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Molecular basis for blue light-dependent phosphorylation of Arabidopsis cryptochrome 2
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Molecular basis for blue light-dependent phosphorylation of Arabidopsis cryptochrome 2
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Molecular basis for blue light-dependent phosphorylation of Arabidopsis cryptochrome 2
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Journal Article
Molecular basis for blue light-dependent phosphorylation of Arabidopsis cryptochrome 2
2017
Overview
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
amiR
4k
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.
Plant cryptochromes are regulated by blue-light dependent phosphorylation. Here the authors map the
in vivo
phosphorylation sites of
Arabidopsis
cryptochrome 2 and identify four closely related kinases that act to both activate and destabilize the receptor in response to blue light.
