Photoactivation and inactivation of Arabidopsis cryptochrome 2

Wang, Q. et al. (2016) Photoactivation and inactivation of Arabidopsis cryptochrome 2. Science, 354(6310), pp. 343-347. (doi: 10.1126/science.aaf9030) (PMID:27846570) (PMCID:PMC6180212)

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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.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Liu, Dr Wei
Authors: Wang, Q., Zuo, Z., Wang, X., Gu, L., Yoshizumi, T., Yang, Z., Yang, L., Liu, Q., Liu, W., Han, Y.-J., Kim, J.-I., Liu, B., Wohlschlegel, J. A., Matsui, M., Oka, Y., and Lin, C.
College/School:College of Medical Veterinary and Life Sciences > School of Molecular Biosciences
Journal Name:Science
Publisher:American Association for the Advancement of Science
ISSN (Online):1095-9203

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