A truncated form of RGS3 negatively regulates G protein-coupled receptor stimulation of map, kinase, adenylyl cyclase and phosphoinositide phospholipase C

T. K. Chatterjee, R. A. Fisher

Research output: Contribution to journalArticle

Abstract

Recent identification of a family of proteins that function as negative regulators of G protein signaling has provoked new understanding of desensitization of this signaling process. Several RGS proteins have been shown to interact with and function as GTPase-activating proteins specifically for G proteins in the (;, family. Here, we investigated the functional activity of RGS3 and a truncated form of RGS3 (RGS3T) on (; protein-coupled receptormediated activation of MAP kinase, adenylyl cyclase and phosphoinositide phospholipase C ill intact cells. RGS3T transcripts encode the approximate carboxyl terminal half of R(;S3 and are expressed in a tissue-specific manner. BHK cells transiently transfected with RGS3 or RGS3T cDNAs showed a marked reduction in lysophosphatidic acid-stimulated tyrosine phosphorylation of ERK1 and ERK2. BHK cells transfected with RGS3T eDNA but not those transfected with RGS3 eDNA exhibited a pronounced impairment in platelet-activating factor- or pituitary-adenylate cyclase-activating polypeptide (PA(?AP)-stimulated inositol phosphate production and in calcitonin generelated peptide- or PACAP stimulated intracellular cAMP production. These results provide the first evidence for regulatory effects of an RGS protein on Gs- or (;mediated signaling pathways in intact cells and document that the carboxyl terminal region of RGS3 comprises the structural domain for this activity. (NIII IIL,t 1071. DK25295).

Original languageEnglish (US)
Pages (from-to)A1334
JournalFASEB Journal
Volume11
Issue number9
StatePublished - Dec 1 1997

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics

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