Phototropins Function in High-Intensity Blue Light-Induced Hypocotyl Phototropism in Arabidopsis by Altering Cytosolic Calcium
Open accessAbstract
Phototropins (phot1 and phot2), the blue light receptors in plants, regulate hypocotyl phototropism in a fluence-dependent manner. Especially under high fluence rates of blue light (HBL), the redundant function mediated by both phot1 and phot2 drastically restricts the understanding of the roles of phot2. Here, systematic analysis of phototropin-related mutants and overexpression transgenic lines revealed that HBL specifically induced a transient increase in cytosolic Ca2+ concentration ([Ca2+]cyt) in Arabidopsis (Arabidopsis thaliana) hypocotyls and that the increase in [Ca2+]cyt was primarily attributed to phot2. Pharmacological and genetic experiments illustrated that HBL-induced Ca2+ increases were modulated differently by phot1 and phot2. Phot2 mediated the HBL-induced increase in [Ca2+]cyt mainly by an inner store-dependent Ca2+-release pathway, not by activating plasma membrane Ca2+ channels. Further analysis showed that the increase in [Ca2+]cyt was possibly responsible for HBL-induced hypocotyl phototropism. An inhibitor of auxin efflux carrier exhibited significant inhibitions of both phototropism and increases in [Ca2+]cyt, which indicates that polar auxin transport is possibly involved in HBL-induced responses. Moreover, PHYTOCHROME KINASE SUBSTRATE1 (PKS1), the phototropin-related signaling element identified, interacted physically with phototropins, auxin efflux carrier PIN-FORMED1 and calcium-binding protein CALMODULIN4, in vitro and in vivo, respectively, and HBL-induced phototropism was impaired in pks multiple mutants, indicating the role of the PKS family in HBL-induced phototropism. Together, these results provide new insights into the functions of phototropins and highlight a potential integration point through which Ca2+ signaling-related HBL modulates hypocotyl phototropic responses.
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Although NPH3 and RPT2 are involved in PHOT2-mediated phototropism under high-fluence blue light, RPT2 does not interact with PHOT2 in vivo.
“Although NPH3 and RPT2 are involved in PHOT2-mediated phototropism under high-fluence blue light, RPT2 does not interact with PHOT2 in vivo, and the regulatory mechanism remains unclear (Sakai et al., 2000; Lariguet et al., 2006; Zhao et al., 2013; Zhu et al., 2021a).”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Zhao et al., 2013
The passage labeled Abstract (page unavailable) explicitly says that RPT2 does not act in the phot2-mediated pathway, contrary to the claim that RPT2 is involved in it. The BiFC Assay passage (page unavailable) reports other protein-interaction tests, not an in vivo test of RPT2–PHOT2 interaction. (LLM, conf=0.88)
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredPHOT1 and PHOT2 can mediate the influx of Ca2+ under high- and low-fluence blue light, respectively.
“PHOT1 and PHOT2 can mediate the influx of Ca2+ under high- and low-fluence blue light, respectively (Babourina et al., 2002; Zhao et al., 2013).”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Zhao et al., 2013
The paper states that under low-fluence blue light, phot1 alone mediates Ca2+ influx—not phot2 (passage [2], page not provided). In its high-intensity experiments, phot1 activates plasma-membrane Ca2+ channels, while phot2 acts mainly through release from internal stores (passages [1] and [3], page not provided). The claimed assignment of receptors to light intensities and influx mechanisms is therefore contrary to the source. (LLM, conf=0.89)
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredUnder high-fluence blue light, the hypocotyl axis of a phot1 mutant was bent toward light but the NPH3 protein was not phosphorylated, indicating that PHOT2 does not require phosphorylation of NPH3 to mediate phototropism in Arabidopsis.
“The study showed that under high-fluence blue light, the hypocotyl axis of a phot1 mutant was bent toward light but the NPH3 protein was not phosphorylated, indicating that PHOT2 does not require phosphorylation of NPH3 to mediate phototropism in Arabidopsis (Tsuchida-Mayama et al., 2008; Zhao et al., 2013).”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Zhao et al., 2013
The section “Phot2 Is Required for Phototropism under HBL” reports significant hypocotyl bending in phot1 mutants under high-intensity blue light, supporting that part of the claim. Our copy does not report NPH3 phosphorylation measurements or establish that PHOT2-mediated phototropism does not require NPH3 phosphorylation (searched: NPH3 phosphorylation and dephosphorylation). Page numbers were not provided for these passages. (LLM, conf=0.88)
Experimental — accuracy not yet measuredThe blue light receptor phototropin mainly mediates the phototropism of angiosperms, and phot1 phot2 double mutants exhibit slight phototropism after intense blue light irradiation.
“The blue light receptor phototropin mainly mediates the phototropism of angiosperms, and phot1 phot2 double mutants exhibit slight phototropism after intense blue light irradiation (Sakai et al., 2001; Zhao et al., 2013, 2018, 2020).”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Zhao et al., 2013
The introductory passage labeled Abstract and the section ‘The Role of phot2 in Hypocotyl Phototropic Responses’ identify phot1 and phot2 as blue-light receptors regulating hypocotyl phototropism in Arabidopsis. Figure 6’s caption says the double mutant was tested under high-intensity blue light, but the available text does not state that it exhibited slight phototropism. The paper’s findings are also specific to Arabidopsis rather than angiosperms generally; the indexed passages have no page numbers. (LLM, conf=0.82)
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- Authors
- Zhao, X., Wang, Y.-L., Qiao, X.-R., Wang, J., Wang, L.-D., Xu, C.-S., & Zhang, X.
- Affiliations
- Henan University (CN)
- Institute of Plant Stress Biology, State Key Laboratory of Cotton Biology, School of Life Sciences, Henan University, Kaifeng 475004, People’s Republic of China
- Venue
- Plant Physiology
- Publisher
- Oxford University Press (OUP)
- Published
- 2013-05-14
- Volume
- 162
- Issue
- 3
- Pages
- 1539-1551
- ISSN
- 0032-0889 (ISSN-L)
- 1532-2548
- PMC
- PMC3700674
- OpenAlex
- W2046390665
- Cited by
- 84
- References
- 49
- Citations by year
- 2026: 6 · 2025: 3 · 2024: 7 · 2023: 4 · 2022: 4 · 2021: 14 · 2020: 17 · 2019: 3 · 2018: 10 · 2017: 4 · 2016: 1 · 2015: 6 · 2014: 4 · 2013: 1
- FWCI
- 4.83
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- PLANT PHYSIOLOGY (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Université de Genève
- 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 › Agricultural and Biological Sciences › Plant Science › Plant Parasitism and Resistance
- Keywords
- phototropin, phot1, phot2, intracellular calcium, calcium signaling, blue light receptor, polar auxin transport, auxin efflux carriers, PKS1, calmodulin, plasma membrane calcium channels, Arabidopsis thaliana
- MeSH terms
- Calcium, Calmodulin, Cytosol, Indoleacetic Acids, Light, Membrane Proteins, Mutation, Phosphoproteins, Signal Transduction, Protein Serine-Threonine Kinases, Arabidopsis, Gene Expression Regulation, Plant, Phototropism, Hypocotyl, Membrane Transport Proteins, Arabidopsis Proteins, Plants, Genetically Modified, Intracellular Signaling Peptides and Proteins
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