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Targeting Proteins for Degradation by Arabidopsis COP1: Teamwork Is What Matters
Author(s) -
Lin Rongcheng,
Wang Haiyang
Publication year - 2007
Publication title -
journal of integrative plant biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.734
H-Index - 83
eISSN - 1744-7909
pISSN - 1672-9072
DOI - 10.1111/j.1744-7909.2006.00414.x
Subject(s) - photomorphogenesis , arabidopsis , ubiquitin ligase , cop9 signalosome , ubiquitin , biology , cryptochrome , microbiology and biotechnology , repressor , crucifer , transcription factor , genetics , botany , biochemistry , mutant , gene , peptide hydrolases , circadian clock , protease , enzyme
Abstract Arabidopsis COP1 ( Constitutive Photomorphogenic 1 ) defines a key repressor of photomorphogenesis in darkness by acting as an E3 ubiquitin ligase in the nucleus, and is responsible for the targeted degradation of a number of photomorphogenesis‐promoting factors, including phyA, HY5, LAF1, and HFR1. Light activation of multiple classes of photoreceptors (including both phytochromes and cryptochromes) inactivates COP1 and reduces its nuclear abundance, allowing the accumulation of these positively acting light signaling intermediates to promote photomorphogenic development. Recent studies suggest that Arabidopsis COP1 teams up with a family of SPA proteins (SPA1‐SPA4) to form the physiologically active COP1‐SPA E3 ubiquitin ligase complexes. These COP1‐SPA complexes play overlapping and distinct functions in regulating seedling photomorphogenesis under different light conditions and adult plant growth. Further, the COP1‐SPA complexes act in concert at a biochemical level with the CDD (COP10, DET1, and DDB1) complex and COP9 signalosome (CSN) to orchestrate the repression of photomorphogenesis.