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Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease
Open accessAbstract
The microtubule-associated protein Tau is a major component of the neurofibrillary tangles that serve as a neuropathological hallmark of Alzheimer's disease. Tau is a substrate for protein phosphorylation at multiple sites and occurs in tangles in a hyperphosphorylated state. However, the physiological functions of Tau phosphorylation or how it may contribute mechanistically to Alzheimer's pathophysiology are not completely understood. Here, we examined the function of human Tau phosphorylation at three sites, Ser199, Ser202, and Thr205, which together comprise the AT8 sites that mark abnormal phosphorylation in Alzheimer's disease. Overexpression of wild-type Tau or mutated forms in which these sites had been changed to either unphosphorylatable alanines or phosphomimetic aspartates inhibited mitochondrial movement in the neurite processes of PC12 cells as well as the axons of mouse brain cortical neurons. However, the greatest effects on mitochondrial translocation were induced by phosphomimetic mutations. These mutations also caused expansion of the space between microtubules in cultured cells when membrane tension was reduced by disrupting actin filaments. Thus, Tau phosphorylation at the AT8 sites may have meaningful effects on mitochondrial movement, likely by controlling microtubule spacing. Hyperphosphorylation of the AT8 sites may contribute to axonal degeneration by disrupting mitochondrial transport in Alzheimer's disease.
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Written from the paper’s full text.
TL;DR
Tau phosphorylation at the Alzheimer’s disease–associated AT8 sites (Ser199/Ser202/Thr205) more strongly inhibits mitochondrial movement than wild-type or nonphosphorylatable Tau. The phosphomimetic Tau 3D also expands inter-microtubule spacing under reduced membrane tension, suggesting a mechanism linking AT8 phosphorylation to impaired axonal mitochondrial transport.
Key findings
- In NGF-treated PC12 cell neurites, the stationary mitochondrial fraction was 23.0% in controls, 47.6% with Tau WT, 44.1% with Tau 3A, and 61.3% with phosphomimetic Tau 3D.
- In cultured mouse cortical neuron axons, stationary mitochondria were 31.6% in controls, 48.5% with Tau WT, 46.6% with Tau 3A, and 64.4% with Tau 3D.
- In latrunculin B–treated Sf9 cell processes, mean inter-microtubule distances were 26.8 ± 2.7 nm for Tau WT, 27.2 ± 2.0 nm for Tau 3A, and 37.1 ± 2.3 nm for Tau 3D.
- Tau did not alter kinesin head-domain binding to microtubules in vitro, and in PC12 neurites Tau overexpression reduced inter-MT distances to ~33–34 nm without significant differences among WT, 3A, and 3D.
Methods
- The longest human Tau was mutated at Ser199, Ser202, and Thr205 to nonphosphorylatable alanines (3A) or phosphomimetic aspartates (3D); WT, 3A, and 3D were expressed in PC12 cells, mouse embryonic cortical neurons, COS-7 cells, and Sf9 cells.
- Mitochondrial movement was imaged with Mito-GFP at 5 s intervals over 300 s in PC12 neurites and cortical neuron axons; inter-MT distances were measured by electron microscopy, including Sf9 cells treated with latrunculin B to disrupt actin filaments.
- In vitro assays examined Tau phosphorylation by Cdk5-p25, Tau binding to microtubules, and kinesin motor-domain binding to microtubules; statistics used one-way ANOVA with Holm’s test and ANCOVA.
Limitations
- The paper states that untreated Sf9 cells formed only a small number of processes, so the number of inter-MT distances counted was not sufficient; latrunculin B was used to increase process formation.
- The paper notes that in matured or aged neurons, Tau may not be the only space-making protein affecting mitochondrial movement, and that neurofilament tail domains may also contribute; the phosphorylation-dependent tunnel-opening/closing idea is described as a working hypothesis to be explored further.
- Evident from the text: the study relies on cell-culture overexpression systems and phosphomimetic mutants rather than human AD tissue or in vivo models, so the 3D mutant may not fully replicate native phosphorylation effects.
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Claims the paper makes
48 Own result · 15 Own interpretation · 12 Partly supported · 6 No full text of the sources · 4 Not checked yet · 3 No basis given · 2 Supported so far · 2 Couldn’t confirm · 1 Supported · 1 Own method · accuracy not yet measured
The cited sources support only part of this claim — read each source’s verdict below.
In the paper
“confirming that Cdk5 indeed phosphorylated the sites recognized by AT8 (Takahashi et al., 2003) and that these phosphorylation sites were disrupted in 3A and 3D constructs.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Phosphorylation of Tau mutants and their binding to MTs
What the sources say
- Partly supportedcites Takahashi et al., 2003 sourceExperimental — accuracy not yet measured
The Results and Discussion report that Cdk5 is involved in tau phosphorylation detected by AT-8, particularly at Ser-202 and Thr-205 during brain development. The Chemicals and Antibodies section defines AT-8 recognition by phosphorylation at those two sites, not Ser-199; our copy therefore does not support including Ser-199 among the AT-8-recognized sites. Page numbers were not available in our copy. (LLM, conf=0.90)
boosteddirect- Asserted: passes — The authors put it forward as true.
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- Partly supported
The sources with a verdict support this claim; the rest weren’t checked yet, have no full text we could read, or their verdicts aren’t rated yet.
In the paper
“Overexpression of Tau inhibits mitochondrial transport in various cells (Ebneth et al., 1998;Trinczek et al., 1999;Stamer et al., 2002;Dixit et al., 2008;Stoothoff et al., 2009;Vossel et al., 2010).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Introduction
What the sources say
- Supportedcites Ebneth et al., 1998 source
The Results report reduced mitochondrial transport in tau-overexpressing cells, with plus-end–directed transport decreasing approximately tenfold. A separate Results section reports impaired transport into neurites of N2a neuroblastoma cells and explicitly says this resembles the phenotype in CHO cells. (LLM, conf=0.94)
- Not checked — no full text of the sourcecites Trinczek et al., 1999 source
- Supportedcites Stamer et al., 2002 source
The Results section reports that mitochondria nearly disappeared from neurites in tau-transfected cells and that their transport was severely impaired. The Discussion states that the effects of elevated tau were observed in differentiated neuroblastoma cells, primary neurons, and chick retinal ganglion cells. (LLM, conf=0.94)
plaindirect- Asserted: passes — The authors put it forward as true.
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- Supported
The cited sources support only part of this claim — read each source’s verdict below.
In the paper
“Overexpression of either Tau WT, 3A, or 3D reduced anterograde movement of mitochondria in PC12 cells and cortical neurons, as reported (Mandelkow et al., 2004;Hollenbeck and Saxton, 2005;Dixit et al., 2008).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
What the sources say
- Partly supportedcites Mandelkow et al., 2004 sourceExperimental — accuracy not yet measured
The Results (Fig. 5; page unavailable) show that tau expression reduced anterograde mitochondrial movement in retinal ganglion cell axons, and Fig. 7 reports transport inhibition by a non-phosphorylatable tau mutant. The paper does not establish the stated effect for Tau 3D or in PC12 cells and cortical neurons; its experiments here use retinal ganglion cells and a KXGA mutant. (LLM, conf=0.88)
- Not checked — no full text of the sourcecites Hollenbeck and Saxton, 2005 source
- Not checked — no full text of the sourcecites Dixit et al., 2008 source
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
- Partly supported
The sources with a verdict support this claim; the rest weren’t checked yet, have no full text we could read, or their verdicts aren’t rated yet.
In the paper
“Tau overexpression inhibits mitochondrial movement in various cell types (Ebneth et al., 1998;Trinczek et al., 1999;Stamer et al., 2002;Dixit et al., 2008;Stoothoff et al., 2009;Vossel et al., 2010).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
What the sources say
- Supportedcites Ebneth et al., 1998 source
The Results section reports that tau overexpression reduced mitochondrial transport, especially plus-end–directed movement. The Discussion states that the study examined intracellular transport in both CHO and neuroblastoma cells, supporting the claim's reference to multiple cell types. (LLM, conf=0.93)
- Not checked — no full text of the sourcecites Trinczek et al., 1999 source
- Supportedcites Stamer et al., 2002 source
The Results sections report that elevated tau depletes mitochondria from the neurites of N2a cells and primary neurons. Time-lapse imaging of chick retinal ganglion neurons more directly shows that tau overexpression increases the immobile fraction of mitochondria and sharply reduces anterograde movement. The paper thus supports inhibition of mitochondrial movement across several cell types, although movement is not abolished. (LLM, conf=0.93)
plaindirect- Asserted: passes — The authors put it forward as true.
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- Supported
The cited sources support only part of this claim — read each source’s verdict below.
In the paper
“Considering that mitochondria would be transported within MT bundles in cultured neurons (Yu and Baas, 1994;Rochlin et al., 1996), limited spacing between MTs may block mitochondrial movement in neuritic processes such as axon and dendrites.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
What the sources say
- Supportedcites Yu and Baas, 1994 source
The citation supports the premise that mitochondria travel along microtubules in cultured neurons: the paper’s introductory passage describes microtubules as railways for organelles including mitochondria, and its Results describe closely spaced, parallel microtubules in axons. The suggestion that limited spacing may block movement is the citing authors’ own inference after the citations, not a finding they attribute to Yu and Baas. (LLM, conf=0.86)
- Partly supportedcites Rochlin et al., 1996 sourceExperimental — accuracy not yet measured
The Additional information section says microtubules could provide a scaffold along which endoplasmic reticulum and other axoplasmic elements advance. It does not specifically describe mitochondrial transport within microtubule bundles. The suggestion that limited spacing may block movement is the citing authors’ inference, not a finding attributed to this source. (LLM, conf=0.76)
hedgedconditional- Asserted: passes — The authors put it forward as true.
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- Based: passes — The paper gives a reason why it holds.
- Supported
The cited sources support only part of this claim — read each source’s verdict below.
In the paper
“When the Ser199/Ser202/Thr205 sites are phosphorylated the N-terminal domain swings away from the C-terminal domain, resulting in a conformation that extends from the MT wall (Jeganathan et al., 2008).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
What the sources say
- Partly supportedcites Jeganathan et al., 2008 sourceExperimental — accuracy not yet measured
The Results passage on the AT8* mutant (page unavailable) reports that mimicking phosphorylation at Ser199, Ser202, and Thr205 makes the N-terminal domain swing away from the C-terminal domain. The paper used phosphomimetic mutations rather than directly phosphorylating those sites. It separately states that Tau’s N-terminal domain projects away from the microtubule surface, but does not establish that AT8* produces a conformation extending from the microtubule wall. (LLM, conf=0.87)
plaindirect- Asserted: passes — The authors put it forward as true.
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- Load-bearing: passes — The paper’s conclusions depend on it.
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- Partly supported
The cited sources that could be checked couldn’t confirm or dispute this claim.
In the paper
“These features may indicate that the axoplasmic MT milieu is under the strong tension (Yu and Baas, 1994;Rochlin et al., 1996).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
What the sources say
- Could not verifycites Yu and Baas, 1994 sourceExperimental — accuracy not yet measured
The Results and Discussion describe closely spaced, parallel axonal microtubules, but do not say that the axoplasmic microtubule milieu is under strong tension. Searches for tension and mechanical stress found no passage addressing that claim; page numbers were not available in our copy. (LLM, conf=0.74)
- Could not verifycites Rochlin et al., 1996 sourceExperimental — accuracy not yet measured
The Microtubules section discusses microtubule stability and assembly kinetics, and the Results describe the shape of microtubules in growth cones. Neither passage addresses whether the axoplasmic microtubule milieu is under strong mechanical tension. Searches for tension, tensile stress, and related mechanical terms found no passage establishing that point. (LLM, conf=0.70)
hedged- Asserted: passes — The authors put it forward as true.
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- Based: passes — The paper gives a reason why it holds.
- Could not verify
The cited sources support only part of this claim — read each source’s verdict below.
In the paper
“Impairment of mitochondrial traffic is also a feature of tauopathies (Stokin et al., 2005;Lippens et al., 2007).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
What the sources say
- Not checked — no full text of the sourcecites Stokin et al., 2005 source
- Partly supportedcites Lippens et al., 2007 sourceExperimental — accuracy not yet measured
A passage labeled Abstract (page unavailable) says that tau deregulation can cause defects in axonal transport in Alzheimer’s disease and discusses transport of organelles. It does not specifically identify impaired mitochondrial traffic, so it supports the broader transport point but not the claim’s mitochondrial specificity. (LLM, conf=0.84)
plaincorrelational- Asserted: passes — The authors put it forward as true.
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Every source the paper cites for this claim was checked and supports it.
In the paper
“Tau WT overexpression increased the pausing frequency from 31.6 to 48.5% in neurons, which is almost identical to previous results (Stamer et al., 2002).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
What the sources say
- Supportedcites Stamer et al., 2002 source
The citation is offered for the comparison with previous results, not as the source of the citing authors’ 31.6% and 48.5% figures. In Results, under time-lapse imaging of transport (page unavailable), Stamer et al. report that tau expression increased the immobile fraction of mitochondria in chick retinal ganglion neurons from 20% to approximately 50%, supporting the stated similarity. (LLM, conf=0.89)
plaindirect- Asserted: passes — The authors put it forward as true.
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- Load-bearing: unclear — It is unclear whether the paper’s conclusions depend on it.
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- Supported
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“However, the greatest effects on mitochondrial translocation were induced by phosphomimetic mutations.”
- Also stated in: § Tau phosphorylation reduces mitochondrial motility in neuritic processes of PC12 cells · hedged
“Moving mitochondria in neurites overexpressing Tau 3D were significantly fewer than those in Tau WT or 3A-expressing neurites, indicating the stronger inhibitory activity of Tau 3D.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Abstract
plaindirect- Asserted: passes — The authors put it forward as true.
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- Also stated in: § Tau phosphorylation reduces mitochondrial motility in neuritic processes of PC12 cells · hedged
- It may state two separate claims as one. 30
- Probably not a substantial claim. 12
- The quote only partly states this claim. 5
The cited sources support only part of this claim — read each source’s verdict below.
In the paper
“Hyperphosphorylation of the tail domains would increase the inter-NF distances to expand the NF domain in axons (Kumar et al., 2002;Kanungo et al., 2011), giving higher pressure to the MT domain.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
What the sources say
- Partly supportedcites Kumar et al., 2002 sourceExperimental — accuracy not yet measured
The Discussion reports that increased sidearm phosphorylation expands the sidearm brush and regulates spacing between neurofilaments. It does not establish that this expands a distinct NF domain in the axon. The subsequent suggestion of higher pressure on the MT domain is not addressed by the paper and appears to be the citing authors’ inference. (LLM, conf=0.84)
- Not matchedcites Kanungo et al., 2011
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
hedgeddirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: unclear — It is unclear whether the paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
- Partly supported
The cited sources support only part of this claim — read each source’s verdict below.
In the paper
“However, hyperphosphorylation is linked to neurodegeneration with phosphorylation of more than 20 sites shown in the degenerated brains of Alzheimer's patients (Watanabe et al., 1993;Morishima-Kawashima et al., 1995;Stoothoff and Johnson, 2005).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Introduction
What the sources say
- Not checked — no full text of the sourcecites Watanabe et al., 1993 source
- Partly supportedcites Morishima-Kawashima et al., 1995 sourceExperimental — accuracy not yet measured
The opening section reports abnormal phosphorylation of PHF-tau in Alzheimer’s disease and identifies 19 sites, not more than 20. It also describes neurofibrillary tangles as closely related to neuronal loss, while the Discussion presents a link between abnormal tau phosphorylation and neuronal degeneration as a possibility rather than an established finding. (LLM, conf=0.90)
- Not matchedcites Stoothoff and Johnson, 2005
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
plaincorrelational- Asserted: passes — The authors put it forward as true.
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- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. It may state two separate claims as one.
The cited sources that could be checked couldn’t confirm or dispute this claim.
In the paper
“their detection by this antibody is commonly used as a marker of abnormal phosphorylation in brains of Alzheimer's patients.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Introduction
What the sources say
- Not checked — no full text of the sourcecites Goedert et al., 1995 source
- Could not verifycites Wang et al., 2006 sourceExperimental — accuracy not yet measured
The Abstract links Alzheimer’s disease to tau hyperphosphorylation, but it does not identify AT8 or describe its use as a marker in patients’ brains. Searches for AT8 and for antibody-based detection found no passage addressing that point. (LLM, conf=0.74)
- Not checked — no full text of the sourcecites Hanger et al., 2009 source
plaincorrelational- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. The paper’s conclusions may not depend on it.
The cited sources support only part of this claim — read each source’s verdict below.
In the paper
“Phosphorylation at these sites may extend the projection domain outwards from the surface of MTs (Jeganathan et al., 2008) and affect mitochondrial transport (Mukhopadhyay and Hoh, 2001;Jeganathan et al., 2008;Shahpasand et al., 2008).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Introduction
What the sources say
- Partly supportedcites Jeganathan et al., 2008 sourceExperimental — accuracy not yet measured
The Results passage (Fig. 2C–D; page unavailable) reports that an AT8 phosphorylation mimic makes tau’s N-terminal domain swing away from its C-terminal domain. The introductory passage says the N-terminal domain projects away from the microtubule surface, but the study does not show that AT8 phosphorylation extends it farther from that surface. It discusses microtubule-based organelle transport generally, not an effect on mitochondrial transport. (LLM, conf=0.82)
- Partly supportedcites Mukhopadhyay and Hoh, 2001 sourceExperimental — accuracy not yet measured
The citation to Mukhopadhyay and Hoh is attached to the mitochondrial-transport clause. In Results and discussion (page unavailable), the paper says MAPs may regulate motor-protein interactions and reports that tau affects motor attachment and detachment, but not transport speed. It does not address mitochondrial transport or link phosphorylation at AT8 sites to a transport effect. (LLM, conf=0.82)
- Not checked — no full text of the sourcecites Shahpasand et al., 2008 source
hedgedconditional- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
- Partly supported
The cited sources support only part of this claim — read each source’s verdict below.
In the paper
“The AT8 sites are not only physiological phosphorylation sites (Kimura et al., 2007;Verwer et al., 2007) but also markers of hyperphosphorylation in Alzheimer's disease (Plattner et al., 2006).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
What the sources say
- Partly supportedcites Kimura et al., 2007 sourceExperimental — accuracy not yet measured
The Results section (page unavailable) reports AT8 phosphorylation in both adult and aged mice expressing wild-type human tau, without an age-related increase. This supports the narrower point that AT8 phosphorylation can occur without age-related hyperphosphorylation, but the study does not establish that the sites are physiological in normal animals; it also identifies the AT8 sites as Ser202 and Ser205, not Ser199/Ser202/Thr205. The Alzheimer's disease marker claim is attributed to Plattner et al., not Kimura et al., in the citing sentence. (LLM, conf=0.83)
- Not checked — no full text of the sourcecites Verwer et al., 2007 source
- Supportedcites Plattner et al., 2006 source
The citation to Plattner et al. supports the disease-marker part of the sentence, not the physiological-phosphorylation part, which cites other papers. The Abstract identifies Ser-202/Thr-205 (AT8) as a pathological phosphosite among those aberrantly hyperphosphorylated in tauopathies including Alzheimer disease. The paper identifies AT8 as Ser-202/Thr-205; it does not include Ser-199 in that designation. (LLM, conf=0.91)
plaincorrelational- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
- Partly supported
The cited sources support only part of this claim — read each source’s verdict below.
In the paper
“The AT8 sites are physiological sites for phosphorylation, but they are not always phosphorylated (Kimura et al., 2007;Verwer et al., 2007).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
What the sources say
- Partly supportedcites Kimura et al., 2007 sourceExperimental — accuracy not yet measured
The section on PHF1-site phosphorylation identifies AT8 as recognizing tau phosphorylated at Ser202 and Ser205, and reports AT8 immunoreactivity in the studied mice. The Discussion says AT8-site phosphorylation did not increase with aging in those mice, but it does not establish that phosphorylation at these sites is physiological or that the sites are sometimes unphosphorylated. (LLM, conf=0.78)
- Not checked — no full text of the sourcecites Verwer et al., 2007 source
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
- Partly supported
The cited sources support only part of this claim — read each source’s verdict below.
In the paper
“The C-terminal tail domains of neurofilament M and H subunits extrude outward from core filaments, as does the projection domain of Tau, to make spaces between neurofilaments (NFs) (Hisanaga and Hirokawa, 1989).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
What the sources say
- Partly supportedcites Hisanaga and Hirokawa, 1989 sourceExperimental — accuracy not yet measured
The section “Structure of the projections of control and dephosphorylated NFs” (page unavailable) describes projections extending from NF core filaments, and the Discussion describes cross-bridges between NFs that seem to comprise NF-H and NF-M tail domains. The copy does not discuss Tau’s projection domain or establish that these projections create the spaces between neurofilaments. (LLM, conf=0.86)
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
- Partly supported
The cited sources support only part of this claim — read each source’s verdict below.
In the paper
“When Tau is overexpressed in cortical neurons, tubulin synthesis is upregulated and MTs become more numerous and densely packed, resulting in inhibition of mitochondrial movement.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
What the sources say
- Partly supportedcites Thies and Mandelkow, 2007 sourceExperimental — accuracy not yet measured
The Microtubule bundling section reports increased tubulin production and denser, more numerous microtubules after tau transfection; the mitochondrial-movement section reports strongly inhibited movement. However, Materials and Methods identifies the cells as hippocampal, not cortical, neurons, and the Discussion describes increased microtubule density and bundling as a possible contributor to the transport defect rather than its established sole cause. Page numbers were not available in our copy. (LLM, conf=0.90)
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
- Partly supported
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Phosphorylated Tau WT was immunoreactive to AT8, whereas phosphorylated Tau 3A and 3D were not (Fig. 1 B)”
- Also stated in: § Phosphorylation of Tau mutants and their binding to MTs · boosted
“Immunodetection of Tau WT but not 3A nor 3D clearly demonstrated that Tau WT was phosphorylated at the AT8 recognition sites in COS-7 cells (Fig. 1C, middle).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Phosphorylation of Tau mutants and their binding to MTs
boosted- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
- Also stated in: § Phosphorylation of Tau mutants and their binding to MTs · boosted
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“The ratio of stationary phase was 23.0% in control PC12 cells but 47.6% in cells expressing Tau WT and 44.1% for 3A; for 3D, however, the percentage was higher still, 61.3% (Fig. 4B).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Tau phosphorylation reduces mitochondrial motility in neuritic processes of PC12 cells
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Expression levels were almost similar among Tau WT, 3A, and 3D constructs (Fig. 3 B, C).”
- Also stated in: § Expression of Tau constructs in PC12 cells and cultured cortical neurons · plain
“When 2.5 g of plasmids were used, the fluorescent intensities were ϳ1.7 and ϳ1.5 fold of untransfected PC12 cells (Fig. 3B) and cultured neurons (Fig. 3C), respectively.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Expression of Tau constructs in PC12 cells and cultured cortical neurons
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
The quote only partly states this claim.
- Also stated in: § Expression of Tau constructs in PC12 cells and cultured cortical neurons · plain
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“The inter-MT distance was the same (15-25 nm) in MT bundles formed by Tau WT, 3A, and 3D in Sf9 cell processes, but it was expanded to 35-45 nm in processes expressing Tau 3D when actin filaments were disrupted by latrunculin B.”
- Also stated in: § Discussion · plain
“The mean distance was 15.7 Ϯ 2.2 nm for Tau WT (n ϭ 30), 17.5 Ϯ 2.7 nm for Tau 3A (n ϭ 27), and 16.3 Ϯ 2.2 nm for Tau 3D (n ϭ 28).”
- Also stated in: § Discussion · plain
“The mean distance was 26.8 Ϯ 2.7 nm for Tau WT (n ϭ 60), 27.2 Ϯ 2.0 nm for Tau 3A (n ϭ 80), and 37.1 Ϯ 2.3 nm for Tau 3D (n ϭ 75).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
plaindirect- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
- Also stated in: § Discussion · plain
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“However, the ratio of mitochondria moving anterogradely and retrogradely was not different among three Tau constructs, indicating that phosphorylation at the AT8 sites does not affect the direction of mitochondrial movements.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Tau phosphorylation reduces mitochondrial motility in neuritic processes of PC12 cells
hedged- Asserted: passes — The authors put it forward as true.
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The quote only partly states this claim.
In the paper
“The duration of stationary phase was 31.6% in control neurons, which was higher than that observed in PC12 cells, consistent with a previous report (Morel et al., 2010).A significant increase in stationary phase was observed after transfection with Tau WT (48.5%) or 3A (46.6%); however, a higher stationary state (64.4%) was caused by Tau 3D (Fig. 5B).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Tau phosphorylation reduces mitochondrial motility in neuritic processes of PC12 cells
What the sources say
- Not checked — no full text of the sourcecites Morel et al., 2010 source
plain- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“The mean distance was 11.7 Ϯ 1.7 nm for Tau WT (n ϭ 48), 11.8 Ϯ 2.1 nm for Tau 3A (n ϭ 51), and 11.9 Ϯ 1.6 nm for Tau 3D (n ϭ 69).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
plain- Asserted: passes — The authors put it forward as true.
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A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“While transfection with less than 2 g did not significantly affect mitochondrial movement, more than 3 g had a substantial (and similar) effect for all Tau constructs (data not shown).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Expression of Tau constructs in PC12 cells and cultured cortical neurons
plaindirect- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“The ratio was significantly different between control and Tau-overexpressing neurons (p Ͻ 0.01) but was not different between three Tau constructs(pϭ0.55).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
plain- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“We observed here that Tau overexpression increased the number of MTs and reduced the inter-MT spaces in neurites of PC12 cells.”
- Also stated in: § Discussion · plain
“The mean distance was 45.1 Ϯ 2.2 (n ϭ 54) for control PC12 cells and 33.1 Ϯ 2.4 nm (n ϭ 49), 34.1 Ϯ 2.6 nm (n ϭ 44), and 34.19 Ϯ 2.8 nm (n ϭ 62) for PC12 cells overexpressing Tau WT, 3A, and 3D, respectively.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
plaindirect- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
- Also stated in: § Discussion · plain
The paper states this without a source or data behind it here, so there is nothing to check it against. The quote shows it is in the paper.
In the paper
“Because Tau 3A and 3D have similar phosphorylation profiles at other sites”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
plain- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim. The paper may give no reason why it holds.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“The mean distance was 45.1 Ϯ 2.2 (n ϭ 54) for control PC12 cells and 33.1 Ϯ 2.4 nm (n ϭ 49), 34.1 Ϯ 2.6 nm (n ϭ 44), and 34.19 Ϯ 2.8 nm (n ϭ 62) for PC12 cells overexpressing Tau WT, 3A, and 3D, respectively.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
plain- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“The inter-MT distances were greater in Tau 3Doverexpressing cells compared to those overexpressing WT or 3A (Fig. 7L).”
- Also stated in: § The phosphorylation mimic Tau 3D increases MT spacing in processes of Sf9 cells · plain
“that range was 35-45 nm in Tau 3D-expressing cells (mean distance ϭ 37.1 Ϯ 2.3 nm)”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > The phosphorylation mimic Tau 3D increases MT spacing in processes of Sf9 cells
plaincorrelational- Asserted: passes — The authors put it forward as true.
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The quote only partly states this claim.
- Also stated in: § The phosphorylation mimic Tau 3D increases MT spacing in processes of Sf9 cells · plain
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Tau overexpression also reduced the velocity of mitochondria in axons.”
- Also stated in: § Tau phosphorylation reduces mitochondrial motility in neuritic processes of PC12 cells · plain
“The mean anterograde and retrograde velocities were 0.55 Ϯ 0.08 and 0.45 Ϯ 0.03 m/s, respectively, in control cells, but they were reduced to 0.17 Ϯ 0.03 and 0.18 Ϯ 0.06 m/s in Tau WT-overexpressing neurons, 0.18 Ϯ 0.03 and 0.19 Ϯ 0.07 m/s in Tau 3A-overexpressing neurons, and 0.18 Ϯ 0.03 and 0.18 Ϯ 0.04 m/s in Tau 3Doverexpressing neurons.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Tau phosphorylation reduces mitochondrial motility in neuritic processes of PC12 cells
plaindirect- Asserted: passes — The authors put it forward as true.
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The quote only partly states this claim.
- Also stated in: § Tau phosphorylation reduces mitochondrial motility in neuritic processes of PC12 cells · plain
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Velocities faster than 1 m/s, which accounted for 15 and 11% of anterograde and retrograde movements, respectively, in control neurons, were not observed in any Tau-overexpressing neurons.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Tau phosphorylation reduces mitochondrial motility in neuritic processes of PC12 cells
plain- Asserted: fails — The authors may not put it forward as true.
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Probably not a substantial claim. The authors may not put it forward as true. The paper’s conclusions may not depend on it. The quote only partly states this claim.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“The distances were typically Ͻ10 nm in the MT pellets polymerized with Tau WT, 3A, and 3D (Fig. 7D), indicating that the phosphorylationmimicking mutation at Ser199/Ser202/Thr205 did not affect the inter-MT spacing in pelleted MTs.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > The phosphorylation mimic Tau 3D increases MT spacing in processes of Sf9 cells
hedged- Asserted: passes — The authors put it forward as true.
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- Load-bearing: passes — The paper’s conclusions depend on it.
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It may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“The mean distance was 15.7 Ϯ 2.2 nm for Tau WT (n ϭ 30), 17.5 Ϯ 2.7 nm for Tau 3A (n ϭ 27), and 16.3 Ϯ 2.2 nm for Tau 3D (n ϭ 28).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
plain- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Phosphorylated Tau 3A and 3D had similar, but not identical, banding patterns, suggesting that these mutants underwent similar phosphorylation at other sites (Fig. 1 D).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Phosphorylation of Tau mutants and their binding to MTs
hedgedcorrelational- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
The paper states this without a source or data behind it here, so there is nothing to check it against. The quote shows it is in the paper.
In the paper
“As a whole, the decreased mobility of Tau WT compared to Tau 3A indicated the higher level of phosphorylation of Tau WT, including the AT8 site.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Phosphorylation of Tau mutants and their binding to MTs
hedgedcorrelational- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“The ratio was significantly different between control and Tau-overexpressing PC12 cells (*p Ͻ 0.01), but was not significant between three Tau constructs ( p ϭ 0.75).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
plain- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“The mean distance was 26.8 Ϯ 2.7 nm for Tau WT (n ϭ 60), 27.2 Ϯ 2.0 nm for Tau 3A (n ϭ 80), and 37.1 Ϯ 2.3 nm for Tau 3D (n ϭ 75).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
plain- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Thus, Tau phosphorylation at the AT8 sites may have meaningful effects on mitochondrial movement, likely by controlling microtubule spacing.”
- Also stated in: § Discussion · hedged
“we would like to propose that phosphorylation of Tau at the AT8 sites affects the transport of mitochondria along MTs by changing the inter-MT spaces.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Abstract
hedgedconditional- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
- Rests on an assumption: Increased inter-microtubule spacing impairs mitochondrial transport.
- Also stated in: § Discussion · hedged
A claim is checked only against the cited paper’s full text, never its abstract, and none is available for its sources.
In the paper
“AT8, which recognizes Tau that is phosphorylated at Ser202 and Thr205 (Goedert et al., 1995) or Ser199, Ser202, and Thr205 (Hanger et al., 2009).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Phosphorylation of Tau mutants and their binding to MTs
What the sources say
plain- Asserted: passes — The authors put it forward as true.
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- Load-bearing: passes — The paper’s conclusions depend on it.
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It may state two separate claims as one.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Increased repulsive forces between MTs would generate a stronger reactive resistance against mitochondria moving inside MT bundles.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
hedgeddirect- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim.
A claim is checked only against the cited paper’s full text, never its abstract, and none is available for its sources.
In the paper
“Phosphorylation at these sites reduces, but does not abolish, Tau binding to MTs, leading to more dynamic MTs (Wada et al., 1998;Liu et al., 2007).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
What the sources say
plaindirect- Asserted: passes — The authors put it forward as true.
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- Load-bearing: passes — The paper’s conclusions depend on it.
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It may state two separate claims as one.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“This would suppress mitochondrial transport along MTs by restricting radial displacement of MTs.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
hedgeddirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. The paper’s conclusions may not depend on it.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“The force produced by outward extension of the projection domain may not be strong enough to push surrounding MTs against the membrane, which may explain why phosphorylation-induced expansion of the inter-MT distance has not been reported.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
hedgedconditional- Asserted: passes — The authors put it forward as true.
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- Load-bearing: passes — The paper’s conclusions depend on it.
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Probably not a substantial claim. It may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“AT8 reactivity has been frequently used as an indicator of hyperphosphorylation of Tau in AD brains or other tauopathies (Stoothoff and Johnson, 2005;Hanger et al., 2009).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
What the sources say
- Not matchedcites Stoothoff and Johnson, 2005
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- Not checked — no full text of the sourcecites Hanger et al., 2009 source
plaincorrelational- Asserted: passes — The authors put it forward as true.
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- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. The paper’s conclusions may not depend on it.
- Not matched
What the paper did — it cites no source for this, so there is none to check. The quote shows it is in the paper.
In the paper
“All experiments were performed at least three times, and representative results are shown.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > SDS-PAGE and immunoblotting.
plain- Asserted: passes — The authors put it forward as true.
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- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. The paper’s conclusions may not depend on it.
In the paper
“According to the paperclip structural model of Tau (Jeganathan et al., 2006), the site near Ser199/Ser202/Thr205 folds and the N-terminal region is situated close to the MT-binding repeats.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
What the sources say
- Not checked — no full text of the sourcecites Jeganathan et al., 2006 source
plain- Asserted: passes — The authors put it forward as true.
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- Load-bearing: fails — The paper’s conclusions may not depend on it.
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Probably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
In the paper
“Tau impairs mitochondrial movement by inhibiting the interaction of kinesin with MTs (Hagiwara et al., 1994).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Tau phosphorylation reduces mitochondrial motility in neuritic processes of PC12 cells
What the sources say
- Not checked — no full text of the sourcecites Hagiwara et al., 1994 source
plaindirect- Asserted: fails — The authors may not put it forward as true.
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- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: fails — The paper may give no reason why it holds.
Probably not a substantial claim. The authors may not put it forward as true. The paper’s conclusions may not depend on it. The paper may give no reason why it holds.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Thus, our results suggest that the increased phosphorylation of the AT8 sites in brains of Alzheimer's patients decreases mitochondrial transport in axons, leading to axonal degeneration.”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
hedgeddirect- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“Tau is also a phosphoprotein, the functions of which can be regulated by phosphorylation (Stoothoff and Johnson, 2005;Hanger et al., 2009).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Introduction
What the sources say
- Not matchedcites Stoothoff and Johnson, 2005
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- Not checked — no full text of the sourcecites Hanger et al., 2009 source
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. It may state two separate claims as one.
- Not matched
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Phosphorylation of Tau at the AT8 sites tends to increase the inter-MT distance, but under strong tension the inter-MT distance cannot expand (Fig. 8), and instead the repulsive forces between MTs increase (Fig. 9).”
§ Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease > Discussion
plainconditional- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
The paper relies on this without support.
Findings from cultured cells and overexpression of Tau mutants generalize to Alzheimer's disease pathophysiology.
“Hyperphosphorylation of the AT8 sites may contribute to axonal degeneration by disrupting mitochondrial transport in Alzheimer's disease.”
The paper relies on this without support.
Disrupted mitochondrial transport causes axonal degeneration.
“Hyperphosphorylation of the AT8 sites may contribute to axonal degeneration by disrupting mitochondrial transport in Alzheimer's disease.”
The paper relies on this without support.
Increased inter-microtubule spacing impairs mitochondrial transport.
“we would like to propose that phosphorylation of Tau at the AT8 sites affects the transport of mitochondria along MTs by changing the inter-MT spaces.”
The paper relies on this without support.
Site-specific functions of Tau phosphorylation have not been completely investigated.
“However, site-specific functions have not been completely investigated.”
The paper relies on this without support.
Actin filaments are abundant in submembranous regions, providing tension to plasma membranes.
“Actin filaments are abundant in submembranous regions, providing tension to plasma membranes.”
The paper relies on this without support.
The Ser199/Ser202/Thr205 sites are present in the border between the N-terminal projection region and the MT-binding region.
“The Ser199/Ser202/Thr205 sites are present in the border between the N-terminal projection region and the MT-binding region.”
Citations
Cites
The axonal transport of mitochondria
Saxton, W. M., & Hollenbeck, P. J. (2012) · Journal of Cell Science · doi:10.1242/jcs.053850 · Cited by 1,218
Axonopathy and Transport Deficits Early in the Pathogenesis of Alzheimer’s Disease
Stokin, G. B., Lillo, C., Falzone, T. L., Brusch, R. G., Rockenstein, E., Mount, S. L., Raman, R., Davies, P., Masliah, E., Williams, D. S., et al. (2005) · Science · doi:10.1126/science.1105681 · Cited by 1,214
Phosphate-binding Tag, a New Tool to Visualize Phosphorylated Proteins
Kinoshita, E., Kinoshita‐Kikuta, E., Takiyama, K., & Koike, T. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t500024-mcp200 · Cited by 1,112
Differential Regulation of Dynein and Kinesin Motor Proteins by Tau
Dixit, R., Ross, J. L., Goldman, Y. E., & Holzbaur, E. L. F. (2008) · Science · doi:10.1126/science.1152993 · Cited by 1,012
Tau phosphorylation: the therapeutic challenge for neurodegenerative disease
Hanger, D. P., Anderton, B. H., & Noble, W. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.01.003 · Cited by 965
Stamer, K., Vogel, R., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200108057 · Cited by 885
Ebneth, A., Godemann, R., Stamer, K., Illenberger, S., Trinczek, B., Mandelkow, E.-M., & Mandelkow, E. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.3.777 · Cited by 820
The axonal transport of mitochondria
Hollenbeck, P. J., & Saxton, W. M. (2005) · Journal of Cell Science · doi:10.1242/jcs.02745 · Cited by 771
Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205
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Metadata
- Authors
- Shahpasand, K., Uemura, I., Saito, T., Asano, T., Hata, K., Shibata, K., Toyoshima, Y., Hasegawa, M., & Hisanaga, S.-I.
- Affiliations
- Tokyo Metropolitan University (JP)
- The University of Tokyo (JP)
- Tokyo Metropolitan Institute of Medical Science (JP)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2012-02-14
- Volume
- 32
- Issue
- 7
- Pages
- 2430-2441
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6621814
- OpenAlex
- W2075421841
- Semantic Scholar
- a4791d1257573d035e515b969027264b27c9b2a9
- Cited by
- 206
- References
- 67
- Citations by year
- 2026: 10 · 2025: 16 · 2024: 11 · 2023: 18 · 2022: 15 · 2021: 23 · 2020: 16 · 2019: 10 · 2018: 12 · 2017: 9 · 2016: 15 · 2015: 15 · 2014: 16 · 2013: 12 · 2012: 8
- FWCI
- 10.94
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology
- Japan Society for the Promotion of Science (23240050)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- tau phosphorylation, Alzheimer's disease, mitochondrial transport, neurofibrillary tangles, axonal degeneration, phosphomimetic mutations, PC12 cells, cortical neurons, axonal mitochondria
- MeSH terms
- Alanine, Alzheimer Disease, Animals, Aspartic Acid, Biological Transport, Cells, Cultured, Chlorocebus aethiops, Female, Humans, Male, Microtubules, Mitochondria, Mutation, Phosphorylation, Protein Binding, PC12 Cells, tau Proteins, COS Cells, Mice, Rats
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