Phosphorylation of chemoattractant receptors is not essential for chemotaxis or termination of G-protein-mediated responses

Ji Yun Kim, Ron D.M. Soede, Pauline Schaap, Romi Valkema, Jane A. Borleis, Peter J.M. Van Haastert, Peter N. Devreotes, Dale Hereld

Research output: Contribution to journalArticle

Abstract

In several G-protein-coupled signaling systems, ligand-induced receptor phosphorylation by specific kinases is suggested to lead to desensitization via mechanisms including receptor/G-protein uncoupling, receptor internalization, and receptor down-regulation. We report here that elimination of phosphorylation of a chemoattractant receptor of Dictyostelium, either by site-directed substitution of the serines or by truncation of the C-terminal cytoplasmic domain, completely prevented agonist-induced loss of ligand binding but did not impair the adaptation of several receptor-mediated responses including the activation of adenylyl and guanylyl cyclases and actin polymerization. In addition, the phosphorylation- deficient receptors were capable of mediating chemotaxis, aggregation, and differentiation. We propose that for chemoattractant receptors agonist- induced phosphorylation regulates surface binding activity but other phosphorylation-independent mechanisms mediate response adaptation.

Original languageEnglish (US)
Pages (from-to)27313-27318
Number of pages6
JournalJournal of Biological Chemistry
Volume272
Issue number43
DOIs
StatePublished - Nov 1 1997

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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