Regulation of the rhodopsin protein phosphatase, RDGC, through interaction with calmodulin
Regulation of the rhodopsin protein phosphatase, RDGC, through interaction with calmodulin
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DOI：
10.1016/s0896-6273(01)00538-4
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发表时间：
2001-12-26
期刊：
影响因子：
16.2
通讯作者：
Montell, C
中科院分区：
文献类型：
--
作者：
Lee, SJ;Montell, C
已经鉴定了数百种G蛋白偶联受体（GPCR）和至少6种GPCR激酶，但唯一明确证明的GPCR磷酸酶是由果蝇的rdgC基因座编码的视紫红质磷酸酶。rdgC的突变导致光反应终止的缺陷，并导致严重的视网膜变性。在目前的工作中，我们证明，RDGC结合钙调蛋白，并在IQ基序，消除钙调蛋白/RDGC相互作用的突变，防止视紫红质在体内的去磷酸化和破坏终止的光响应。我们的数据表明，RDGC是一种新的钙调蛋白依赖性蛋白磷酸酶，并提高了通过去磷酸化调节其他GPCR的可能性，可能是由钙调蛋白依赖性蛋白磷酸酶RDGC相关的控制。
Hundreds of G protein-coupled receptors (GPCRs) and at least six GPCR kinases have been identified, but the only GPCR phosphatase that has been definitively demonstrated is the rhodopsin phosphatase encoded by the rdgC locus of Drosophila. Mutations in rdgC result in defects in termination of the light response and cause severe retinal degeneration. In the current work, we demonstrate that RDGC binds to calmodulin, and a mutation in an IQ motif that eliminates the calmodulin/RDGC interaction prevents dephosphorylation of rhodopsin in vivo and disrupts termination of the photoresponse. Our data indicate that RDGC is a novel calmodulin-dependent protein phosphatase and raise the possibility that regulation of other GPCRs through dephosphorylation may be controlled by calmodulin-dependent protein phosphatases related to RDGC.