Phytochrome Kinase Substrate 4 is phosphorylated by the phototropin 1 photoreceptor
Open accessAbstract
Phototropism allows plants to redirect their growth towards the light to optimize photosynthesis under reduced light conditions. Phototropin 1 (phot1) is the primary low blue light-sensing receptor triggering phototropism in Arabidopsis. Light-induced autophosphorylation of phot1, an AGC-class protein kinase, constitutes an essential step for phototropism. However, apart from the receptor itself, substrates of phot1 kinase activity are less clearly established. Phototropism is also influenced by the cryptochromes and phytochromes photoreceptors that do not provide directional information but influence the process through incompletely characterized mechanisms. Here, we show that Phytochrome Kinase Substrate 4 (PKS4), a known element of phot1 signalling, is a substrate of phot1 kinase activity in vitro that is phosphorylated in a phot1-dependent manner in vivo. PKS4 phosphorylation is transient and regulated by a type 2-protein phosphatase. Moreover, phytochromes repress the accumulation of the light-induced phosphorylated form of PKS4 showing a convergence of photoreceptor activity on this signalling element. Our physiological analyses suggest that PKS4 phosphorylation is not essential for phototropism but is part of a negative feedback mechanism.
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Blue light-activated phototropin can phosphorylate ABCB19 and PKS4 to inhibit their activity and enhance phototropism.
“Blue light-activated phototropin can phosphorylate ABCB19 and PKS4 to inhibit their activity and enhance phototropism (Christie et al., 2011; Demarsy et al., 2012).”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Demarsy et al., 2012
The Abstract reports that blue-light receptor phot1 phosphorylates PKS4. But the section “Phosphorylation of PKS4 negatively regulates phototropism” says phosphorylated PKS4 is a negative regulator, not that its phosphorylation enhances phototropism; it also does not establish inhibition of PKS4’s activity. ABCB19 is associated with the separate Christie et al. citation. (LLM, conf=0.90)
Experimental — accuracy not yet measuredBlue light can activate PHOT1 and convert PKS4 into phosphorylated PKS4L, and phytochrome can promote dephosphorylation of PKS4L; PKS4L can inhibit phototropism; therefore, phytochrome-promoted dephosphorylation of PKS4L may enhance phototropism.
“Blue light can activate PHOT1 and convert PKS4 into phosphorylated PKS4L, and phytochrome can promote dephosphorylation of PKS4L. PKS4L can inhibit phototropism; therefore, phytochrome-promoted dephosphorylation of PKS4L may enhance phototropism (Fig. 1B) (Demarsy et al., 2012).”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Demarsy et al., 2012
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Experimental — accuracy not yet measuredOnly two substrates have been identified for phototropin kinases: ABCB19 and PKS4 involved in regulating hypocotyl phototropism.
“Currently, only two substrates have been identified for phototropin kinases: ATP-binding cassette B19 (ABCB19) and PHYTOCHROME KINASE SUBSTRATE 4 (PKS4) involved in regulating hypocotyl phototropism (Christie et al., 2011; Demarsy et al., 2012).”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Demarsy et al., 2012
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Self-citation
- Authors
- Demarsy, E., Schepens, I., Okajima, K., Hersch, M., Bergmann, S., Christie, J., Shimazaki, K., Tokutomi, S., & Fankhauser, C.
- Affiliations
- University of Lausanne (CH)
- Osaka Prefecture University (JP)
- SIB Swiss Institute of Bioinformatics (CH)
- University of Glasgow (GB)
- Kyushu University (JP)
- Corresponding author
- Fankhauser, Christian
- ORCID
- Venue
- The EMBO Journal
- Published
- 2012-07-10
- Volume
- 31
- Issue
- 16
- Pages
- 3457-3467
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC3419926
- OpenAlex
- W2126646286
- Cited by
- 94
- References
- 65
- Citations by year
- 2026: 4 · 2025: 3 · 2024: 3 · 2023: 7 · 2022: 7 · 2021: 8 · 2020: 4 · 2019: 7 · 2018: 5 · 2017: 7 · 2016: 10 · 2015: 9 · 2014: 7 · 2013: 10 · 2012: 3
- FWCI
- 10.57
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- SERVAL (Université de Lausanne) (acceptedVersion, other-oa)
- IRIS (submittedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
- Funders
- National Science Foundation
- Ministry of Education, Culture, Sports, Science and Technology (22120005)
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (3100A0, 112638)
- Université de Lausanne
- 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
- phototropism, phototropin 1, protein phosphorylation, AGC protein kinases, phytochrome, cryptochrome, negative feedback, Arabidopsis thaliana
- MeSH terms
- Phosphoproteins, Phosphorylation, Protein Processing, Post-Translational, Signal Transduction, Protein Serine-Threonine Kinases, Arabidopsis, Arabidopsis Proteins, Intracellular Signaling Peptides and Proteins, Phototrophic Processes
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