the previously reported function of the COP1-SPA1 protein complex in blue light-dependent CRY2 degradation is more likely to be attributable to its cullin 4 (CUL4)-based E3 ubiquitin ligase activity
First-pass extracted concept
CUL4-based E3 ubiquitin ligase
Candidate: toolkit item1 source documents3 linked claims
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The role of the COP1-SPA1 complex in blue light-dependent CRY2 degradation is more likely attributable to its CUL4-based E3 ubiquitin ligase activity than to its activity as a cryptochrome signaling partner.
Quoted textsource-backed
the previously reported function of the COP1-SPA1 protein complex in blue light-dependent CRY2 degradation is more likely to be attributable to its cullin 4 (CUL4)-based E3 ubiquitin ligase activity than its activity as the cryptochrome signaling partner
Photoexcited CRY2 undergoes Lys48-linked polyubiquitination catalyzed by CUL4- and CUL1-based E3 ubiquitin ligases.
Quoted textsource-backed
we propose that photoexcited CRY2 undergoes Lys48-linked polyubiquitination catalyzed by the CUL4- and CUL1-based E3 ubiquitin ligases
Blue light-dependent CRY2 degradation is only partially impaired in cul4, cop1-5 null, and spa1234 mutants, suggesting involvement of additional E3 ubiquitin ligases.
Quoted textsource-backed
the blue light-dependent CRY2 degradation is only partially impaired in the cul4 mutant, the cop1-5 null mutant and the spa1234 quadruple mutant, suggesting a possible involvement of additional E3 ubiquitin ligases in the regulation of CRY2