Molecular basis for blue light-dependent phosphorylation of Arabidopsis cryptochrome 2.
Molecular basis for blue light-dependent phosphorylation of Arabidopsis cryptochrome 2.
复制标题
拟南芥隐花色素2蓝光依赖性磷酸化的分子基础
DOI:
10.1038/ncomms15234
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发表时间:
2017-05-11
影响因子:
16.6
通讯作者:
Lin C
中科院分区:
文献类型:
--
作者:
Liu Q;Wang Q;Deng W;Wang X;Piao M;Cai D;Li Y;Barshop WD;Yu X;Zhou T;Liu B;Oka Y;Wohlschlegel J;Zuo Z;Lin C
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.