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(Received for publication, April 21, 1997, and in revised form, August 11, 1997)
From the 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.
Volume 272, Number 43,
Issue of October 24, 1997
pp. 27313-27318
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Phosphorylation of Chemoattractant Receptors Is Not Essential for
Chemotaxis or Termination of G-protein-mediated Responses
,
,
and
Department of Biological Chemistry, The
Johns Hopkins University School of Medicine,
Baltimore, Maryland 21205; § Institute for Molecular Plant
Sciences, University of Leiden, Leiden, The Netherlands; and the
¶ Department of Biochemistry, University of Groningen,
Groningen, The Netherlands
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