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Photoactivation and inactivation of Arabidopsis cryptochrome 2.

  • Author(s): Wang, Qin
  • Zuo, Zecheng
  • Wang, Xu
  • Gu, Lianfeng
  • Yoshizumi, Takeshi
  • Yang, Zhaohe
  • Yang, Liang
  • Liu, Qing
  • Liu, Wei
  • Han, Yun-Jeong
  • Kim, Jeong-Il
  • Liu, Bin
  • Wohlschlegel, James A
  • Matsui, Minami
  • Oka, Yoshito
  • Lin, Chentao
  • et al.
Abstract

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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