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Originally published In Press as doi:10.1074/jbc.M105364200 on September 6, 2001

J. Biol. Chem., Vol. 276, Issue 47, 43663-43667, November 23, 2001
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beta -Arrestin-mediated Recruitment of the Src Family Kinase Yes Mediates Endothelin-1-stimulated Glucose Transport*

Takeshi ImamuraDagger §, Jie HuangDagger , Stephane DalleDagger , Satoshi UgiDagger , Isao UsuiDagger , Louis M. Luttrell||, William E. Miller||, Robert J. Lefkowitz||, and Jerrold M. OlefskyDagger **

From the Dagger  Department of Medicine, Division of Endocrinology and Metabolism, University of California, San Diego, La Jolla, California 92093-0673 and the Veterans Affairs Medical Center, San Diego, California 92161 and the  Geriatric Research, Education and Clinical Center, Durham Veterans Affairs Medical Center and the || Departments of Medicine and Biochemistry, Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710

The insulin and the endothelin type A (ETA) receptor both can couple into the heterotrimeric G protein alpha q/11 (Galpha q/11), leading to Galpha q/11 tyrosine phosphorylation, phosphatidylinositol 3-kinase activation, and subsequent stimulation of glucose transport. In this study, we assessed the potential role of Src kinase in ET-1 signaling to glucose transport in 3T3-L1 adipocytes. Src kinase inhibitor PP2 blocked ET-1-induced Src kinase activity, Galpha q/11 tyrosine phosphorylation, and glucose transport stimulation. To determine which Src family kinase member was involved, we microinjected anti-c-Src, -c-Fyn, or -c-Yes antibody into these cells and found that only anti-c-Yes antibody blocked GLUT4 translocation (70% decreased). Overexpression or microinjection of a dominant negative mutant (K298M) of Src kinase also inhibited ET-1-induced Galpha q/11 tyrosine phosphorylation and GLUT4 translocation. In co-immunoprecipitation experiments, we found that beta -arrestin 1 associated with the ETA receptor in an agonist-dependent manner and that beta -arrestin 1 recruited Src kinase to a molecular complex that included the ETA receptor. Microinjection of beta -arrestin 1 antibody inhibited ET-1- but not insulin-stimulated GLUT4 translocation. In conclusion, 1) the Src kinase Yes can induce tyrosine phosphorylation of Galpha q/11 in response to ET-1 stimulation, and 2) beta -arrestin 1 and Src kinase form a molecular complex with the ETA receptor to mediate ET-1 signaling to Galpha q/11 with subsequent glucose transport stimulation.

* This work was supported in part by National Institutes of Health Grant DK-33651 and the Veterans Affairs Medical Research Service.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported through an American Diabetes Association Mentor-based Fellowship Award.

** To whom correspondence should be addressed: Dept. of Medicine (0673), University of California, San Diego, 9500 Gilman Dr., La Jolla, CA 92093-0673. Tel.: 858-534-6651; Fax: 858-534-6653; E-mail: jolefsky@ucsd.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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