We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Regulation of Arabidopsis photoreceptor CRY2 by two distinct E3 ubiquitin ligases.
- Authors
Chen, Yadi; Hu, Xiaohua; Liu, Siyuan; Su, Tiantian; Huang, Hsiaochi; Ren, Huibo; Gao, Zhensheng; Wang, Xu; Lin, Deshu; Wohlschlegel, James A.; Wang, Qin; Lin, Chentao
- Abstract
Cryptochromes (CRYs) are photoreceptors or components of the molecular clock in various evolutionary lineages, and they are commonly regulated by polyubiquitination and proteolysis. Multiple E3 ubiquitin ligases regulate CRYs in animal models, and previous genetics study also suggest existence of multiple E3 ubiquitin ligases for plant CRYs. However, only one E3 ligase, Cul4COP1/SPAs, has been reported for plant CRYs so far. Here we show that Cul3LRBs is the second E3 ligase of CRY2 in Arabidopsis. We demonstrate the blue light-specific and CRY-dependent activity of LRBs (Light-Response Bric-a-Brack/Tramtrack/Broad 1, 2 & 3) in blue-light regulation of hypocotyl elongation. LRBs physically interact with photoexcited and phosphorylated CRY2, at the CCE domain of CRY2, to facilitate polyubiquitination and degradation of CRY2 in response to blue light. We propose that Cul4COP1/SPAs and Cul3LRBs E3 ligases interact with CRY2 via different structure elements to regulate the abundance of CRY2 photoreceptor under different light conditions, facilitating optimal photoresponses of plants grown in nature. The fate of proteins in cells is determined by not only synthesis but also degradation. Here Chen et al. show that degradation of the plant blue light receptor CRY2 is determined by two distinct E3 ubiquitin ligases, Cul4COP1/SPAs and Cul3LRBs, regulating the function of CRY2 under different light conditions.
- Subjects
UBIQUITIN ligases; PHOTORECEPTORS; MOLECULAR clock; ARABIDOPSIS; BLUE light; LIGASES
- Publication
Nature Communications, 2021, Vol 12, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-021-22410-x