CRY1 and CRY2 which subsequently initiate light signal transduction by repressing the COP1/SPA E3 ubiquitin ligase
First-pass extracted concept
COP1/SPA complex
Candidate: toolkit item1 source documents5 linked claims
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Aliases
COP1/SPA E3 ubiquitin ligase
Evidence Snippets
Supporting Sources
Linked Claims
CRY1 and CRY2 differ strongly in their blue-light-induced interaction with the COP1/SPA complex.
Quoted textsource-backed
In total, our results demonstrate that CRY1 and CRY2 strongly differ in their blue light-induced interaction with the COP1/SPA complex.
SPA proteins are required for the high-affinity blue-light-induced interaction between CRY1 and COP1 in vivo.
Quoted textsource-backed
In a spa quadruple mutant that is devoid of all four SPA proteins, CRY1 and COP1 did not interact in vivo, neither in dark-grown nor in blue light-grown seedlings. Hence, SPA proteins are required for the high-affinity interaction between CRY1 and COP1 in blue light.
The blue-light-induced association between CRY2 and COP1 is not dependent on SPA proteins in vivo.
Quoted textsource-backed
In contrast, the blue light-induced association between CRY2 and COP1 was not dependent on SPA proteins in vivo.
SPA1 enhances the CRY1-COP1 interaction in yeast three-hybrid experiments.
Quoted textsource-backed
Yeast three-hybrid experiments also show that SPA1 enhances the CRY1-COP1 interaction.
CRY1 and CRY2 form a complex with COP1 only after blue-light exposure and not in dark-grown seedlings.
Quoted textsource-backed
our in vivo co-immunoprecipitation experiments suggest that CRY1 and CRY2 form a complex with COP1 only after seedlings were exposed to blue light. No association between COP1 and CRY1 or CRY2 was observed in dark-grown seedlings.