Molecular basis for blue light-dependent phosphorylation of Arabidopsis cryptochrome 2 View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-05-11

AUTHORS

Qing Liu, Qin Wang, Weixian Deng, Xu Wang, Mingxin Piao, Dawei Cai, Yaxing Li, William D Barshop, Xiaolan Yu, Tingting Zhou, Bin Liu, Yoshito Oka, James Wohlschlegel, Zecheng Zuo, Chentao Lin

ABSTRACT

Plant cryptochromes undergo blue light-dependent phosphorylation to regulate their activity and abundance, but the protein kinases that phosphorylate plant cryptochromes have remained unclear. Here we show that photoexcited Arabidopsis cryptochrome 2 (CRY2) is phosphorylated in vivo on as many as 24 different residues, including 7 major phosphoserines. We demonstrate that four closely related Photoregulatory Protein Kinases (previously referred to as MUT9-like kinases) interact with and phosphorylate photoexcited CRY2. Analyses of the ppk123 and ppk124 triple mutants and amiR4k artificial microRNA-expressing lines demonstrate that PPKs catalyse blue light-dependent CRY2 phosphorylation to both activate and destabilize the photoreceptor. Phenotypic analyses of these mutant lines indicate that PPKs may have additional substrates, including those involved in the phytochrome signal transduction pathway. These results reveal a mechanism underlying the co-action of cryptochromes and phytochromes to coordinate plant growth and development in response to different wavelengths of solar radiation in nature. More... »

PAGES

15234

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncomms15234

DOI

http://dx.doi.org/10.1038/ncomms15234

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1085389911

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/28492234


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