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J Biol Chem, Vol. 273, Issue 48, 31640-31643, November 27, 1998
From the Howard Hughes Medical Institute, Departments of Medicine
and Biochemistry, Duke University Medical Center,
Durham, North Carolina 27710
COMMUNICATION
-Arrestins Regulate Mitogenic Signaling and Clathrin-mediated
Endocytosis of the Insulin-like Growth Factor I Receptor
-Arrestins mediate
agonist-dependent desensitization of G protein-coupled
receptors and target the receptors to clathrin-coated pits for
internalization. Here we report an expanded role of -arrestins in
promoting clathrin-mediated endocytosis of a tyrosine kinase growth
factor receptor, i.e. the insulin-like growth factor I (IGF-1) receptor. -Arrestins bind to the ligand-occupied IGF-1 receptors, promote their endocytosis, and enhance
IGF-1-dependent mitogen-activated protein kinase
phosphorylation and DNA synthesis. Our results suggest a role for
-arrestins in regulating mitogenic signaling and clathrin-mediated
endocytosis of receptors not classically coupled to G proteins.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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