Journal
EMBO JOURNAL
Volume 31, Issue 16, Pages 3457-3467Publisher
WILEY
DOI: 10.1038/emboj.2012.186
Keywords
light-activated protein kinase; photoreceptor co-action; phototropin 1; phototropism; Phytochrome Kinase Substrate 4
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Funding
- University of Lausanne
- Swiss National Science Foundation [3100A0-112638]
- MEXT of Japan [22120005]
- EMBO LT post-doctoral fellowship
- Grants-in-Aid for Scientific Research [22120005] Funding Source: KAKEN
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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. The EMBO Journal (2012) 31, 3457-3467. doi:10.1038/emboj.2012.186; Published online 10 July 2012
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