pulvini · p. 3The GST probe did not bind to either H+-ATPase or phototropin.
“The GST probe was bound to neither the H 1 -ATPase nor phototropin (data not shown).”
Quote in the paperNot a substantial claimClassified as probably not a substantial claim.
Study design and conductown data§ Cloning of Phototropins from Pulvini of Kidney Bean · p. 6Immunoblot analyses showed each lane contained an equal amount of protein.
“Immunoblot analyses showed that each lane contained an equal amount of protein (data not shown).”
Quote in the paperSubstantial claimMay combine two claims.
Interpretationown data§ The Plasma Membrane H 1 -ATPase Was Dephosphorylated by Blue Light in Pulvini · p. 3The H+-ATPase exists in a phosphorylated state with high activity in motor cells under darkness and is inactivated by dephosphorylation with dissociation of 14-3-3 protein in response to blue light.
“The results suggest that the H 1 -ATPase exists in a phosphorylated state with high activity in the motor cells under darkness and that the H 1 -ATPase is inactivated by dephosphorylation with the dissociation of 14-3-3 protein from the H 1 -ATPase in response to blue light.”
Quote in the paperSubstantial claim- Rests on an assumption: In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
Classified as probably not a substantial claim.
Interpretationreasoning§ Phototropin-Mediated Blue Light Signal Transduction to the Plasma Membrane H 1 -ATPase · p. 8The difference in H+-ATPase phosphorylation status between motor cells and guard cells may be produced by the activity balance between unidentified protein kinases and phosphatases acting on the C terminus.
“This difference may be produced by the activity balance between a set of unidentified protein kinase(s) and protein phosphatase(s) whose substrates are the C terminus of plasma membrane H 1 -ATPase.”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
Study design and conductown data§ Expression of PvPHOT s · p. 7Separate experiments repeated three times gave similar results.
“Separate experiments repeated three times gave similar results.”
Quote in the paperNot a substantial claimClassified as probably not a substantial claim.
Premisecitation§ Phototropin-Mediated Blue Light Signal Transduction to the Plasma Membrane H 1 -ATPase · p. 9Phot1 mediates the early phase of growth inhibition in Arabidopsis hypocotyls in response to blue light.
“For example, Folta and Spalding (2001) demonstrated that phot1 mediates the early phase of growth inhibition in Arabidopsis hypocotyls in response to blue light.”
Quote in the paperSubstantial claim0 of 1 sources checked- cites Folta and Spalding, 2001
Not checked in the free run.
Probably not a substantial claim: may not pass S1 (asserted), S3 (load-bearing), S4 (based). May combine two claims.
Interpretationreasoning§ Phototropin-Mediated Blue Light Signal Transduction to the Plasma Membrane H 1 -ATPase · p. 8The phototropin-mediated light signal may inactivate protein phosphatase in guard cells but activate the phosphatase in motor cells.
“For example, phototropin-mediated light signal may inactivate protein phosphatase in guard cells but activate the phosphatase in motor cells.”
Quote in the paperNot a substantial claimMay combine two claims.
Interpretationown data§ Biochemical Evidence for the Inactivation of the Plasma Membrane H 1 -ATPase by Blue Light in Pulvinar Motor Cells · p. 8Blue light inactivates the plasma membrane H+-ATPase in pulvinar motor cells by dephosphorylating the phosphorylated C-terminal threonine and then causing dissociation of 14-3-3 protein.
“These results demonstrate that the H 1 -ATPase is inactivated by dephosphorylation of the phosphorylated Thr in the C terminus and by the subsequent dissociation of 14-3-3 protein in the motor cells by blue light.”
Quote in the paperSubstantial claimMay combine two claims.
Interpretationown data§ Phototropin-Mediated Blue Light Signal Transduction to the Plasma Membrane H 1 -ATPase · p. 8The H+-ATPase is not a direct substrate for phototropin kinase, and other components must lie between phototropin and the H+-ATPase.
“This observation clearly indicates that the H 1 -ATPase is not a direct substrate for phototropin kinase and that there must be other components between phototropin and the H 1 -ATPase.”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
Study design and conductown data§ Involvement of Phototropin in Blue Light-Induced Inactivation of the H 1 -ATPase · p. 8The phototropin isoproteins could not be distinguished from one another because of their similar molecular masses.
“However, we could not distinguish these isoproteins from each other because of their similar molecular masses.”
Quote in the paperNot a substantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
Study design and conductnone given§ Expression of PvPHOT s · p. 7ACTIN was used as an internal standard for cDNA amounts.
“ACTIN was used as an internal standard for cDNA amounts.”
Quote in the paperNot a substantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
Premisecitation§ Biochemical Evidence for the Inactivation of the Plasma Membrane H 1 -ATPase by Blue Light in Pulvinar Motor Cells · p. 8In Arabidopsis hypocotyls, activation of the anion channel seems to be induced by cry1 and cry2 as blue light receptors.
“and the activation seems to be induced by cry1 and cry2 as blue light receptors (Spalding and Cosgrove, 1989; Cho and Spalding, 1996; Parks et al., 1998; Folta and Spalding, 2001).”
Quote in the paperNot a substantial claim0 of 3 sources checked- cites Spalding and Cosgrove, 1989
Not checked in the free run.
- cites Cho and Spalding, 1996
Not checked in the free run.
- cites Folta and Spalding, 2001
Not checked in the free run.
Probably not a substantial claim: may not pass S3 (load-bearing).
Premisecitation§ Biochemical Evidence for the Inactivation of the Plasma Membrane H 1 -ATPase by Blue Light in Pulvinar Motor Cells · p. 8In Arabidopsis hypocotyls, a blue light-activated anion channel brings about membrane depolarization.
“We note that the membrane depolarization is brought about by a blue light-activated anion channel in Arabidopsis hypocotyls”
Quote in the paperNot a substantial claim0 of 3 sources checked- cites Spalding and Cosgrove, 1989
Not checked in the free run.
- cites Cho and Spalding, 1996
Not checked in the free run.
- cites Parks et al., 1998
Not checked in the free run.
Probably not a substantial claim: may not pass S3 (load-bearing).
Premisecitation§ Involvement of Phototropin in Blue Light-Induced Inactivation of the H 1 -ATPase · p. 8Phototropins dramatically enhance the growth of Arabidopsis plants under low-light environments.
“Very recently, Takemiya et al. (2005) demonstrated that phototropins dramatically enhance the growth of Arabidopsis plants under low-light environments”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Takemiya et al., 2005
Not checked in the free run.
Classified as probably not a substantial claim. May combine two claims.
Premisecitation§ Involvement of Phototropin in Blue Light-Induced Inactivation of the H 1 -ATPase · p. 8In Arabidopsis, phototropins mediate phototropism, chloroplast relocation, rapid inhibition of stem growth, and leaf expansion.
“In Arabidopsis, phototropins mediate phototropism (Huala et al., 1997; Christie et al., 1998; Sakai et al., 2001), chloroplast relocations (Jarillo et al., 2001; Kagawa et al., 2001; Sakai et al., 2001), rapid inhibition of stem growth (Folta and Spalding, 2001; Parks et al., 2001), and leaf expansion (Sakamoto and Briggs, 2002).”
Quote in the paperSubstantial claim0 of 3 sources checked- cites Huala et al., 1997
Not checked in the free run.
- cites Christie et al., 1998
Not checked in the free run.
- cites Sakai et al., 2001
Not checked in the free run.
May combine two claims.
Interpretationcitation§ Phototropin-Mediated Blue Light Signal Transduction to the Plasma Membrane H 1 -ATPase · p. 8The phototropin-mediated signal inactivates the H+-ATPase in pulvinar motor cells, whereas the same signal activates the H+-ATPase in stomatal guard cells.
“These results suggest that the phototropin-mediated signal inactivates the H 1 -ATPase in pulvinar motor cells, while the same signal activates the H 1 -ATPase in stomatal guard cells (Kinoshita et al., 2001).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites Kinoshita et al., 2001
Not checked in the free run.
Classified as probably not a substantial claim.
Interpretationcitation§ Involvement of Phototropin in Blue Light-Induced Inactivation of the H 1 -ATPase · p. 8The growth enhancement by phototropins indicates that phototropins improve photosynthetic performance.
“a finding that indicates the improvement of photosynthetic performance by phototropins.”
Quote in the paperSubstantial claim0 of 1 sources checked- cites Takemiya et al., 2005
Not checked in the free run.
Probably not a substantial claim: may not pass S4 (based).
Interpretationreasoning§ Phototropin-Mediated Blue Light Signal Transduction to the Plasma Membrane H 1 -ATPase · p. 8When pulvini or stomata are irradiated with blue light, activated phototropin would change the balance of kinase and phosphatase activities in opposite directions between motor cells and guard cells.
“When the pulvini or stomata are irradiated with blue light, activated phototropin would change the balance of activities in the opposite direction between motor cells and guard cells.”
Quote in the paperNot a substantial claim
The paper relies on this without support.
The biochemical evidence for blue-light inactivation of the plasma membrane H+-ATPase in pulvinar motor cells is insufficient, and the blue-light receptor responsible for this inactivation has not been identified.
“However, biochemical evidence for this response is insufficient, and the blue light receptor responsible for the inactivation of H 1 -ATPase has yet to be identified.”
The paper relies on this without support.
The inhibitors DPI, K-252a, and staurosporine act specifically on the targeted phototropin/kinase pathways in pulvinar cells without relevant off-target effects.
“When the specific flavoprotein inhibitor diphenyleneiodonium and the protein kinase inhibitors K-252a and staurosporine were administered to pulvinar cells, both phototropin phosphorylation and H 1 -ATPase dephosphorylation were inhibited.”
“These observations indicate that these three lines of inhibitors inhibit phototropin function, thereby interrupting the signaling to the H 1 -ATPase in pulvinar motor cells.”
The paper relies on this without support.
The anti-Vicia phototropin and anti-Vicia H+-ATPase antibodies used recognize the corresponding Phaseolus proteins.
“Using the antibodies for Vicia phototropins, we found initially that phototropin with molecular mass of 118 kD was present in the motor cells (Fig. 2D).”
“Anti-Vicia-H 1 -ATPase antibodies were used.”
The paper relies on this without support.
In pulvinar motor cells, the amount of 14-3-3 protein bound to the H+-ATPase and phototropin can be used as a measure of their phosphorylation status.
“We considered that the binding of 14-3-3 protein to the plasma membrane H 1 -ATPase reflected phosphorylation levels of the H 1 -ATPase. However, there is no direct evidence for this in pulvinar motor cells.”
The paper relies on this without support.
Sustained efflux of K+ salt decreases turgor pressure in motor cells exposed to blue light, thereby inducing leaf movement.
“The sustained efflux of K 1 -salt finally results in decreased turgor pressure of motor cells exposed to blue light, thereby inducing leaf movement.”
The paper relies on this without support.
Blue light inactivation of the H+-ATPase ultimately causes shrinkage of motor cells in the kidney bean pulvinus.
“Inactivation of the H 1 -ATPase by blue light ultimately elicits shrinkage of the motor cells in the pulvinus of kidney bean.”
The paper relies on this without support.
Photoreceptors mediating blue light-induced leaf movement in leguminous plants have not been identified.
“Photoreceptors that mediate blue light-induced leaf movement in leguminous plants have not been identified.”
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
Each contradiction between two passages listed here was confirmed by an independent check.
Phototropin binding is cited to the wrong Figure 3 panel
MinorThe results cite Figure 3A for phototropin binding, but the figure caption identifies panel A as H+-ATPase binding and panel C as phototropin binding.
“whereas the amount bound to phototropin increased (Fig. 3A).”
“A, Binding of 14-3-3 protein to the H 1 -ATPase. B, Immunoblotting of the H 1 -ATPase. C, Binding of 14-3-3 protein to phototropin.”
The citation lists haven’t been fetched yet
References 48 · Cited by 52
- Authors
- Inoue, S.-I., Kinoshita, T., & Shimazaki, K.-I.
- Affiliations
- Kyushu University (JP)
- Venue
- Plant Physiology
- Publisher
- Oxford University Press (OUP)
- Published
- 2005-07-22
- Volume
- 138
- Issue
- 4
- Pages
- 1994-2004
- ISSN
- 0032-0889 (ISSN-L)
- 1532-2548
- PMC
- PMC1183390
- OpenAlex
- W2105532285
- Semantic Scholar
- d0c5dceb60302da84db0b5ccf9d3c6c38ba8679f
- Cited by
- 52
- References
- 48
- Citations by year
- 2025: 2 · 2024: 2 · 2023: 1 · 2022: 1 · 2021: 3 · 2020: 1 · 2019: 2 · 2017: 1 · 2016: 1 · 2015: 2 · 2014: 8 · 2013: 2 · 2012: 3
- FWCI
- 7.60
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- PLANT PHYSIOLOGY (publishedVersion, public-domain)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Light effects on plants
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Keywords
- phototropin, blue light, leaf movement, Phaseolus vulgaris, plasma membrane H+-ATPase, protein phosphorylation, dephosphorylation, 14-3-3 proteins, diphenyleneiodonium, protein kinase inhibitors, turgor pressure
- MeSH terms
- Amino Acid Sequence, Flavoproteins, Proton-Translocating ATPases, Light, Molecular Sequence Data, Phylogeny, Protein Binding, RNA, Messenger, Sequence Homology, Amino Acid, Gene Expression Regulation, Plant, Plant Leaves, Phototropism, Phaseolus, 14-3-3 Proteins, Cryptochromes
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