Phototropin Blue-Light Receptors

Christie, John M.

doi:10.1146/annurev.arplant.58.032806.103951

Cited by 937Light effects on plantsPlant Molecular Biology ResearchPhotoreceptor and optogenetics research

Phototropin Blue-Light Receptors

Christie, John M.·2007·Annual Review of Plant Biology

DOI 10.1146/annurev.arplant.58.032806.103951

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Abstract

Phototropins are blue-light receptors controlling a range of responses that serve to optimize the photosynthetic efficiency of plants. These include phototropism, light-induced stomatal opening, and chloroplast movements in response to changes in light intensity. Since the isolation of the Arabidopsis PHOT1 gene in 1997, phototropins have been identified in ferns and mosses where their physiological functions appear to be conserved. Arabidopsis contains two phototropins, phot1 and phot2, that exhibit overlapping functions in addition to having unique physiological roles. Phototropins are light-activated serine/threonine protein kinases. Light sensing by the phototropins is mediated by a repeated motif at the N-terminal region of the protein known as the LOV domain. Photoexcitation of the LOV domain results in receptor autophosphorylation and an initiation of phototropin signaling. Here we summarize the photochemical and biochemical events underlying phototropin activation in addition to the current knowledge of the molecular mechanisms associated with photoreceptor signaling.

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Phototropins are composed of approximately 1000 amino acids and two FMN domains, with an N-terminus containing two repeating conserved sequences LOV1 and LOV2, and a C-terminus STK domain that interconnects with LOV2.
“Phototropins are composed of approximately 1000 amino acids and two flavin mononucleotides (FMN) domain, and their N-terminus contains two repeating conserved sequences, LOV1 and LOV2. The C-terminus of phototropin is a serine/threonine kinase domain (STK) that interconnects with LOV2 (Christie, 2007; Okajima, 2016).”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Christie, 2007
Phototropins (PHOT1 and PHOT2) act as photoreceptors in plants and respond to environmental conditions by regulating phototropism, chloroplast movement, stomatal opening and leaf extension.
“Phototropins (PHOT1 and PHOT2) act as photoreceptors in plants and respond to environmental conditions by regulating phototropism, chloroplast movement, stomatal opening and leaf extension (Christie, 2007).”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Christie, 2007
The chloroplast accumulation response ensures efficient photosynthesis and biomass production under a wide range of light intensities.
“ensuring efficient photosynthesis and biomass production under a wide range of light intensities”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Christie, 2007
Chloroplasts travel toward low-fluence blue light and aggregate along the oblique perimeter wall, which is the accumulation response.
“chloroplasts travel toward low-fluence blue light and aggregate along the oblique perimeter wall (accumulation response)”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Christie, 2007
Blue light is the primary light that induces chloroplast movement to optimize light uptake.
“Blue light is the primary light that induces chloroplast movement to optimize light uptake”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Christie, 2007

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Mutations of Arabidopsis in Potential Transduction and Response Components of the Phototropic Signaling Pathway
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Protein phosphatase 1 positively regulates stomatal opening in response to blue light in Vicia faba
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Phototropins Mediate Blue and Red Light-Induced Chloroplast Movements in Physcomitrella patens
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The Phycomyces madA gene encodes a blue-light photoreceptor for phototropism and other light responses
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Light-mediated changes in two proteins found associated with plasma membrane fractions from pea stem sections
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Blue Light-Induced Chloroplast Relocation in Arabidopsis thaliana as Analyzed by Microbeam Irradiation
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The Rice COLEOPTILE PHOTOTROPISM1 Gene Encoding an Ortholog of Arabidopsis NPH3 Is Required for Phototropism of Coleoptiles and Lateral Translocation of Auxin
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Function Analysis of Phototropin2 using Fern Mutants Deficient in Blue Light-Induced Chloroplast Avoidance Movement
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Analysis of the Phosphorylation Level in Guard-Cell Plasma Membrane H+-ATPase in Response to Fusicoccin
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Dimerization of the plant photoreceptor phototropin is probably mediated by the LOV1 domain
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Biochemical Evidence for the Requirement of 14-3-3 Protein Binding in Activation of the Guard-cell Plasma Membrane H+-ATPase by Blue Light
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Blue light-induced kinetics of H + and Ca 2+ fluxes in etiolated wild-type and phototropin-mutant Arabidopsis seedlings
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Vibration Spectroscopy Reveals Light-Induced Chromophore and Protein Structural Changes in the LOV2 Domain of the Plant Blue-Light Receptor Phototropin 1
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Conformational Dynamics of Phototropin 2 LOV2 Domain with the Linker upon Photoexcitation
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A Plant-Specific Protein Essential for Blue-Light-Induced Chloroplast Movements
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Characterization of a Rapid, Blue Light-Mediated Change in Detectable Phosphorylation of a Plasma Membrane Protein from Etiolated Pea (Pisum sativum L.) Seedlings
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Vibrational Spectroscopy of an Algal Phot-LOV1 Domain Probes the Molecular Changes Associated with Blue-Light Reception
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The LOV2 Domain of Phototropin: A Reversible Photochromic Switch
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A Role for LKP2 in the Circadian Clock of Arabidopsis
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The bacterial counterparts of plant phototropins
Losi, A. (2004) · Photochemical & Photobiological Sciences · doi:10.1039/b400728j · Cited by 97 · see citing works
Light-Induced Structural Changes of LOV Domain-Containing Polypeptides from Arabidopsis Phototropin 1 and 2 Studied by Small-Angle X-ray Scattering
Nakasako, M., Iwata, T., Matsuoka, D., & Tokutomi, S. (2004) · Biochemistry · doi:10.1021/bi0485530 · Cited by 96 · see citing works
14‐3‐3 proteins: regulation of signal‐induced events
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Listening to the blue: the time-resolved thermodynamics of the bacterial blue-light receptor YtvA and its isolated LOV domain
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Primary Inhibition of Hypocotyl Growth and Phototropism Depend Differently on Phototropin-Mediated Increases in Cytoplasmic Calcium Induced by Blue Light
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Phototropins: A New Family of Flavin-Binding Blue Light Receptors in Plants
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LKP1 (LOV kelch protein 1): a factor involved in the regulation of flowering time in Arabidopsis
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Isolation and characterization of a Chlamydomonas gene that encodes a putative blue‐light photoreceptor of the phototropin family
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Light-Induced Structural Changes in the LOV2 Domain of Adiantum Phytochrome3 Studied by Low-Temperature FTIR and UV−Visible Spectroscopy
Iwata, T., Nozaki, D., Tokutomi, S., Kagawa, T., Wada, M., & Kandori, H. (2003) · Biochemistry · doi:10.1021/bi0345135 · Cited by 87 · see citing works
The PAS/LOV protein VIVID supports a rapidly dampened daytime oscillator that facilitates entrainment of the Neurospora circadian clockPreprint
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Mapping of Low- and High-Fluence Autophosphorylation Sites in Phototropin 1
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Blue Light Activates a Specific Protein Kinase in Higher Plants
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The Fern Adiantum capillus-veneris Lacks Stomatal Responses to Blue Light
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Plastid Movement Impaired 2, a New Gene Involved in Normal Blue-Light-Induced Chloroplast Movements in Arabidopsis
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Phototropins and Blue Light-dependent Calcium Signaling in Higher Plants†
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Toward understanding the ecological functions of tropisms: interactions among and effects of light on tropisms
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Blue Light-Induced Phosphorylation of a Plasma Membrane-Associated Protein in Zea mays L
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Phototropin from Chlamydomonas reinhardtii is Functional in Arabidopsisthaliana
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Asymmetric, Blue Light-Dependent Phosphorylation of a 116-Kilodalton Plasma Membrane Protein Can Be Correlated with the First- and Second-Positive Phototropic Curvature of Oat Coleoptiles
Salomon, M., Zacherl, M., & Rüdiger, W. (1997) · PLANT PHYSIOLOGY · doi:10.1104/pp.115.2.485 · Cited by 55 · see citing works
Phototropins and Associated Signaling: Providing the Power of Movement in Higher Plants¶
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Rice NPH1 Homologues, OsNPH1a and OsNPH1b, Are Differently Photoregulated
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Comparative Investigation of the LOV1 and LOV2 Domains in Adiantum Phytochrome3
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Possible Involvement of Phototropins in Leaf Movement of Kidney Bean in Response to Blue Light
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Phototropin 1 is required for high-fluence blue-light-mediated mRNA destabilization
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A Pea Plasma Membrane Protein Exhibiting Blue Light-Induced Phosphorylation Retains Photosensitivity following Triton Solubilization
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Control of mammalian glycogen synthase by PAS kinase
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Chapter 23 Phototropism in higher plants
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Correlation of Blue Light-Induced Phosphorylation to Phototropism in Zea mays L
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Quaternary structure of LOV‐domain containing polypeptide of Arabidopsis FKF1 protein
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The photochemistry of the light‐, oxygen‐, and voltage‐sensitive domains in the algal blue light receptor phot
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Blue Light Induces Phosphorylation at Seryl Residues on a Pea (Pisum sativum L.) Plasma Membrane Protein
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BLUE/UV-A RECEPTORS: HISTORICAL OVERVIEW
Briggs, W. R. (2006) · Springer eBooks · doi:10.1007/1-4020-3811-9_10 · Cited by 28 · see citing works
Phototropins and Associated Signaling: Providing the Power of Movement in Higher Plants¶
Celaya, R. B., & Emmanuel Liscum, A. (2005) · Photochemistry and Photobiology · doi:10.1562/2004-08-22-ir-282.1 · Cited by 28 · see citing works
Exposure of Oat Seedlings to Blue Light Results in Amplified Phosphorylation of the Putative Photoreceptor for Phototropism and in Higher Sensitivity of the Plants to Phototropic Stimulation
Salomon, M., Zacherl, M., Luff, L., & Rudiger, W. (1997) · Plant Physiology · doi:10.1104/pp.115.2.493 · Cited by 27 · see citing works
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Isolation of a Protein Interacting with Vfphot1a in Guard Cells of Vicia faba
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Changes in blue-light-dependent protein phosphorylation during the early development of etiolated oat seedlings
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Blue Light Sensing and Signaling by the Phototropins
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Autophosphorylation, Electrophoretic Mobility and Immuno-reaction of Oat Phototropin 1 under UV and Blue Light
Knieb, E., Salomon, M., & Rüdiger, W. (2004) · Photochemistry and Photobiology · doi:10.1562/2004-04-03-ra-133.1 · Cited by 19 · see citing works
Chromophore Exchange in the LOV2 Domain of the Plant Photoreceptor Phototropin1 from Oat
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Phytochrome regulation of pea phototropin
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Photoreceptor Gene Families in Lower Plants
Suetsugu, N., & Wada, M. (2005) · doi:10.1002/352760510x.ch17 · Cited by 13 · see citing works
LOV‐Domain Photochemistry
Swartz, T. E., & Bogomolni, R. A. (2005) · doi:10.1002/352760510x.ch14 · Cited by 13 · see citing works
Properties of a blue-light-absorbing photoreceptor kinase localized in the plasma membrane of the coleoptile tip region
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Changes in Ion Fluxes During Phototropic Bending of Etiolated Oat Coleoptiles
Babourina, O. (2004) · Annals of Botany · doi:10.1093/aob/mch126 · Cited by 12 · see citing works
Plant Cryptochromes: Their Genes, Biochemistry, and Physiological Roles
Batschauer, A. (2005) · doi:10.1002/352760510x.ch10 · Cited by 11 · see citing works
The ZEITLUPE Family of Putative Photoreceptors
Schultz, T. F. (2005) · doi:10.1002/352760510x.ch16 · Cited by 8 · see citing works
LOV‐Domain Structure, Dynamics, and Diversity
Crosson, S. (2005) · doi:10.1002/352760510x.ch15 · Cited by 5 · see citing works
PHOTOTROPINS
Briggs, W. R., Christie, J. M., & Swartz, T. E. (2006) · Springer eBooks · doi:10.1007/1-4020-3811-9_12 · Cited by 2 · see citing works
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Photoreceptor Signaling Networks in Plant Responses to Shade
Casal, J. J. (2013) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-050312-120221 · Cited by 865 · see citing works
Structure and function of plant photoreceptors
Möglich, A., Yang, X., Ayers, R. A., & Moffat, K. (2010) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042809-112259 · Cited by 499 · see citing works
Plant Flavoprotein Photoreceptors
Christie, J. M., Blackwood, L., Petersen, J., & Sullivan, S. (2015) · Plant and Cell Physiology · doi:10.1093/pcp/pcu196 · Cited by 294 · see citing works
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phot1 Inhibition of ABCB19 Primes Lateral Auxin Fluxes in the Shoot Apex Required For Phototropism
Christie, J. M., Yang, H., Richter, G. L., Sullivan, S., Thomson, C. E., Lin, J., Titapiwatanakun, B., Ennis, M., Kaiserli, E., Lee, O. R., et al. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1001076 · Cited by 245 · see citing works
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Phosphorylation of BLUS1 kinase by phototropins is a primary step in stomatal opening
Takemiya, A., Sugiyama, N., Fujimoto, H., Tsutsumi, T., Yamauchi, S., Hiyama, A., Tada, Y., Christie, J. M., & Shimazaki, K.-I. (2013) · Nature Communications · doi:10.1038/ncomms3094 · Cited by 219 · see citing works
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Phototropism: Growing towards an Understanding of Plant Movement
Liscum, E., Askinosie, S. K., Leuchtman, D. L., Morrow, J., Willenburg, K. T., & Coats, D. R. (2014) · The Plant Cell · doi:10.1105/tpc.113.119727 · Cited by 215 · see citing works
Regulation of Phototropic Signaling in Arabidopsis via Phosphorylation State Changes in the Phototropin 1-interacting Protein NPH3
Pedmale, U. V., & Liscum, E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702551200 · Cited by 169 · see citing works
Shoot phototropism in higher plants: New light through old concepts
Christie, J. M., & Murphy, A. S. (2013) · American Journal of Botany · doi:10.3732/ajb.1200340 · Cited by 152 · see citing works
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Chloroplast Accumulation Response Enhances Leaf Photosynthesis and Plant Biomass Production
Gotoh, E., Suetsugu, N., Yamori, W., Ishishita, K., Kiyabu, R., Fukuda, M., Higa, T., Shirouchi, B., & Wada, M. (2018) · Plant Physiology · doi:10.1104/pp.18.00484 · Cited by 128 · see citing works
Chloroplast photorelocation movement mediated by phototropin family proteins in green plants
Suetsugu, N., & Wada, M. (2007) · bchm · doi:10.1515/bc.2007.118 · Cited by 123 · see citing works
In Vivo Phosphorylation Site Mapping and Functional Characterization of Arabidopsis Phototropin 1
Sullivan, S., Thomson, C. E., Lamont, D. J., Jones, M. A., & Christie, J. M. (2008) · Molecular Plant · doi:10.1093/mp/ssm017 · Cited by 107 · see citing works
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Phototropism: at the crossroads of light-signaling pathways
Goyal, A., Szarzynska, B., & Fankhauser, C. (2013) · Trends in Plant Science · doi:10.1016/j.tplants.2013.03.002 · Cited by 109 · see citing works
The Subcellular Localization and Blue-Light-Induced Movement of Phototropin 1-GFP in Etiolated Seedlings of Arabidopsis thalianaw
Wan, Y.-L., Eisinger, W., Ehrhardt, D., Kubitscheck, U., Baluska, F., & Briggs, W. (2008) · Molecular Plant · doi:10.1093/mp/ssm011 · Cited by 105 · see citing works
Phytochrome Kinase Substrate 4 is phosphorylated by the phototropin 1 photoreceptor
Demarsy, E., Schepens, I., Okajima, K., Hersch, M., Bergmann, S., Christie, J., Shimazaki, K., Tokutomi, S., & Fankhauser, C. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.186 · Cited by 94 · see citing works
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Dynamics and mechanisms of DNA repair by photolyase
Liu, Z., Wang, L., & Zhong, D. (2015) · Physical Chemistry Chemical Physics · doi:10.1039/c4cp05286b · Cited by 86 · see citing works
Phototropins Function in High-Intensity Blue Light-Induced Hypocotyl Phototropism in Arabidopsis by Altering Cytosolic Calcium
Zhao, X., Wang, Y.-L., Qiao, X.-R., Wang, J., Wang, L.-D., Xu, C.-S., & Zhang, X. (2013) · Plant Physiology · doi:10.1104/pp.113.216556 · Cited by 84 · see citing works
Role of the phytochrome and cryptochrome signaling pathways in hypocotyl phototropism: Role of phy and cry in phototropism
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Arabidopsis ROOT PHOTOTROPISM2 Is a Light-Dependent Dynamic Modulator of Phototropin1
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“Phototropins are composed of approximately 1000 amino acids and two flavin mononucleotides (FMN) domain, and their N-terminus contains two repeating conserved sequences, LOV1 and LOV2.”
BackgroundInfluential
Two Coiled-Coil Proteins, WEB1 and PMI2, Suppress the Signaling Pathway of Chloroplast Accumulation Response that Is Mediated by Two Phototropin-Interacting Proteins, RPT2 and NCH1, in Seed Plants
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Authors: Christie, J. M.
Affiliations: University of Glasgow (GB)
Corresponding author: Christie, John M.
ORCID: Christie, John M.
Venue: Annual Review of Plant Biology
Publisher: Annual Reviews
Published: 2007-06-01
Volume: 58
Issue: 1
Pages: 21-45
ISSN: 1543-5008 (ISSN-L)
1545-2123
DOI: 10.1146/annurev.arplant.58.032806.103951
OpenAlex: W2121122292
Cited by: 937
References: 165
Citations by year: 2026: 42 · 2025: 54 · 2024: 51 · 2023: 42 · 2022: 50 · 2021: 45 · 2020: 80 · 2019: 69 · 2018: 52 · 2017: 39 · 2016: 40 · 2015: 41 · 2014: 49 · 2013: 55 · 2012: 59
FWCI: 2.05
Type: journal article
Language: en
Open access: closed
Locations: Annual Review of Plant Biology (publishedVersion)
PubMed (publishedVersion)
ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
Funders: Biotechnology and Biological Sciences Research Council (BB/C000366/1)
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 › Neuroscience › Cellular and Molecular Neuroscience › Photoreceptor and optogenetics research
Keywords: phototropin, blue light receptor, phototropism, stomatal opening, chloroplast movement, LOV domain, ferns, bryophytes, plant photoreceptors
MeSH terms: Calcium, Chloroplasts, Models, Molecular, Phosphorylation, Plant Proteins, Plants, Signal Transduction, Protein Serine-Threonine Kinases, Protein Structure, Tertiary, Phototropism, Hypocotyl, Photosynthetic Reaction Center Complex Proteins, Plant Development

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