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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
-Arrestin-mediated Recruitment of the Src Family Kinase Yes
Mediates Endothelin-1-stimulated Glucose Transport*
Takeshi
Imamura §,
Jie
Huang ,
Stephane
Dalle ,
Satoshi
Ugi ,
Isao
Usui ,
Louis M.
Luttrell¶ ,
William
E.
Miller ,
Robert J.
Lefkowitz , and
Jerrold M.
Olefsky **
From the 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
q/11 (G q/11), leading to
G 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, G 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 G q/11 tyrosine phosphorylation
and GLUT4 translocation. In co-immunoprecipitation experiments, we
found that -arrestin 1 associated with the ETA receptor in an
agonist-dependent manner and that -arrestin 1 recruited
Src kinase to a molecular complex that included the ETA receptor.
Microinjection of -arrestin 1 antibody inhibited ET-1- but not
insulin-stimulated GLUT4 translocation. In conclusion, 1) the Src
kinase Yes can induce tyrosine phosphorylation of G q/11 in response to ET-1 stimulation, and 2) -arrestin 1 and Src kinase form a molecular complex with the ETA receptor to mediate ET-1 signaling to G 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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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.
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