Photoreceptor ubiquitination by COP1 E3 ligase desensitizes phytochrome A signaling
Photoreceptor ubiquitination by COP1 E3 ligase desensitizes phytochrome A signaling
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DOI：
10.1101/gad.1187804
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发表时间：
2004-03-15
影响因子：
10.5
通讯作者：
Chua, NH
中科院分区：
文献类型：
--
作者：
Seo, HS;Watanabe, E;Chua, NH
激活受体的脱敏是终止信号转导的重要机制。在这里，我们表明，光敏色素（phy）A，一个主要的感光体的幼苗去黄化，共定位在核体与组成光形态发生（COP）1，环基序含有E3连接酶。phyA PAS结构域与COP 1 WD40结构域相互作用。Pr和Pfr形式的phyA，以及PHYA脱辅基蛋白，在体外被COPI泛素化。phyA的破坏率降低cop1突变体和表达的COP1环基序突变体。我们的研究结果表明，COP1作为E3连接酶，通过靶向消除phyA光感受器本身来调节phyA信号传导。
Desensitization of activated receptors is an important mechanism for terminating signal transduction. Here we show that phytochrome (phy) A, a predominant photoreceptor for seedling deetiolation, colocalizes in nuclear bodies with CONSTITUTIVELY PHOTOMORPHOGENIC (COP) 1, a RING motif-containing E3 ligase. The phyA PAS domain interacts with the COP1 WD40 domain. Both the Pr and the Pfr forms of phyA, as well as the PHYA apoprotein, are ubiquitinated by COPI in vitro. The phyA destruction rate is decreased in cop1 mutants and by expression of a COP1 RING motif mutant. Our results indicate that COP1 acts as an E3 ligase to regulate phyA signaling by targeting elimination of the phyA photoreceptor itself.