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Photoactivation and inactivation of Arabidopsis cryptochrome 2
Author(s) -
Qin Wang,
Zecheng Zuo,
Xu Wang,
Lianfeng Gu,
Takeshi Yoshizumi,
Zhaohe Yang,
Liang Yang,
Qing Liu,
Wei Liu,
YunJeong Han,
JeongIl Kim,
Bin Liu,
James A. Wohlschlegel,
Minami Matsui,
Y. Oka,
Chentao Lin
Publication year - 2016
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.aaf9030
Subject(s) - cryptochrome , arabidopsis , chemistry , biophysics , biology , biochemistry , gene , circadian clock , mutant
Cryptochromes are blue-light receptors that regulate development and the circadian clock in plants and animals. We found that Arabidopsis cryptochrome 2 (CRY2) undergoes blue light-dependent homodimerization to become physiologically active. We identified BIC1 (blue-light inhibitor of cryptochromes 1) as an inhibitor of plant cryptochromes that binds to CRY2 to suppress the blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2. We hypothesize that regulated dimerization governs homeostasis of the active cryptochromes in plants and other evolutionary lineages.

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