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(Received for publication, August 12, 1996, and in revised form, December 17, 1996)
From the J. A. Haley Veterans' Hospital Research Service and the
Departments of Internal Medicine and Biochemistry/Molecular
Biology, University of South Florida, Tampa, Florida 33612
Insulin reportedly (Standaert, M. L., Avignon,
A., Yamada, K., Bandyopadhyay, G., and Farese, R. V. (1996)
Biochem. J. 313, 1039-1046) activates phospholipase D
(PLD)-dependent hydrolysis of phosphatidylcholine (PC) in
plasma membranes of rat adipocytes by a mechanism that may involve
wortmannin-sensitive phosphatidylinositol (PI) 3-kinase. Because Rho
and ADP ribosylation factor (ARF) activate PC-PLD, we questioned
whether these small G-proteins are regulated by insulin and PI
3-kinase. We found that insulin provoked a rapid translocation of both
Rho and ARF to the plasma membrane and increased GTP loading of Rho.
Wortmannin and LY294002 inhibited Rho translocation in intact
adipocytes, and the polyphosphoinositide, PI
4,5-(PO4)2, stimulated Rho translocation in
adipocyte homogenates. On the other hand, wortmannin did not block GTP
loading of Rho. Guanosine 5
-3-O-(thio)triphosphate
stimulated both Rho and ARF translocation and activated PC-PLD in
homogenates. C3 transferase, which inhibits and depletes Rho, inhibited
PC-PLD activation by insulin in intact adipocytes. C3 transferase also
inhibited insulin stimulation of [3H]2-deoxyglucose
uptake. Our findings suggest that: (a) insulin translocates
Rho by a PI 3-kinase-dependent mechanism, but another factor is responsible for GTP loading of Rho; (b) both Rho
and ARF may contribute to PC-PLD activation during insulin action; and
(c) Rho may be required for insulin stimulation of glucose transport.
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