Phytochrome kinase substrate 4 is phosphorylated by the phototropin 1 photoreceptor

Demarsy, E., Schepens, I., Okajima, K., Hersch, M., Bergmann, S., Christie, J. , Shimazaki, K., Tokutomi, S. and Fankhauser, C. (2012) Phytochrome kinase substrate 4 is phosphorylated by the phototropin 1 photoreceptor. EMBO Journal, 31(16), pp. 3457-3467. (doi: 10.1038/emboj.2012.186)

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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.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Christie, Professor John
Authors: Demarsy, E., Schepens, I., Okajima, K., Hersch, M., Bergmann, S., Christie, J., Shimazaki, K., Tokutomi, S., and Fankhauser, C.
College/School:College of Medical Veterinary and Life Sciences > School of Molecular Biosciences
Journal Name:EMBO Journal
Publisher:Nature Publishing Group for the European Molecular Biology Organization (EMBO)
ISSN:0261-4189
ISSN (Online):1460-2075
Published Online:10 July 2012

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