In Vivo Phosphorylation Site Mapping and Functional Characterization of Arabidopsis Phototropin 1
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Phototropins (phot1 and phot2) are blue-light receptor kinases controlling a range of responses that optimize the photosynthetic efficiency of plants. Light sensing is mediated by two flavin-binding motifs, known as LOV1 and LOV2, located within the N-terminal region of the protein. Photoexcitation via LOV2 leads to activation of the C-terminal kinase domain and consequently receptor autophosphorylation. However, knowledge of the in-vivo phosphorylation sites for Arabidopsis phototropins is lacking and has impeded progress in elucidating the functional significance of receptor phosphorylation. We have purified phot1 from Arabidopsis and identified the in-vivo sites of receptor phosphorylation by liquid chromatography tandem mass spectrometry. Arabidopsis-derived phot1 binds flavin mononucleotide as chromophore and is phosphorylated at four major sites located upstream of LOV2 (Ser(58), Ser(85), Ser(350), and Ser(410)), three of which are induced by blue light. Nevertheless, structure-function analysis indicates that the biological activity of phot1 can be attributed to a modular unit comprising the LOV2-kinase region of the protein. Thus, peptide regions upstream of LOV2, including the sites of receptor phosphorylation identified here, do not appear to be important for receptor signaling. By contrast, these regions may be necessary for maximizing stomatal performance and possibly light-induced relocalization of phot1.
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Phosphorylation site Ser581 of PHOT1 and PHOT2 is ubiquitous in seed plants, ferns, mosses, and green algae.
“Furthermore, phosphorylation site Ser581 of PHOT1 and PHOT2 is ubiquitous in seed plants, ferns, mosses, and green algae (Sullivan et al., 2008).”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Sullivan et al., 2008
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“Furthermore, phosphorylation site Ser581 of PHOT1 and PHOT2 is ubiquitous in seed plants, ferns, mosses, and green algae (Sullivan et al., 2008).”
BackgroundWang, J., Liang, Y.-P., Zhu, J.-D., Wang, Y.-X., Yang, M.-Y., Yan, H.-R., Lv, Q.-Y., Cheng, K., Zhao, X., & Zhang, X. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2021.704618 · Cited by 15 · see citing works
- Authors
- Sullivan, S., Thomson, C. E., Lamont, D. J., Jones, M. A., & Christie, J. M.
- Affiliations
- University of Glasgow (GB)
- University of Dundee (GB)
- Venue
- Molecular Plant
- Publisher
- Elsevier BV
- Published
- 2008-01
- Volume
- 1
- Issue
- 1
- Pages
- 178-194
- ISSN
- 1674-2052 (ISSN-L)
- OpenAlex
- W2081218825
- Cited by
- 107
- References
- 65
- Citations by year
- 2026: 7 · 2025: 5 · 2024: 5 · 2023: 2 · 2022: 2 · 2021: 4 · 2020: 4 · 2019: 5 · 2018: 5 · 2017: 5 · 2016: 5 · 2015: 5 · 2014: 9 · 2013: 3 · 2012: 13
- FWCI
- 6.46
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Plant (publishedVersion)
- PubMed (publishedVersion)
- Open Access at Essex (University of Essex) (submittedVersion)
- Funders
- Royal Society
- 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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Keywords
- phototropin 1, phot1, receptor autophosphorylation, kinase domain, stomatal regulation, protein relocalization, Arabidopsis thaliana
- MeSH terms
- Chromosome Mapping, DNA-Binding Proteins, Flavin Mononucleotide, Light, Phosphoproteins, Phosphorylation, Photosynthesis, Recombinant Fusion Proteins, Mass Spectrometry, Protein Serine-Threonine Kinases, Arabidopsis, Genes, Reporter, Arabidopsis Proteins, Green Fluorescent Proteins
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