4.8 Article

Photoactivation and inactivation of Arabidopsis cryptochrome 2

Journal

SCIENCE
Volume 354, Issue 6310, Pages 343-347

Publisher

AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aaf9030

Keywords

-

Funding

  1. NIH [GM56265, GM089778, GM112763]
  2. Rural Development Administration of Republic of Korea [PJ01104001]
  3. Biomass Engineering Program of RIKEN
  4. Special Postdoctoral Researcher Program of RIKEN
  5. National Natural Science Foundation of China [31500991, 31570674, 31422041, 31371411]
  6. Fujian 2011 Program [2015-75]
  7. Grants-in-Aid for Scientific Research [25113006] Funding Source: KAKEN

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.8
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available