Regulation of the rhodopsin protein phosphatase, RDGC, through interaction with calmodulin

Seung Jae Lee, Craig Montell

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1097-1106
Number of pages10
JournalNeuron
Volume32
Issue number6
DOIs
StatePublished - Dec 20 2001

ASJC Scopus subject areas

  • Neuroscience(all)

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