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J. Biol. Chem., Vol. 275, Issue 35, 26870-26876, September 1, 2000
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From the Department of Medicine, Division of Endocrinology and
Metabolism, University of California, San Diego, La Jolla,
California 92093
Osmotic shock treatment of 3T3-L1 adipocytes
causes an increase in glucose transport activity and translocation of
GLUT4 protein similar to that elicited by insulin treatment. Insulin
stimulation of GLUT4 translocation and glucose transport activity was
completely inhibited by wortmannin, however, activation by osmotic
shock was only partially blocked. Additionally, we have found that the newly identified insulin receptor substrate Gab-1 (Grb2-associated binder-1) is tyrosine-phosphorylated following sorbitol stimulation. Treatment of cells with the tyrosine kinase inhibitor genistein inhibited osmotic shock-stimulated Gab-1 phosphorylation as well as
shock-induced glucose transport. Furthermore, pretreatment with the
selective Src family kinase inhibitor PP2 completely inhibited the
ability of sorbitol treatment to cause tyrosine phosphorylation of
Gab-1. We have also shown that microinjection of anti-Gab-1 antibody
inhibits osmotic shock-induced GLUT4 translocation. Furthermore,
phosphorylated Gab-1 binds and activates phosphatidylinositol 3-kinase
(PI3K) in response to osmotic shock. The PI3K activity associated with
Gab-1 was 82% of that associated with anti-phosphotyrosine antibodies,
indicating that Gab-1 is the major site for PI3K recruitment following
osmotic shock stimulation. Although wortmannin only causes a partial
block of osmotic shock-stimulated glucose uptake, wortmannin completely
abolishes Gab-1 associated PI3K activity. This suggests that other
tyrosine kinase-dependent pathways, in addition to the
Gab-1-PI3K pathway, contribute to osmotic shock-mediated glucose
transport. To date, Gab-1 is the first protein identified as
a member of the osmotic shock signal transduction pathway.
The Osmotic Shock-induced Glucose Transport Pathway in 3T3-L1
Adipocytes Is Mediated by Gab-1 and Requires Gab-1-associated
Phosphatidylinositol 3-Kinase Activity for Full Activation*
,
*
This work was supported in part by NIH Grant DK-33651 and
the VA 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 by a grant from the Slovenian Ministry of Science and Technology.
§
Supported by NIDDK, National Institutes of Health, Individual
National Research Service Award Grant DK09595.
¶
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.
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