Journal
GENES & DEVELOPMENT
Volume 25, Issue 10, Pages 1029-1034Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.2025011
Keywords
blue-light receptor; cryptochrome; E3 ubiquitin ligase; protein degradation; photomorphogenesis
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Funding
- National Institutes of Health [GM56265]
- UCLA
- Sol Leshin BGU-UCLA
- National Transgenic Crop Initiative
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Plant photoreceptors mediate light suppression of the E3 ubiquitin ligase COP1 (CONSTITUTIVE PHOTOMORPHOGENIC 1) to affect gene expression and photomorphogenesis. However, how photoreceptors mediate light regulation of COP1 activity remains unknown. We report here that Arabidopsis blue-light receptor cryptochrome 1 (CRY1) undergoes blue-light-dependent interaction with the COP1-interacting protein SPA1 (SUPPRESSOR OF PHYTOCHROME A). We further show that the CRY1-SPA1 interaction suppresses the SPA1-COP1 interaction and COP1-dependent degradation of the transcription factor HY5. These results are consistent with a hypothesis that photoexcited CRY1 interacts with SPA1 to modulate COP1 activity and plant development.
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