Phytochrome Kinase Substrate 4 is phosphorylated by the phototropin 1 photoreceptor.

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Version: Author's accepted manuscript
Serval ID
serval:BIB_D17C87E21DB2
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Phytochrome Kinase Substrate 4 is phosphorylated by the phototropin 1 photoreceptor.
Journal
EMBO Journal
Author(s)
Demarsy E., Schepens I., Okajima K., Hersch M., Bergmann S., Christie J., Shimazaki K., Tokutomi S., Fankhauser C.
ISSN
1460-2075 (Electronic)
ISSN-L
0261-4189
Publication state
Published
Issued date
2012
Volume
31
Number
16
Pages
3457-3467
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov'tPublication Status: ppublish
Abstract
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.
Keywords
Arabidopsis/enzymology, Arabidopsis/physiology, Arabidopsis Proteins/metabolism, Intracellular Signaling Peptides and Proteins/metabolism, Phosphoproteins/metabolism, Phosphorylation, Phototrophic Processes, Protein Processing, Post-Translational, Signal Transduction
Pubmed
Web of science
Create date
26/10/2012 18:25
Last modification date
20/08/2019 15:51
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