Regulation of Arabidopsis photoreceptor CRY2 by two distinct E3 ubiquitin ligases

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, Cul4(COP1/SPAs), has been reported for plant CRYs so far. Here we show that Cul3(LRBs) 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 Cul4(COP1/SPAs) and Cul3(LRBs) 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, Cul4(COP1/SPAs) and Cul3(LRBs), regulating the function of CRY2 under different light conditions.

Automated summary

The degradation of the plant blue light receptor CRY2 is determined by two distinct E3 ubiquitin ligases, Cul4(COP1/SPAs) and Cul3(LRBs), regulating the function of CRY2 under different light conditions.