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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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