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

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 () and Chentao Lin ()
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Qing Liu: Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry University
Qin Wang: Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry University
Weixian Deng: Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry University
Xu Wang: Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry University
Mingxin Piao: Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry University
Dawei Cai: Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry University
Yaxing Li: Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry University
William D. Barshop: University of California
Xiaolan Yu: Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry University
Tingting Zhou: College of Plant Science, Jilin University
Bin Liu: Institute of Crop Sciences, Chinese Academy of Agricultural Sciences
Yoshito Oka: Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry University
James Wohlschlegel: University of California
Zecheng Zuo: Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry University
Chentao Lin: Cell & Developmental Biology, University of California

Nature Communications, 2017, vol. 8, issue 1, 1-12

Abstract: 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.

Date: 2017
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DOI: 10.1038/ncomms15234

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