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Molecular and Cellular Biology, August 2001, p. 5276-5285, Vol. 21, No. 15
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.15.5276-5285.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

ADP-Ribosylation Factor 6 Delineates Separate Pathways Used by Endothelin 1 and Insulin for Stimulating Glucose Uptake in 3T3-L1 Adipocytes

J. Todd R. Lawrence and Morris J. Birnbaum*

Department of Medicine, Howard Hughes Medical Institute, The Cox Institute, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104

Received 11 December 2000/Returned for modification 8 February 2001/Accepted 30 April 2001

In 3T3-L1 adipocytes, both insulin and endothelin 1 stimulate glucose transport via translocation of the GLUT4 glucose carrier from an intracellular compartment to the cell surface. Yet it remains uncertain as to whether both hormones utilize identical pathways and to what extent each depends on the heterotrimeric G protein Galpha q as an intermediary signaling molecule. In this study, we used a novel inducible system to rapidly and synchronously activate expression of a dominant inhibitory form of ADP-ribosylation factor 6, ARF6(T27N), in 3T3-L1 adipocytes and assessed its effects on insulin- and endothelin-stimulated hexose uptake. Expression of ARF6(T27N) in 3T3-L1 adipocytes was without effect on the ability of insulin to stimulate either 2-deoxyglucose uptake or the translocation of GLUT4 or GLUT1 to the plasma membrane. However, the same ARF6 inhibitory mutant blocked the stimulation of hexose uptake and GLUT4 translocation in response to either endothelin 1 or an activated form of Galpha q, Galpha q(Q209L). These results suggest that endothelin stimulates glucose transport through a pathway that is distinct from that utilized by insulin but is likely to depend on both a heterotrimeric G protein from the Gq family and the small G protein ARF6. These data are consistent with the interpretation that endothelin and insulin stimulate functionally different pools of glucose transporters to be redistributed to the plasma membrane.

* Corresponding author. Mailing address: Howard Hughes Medical Institute, University of Pennsylvania Medical School, 415 Curie Blvd., Room 322 CRB, Philadelphia, PA 19104. Phone: (215) 898-5001. Fax: (215) 573-9138. E-mail: birnbaum{at}mail.med.upenn.edu.

Molecular and Cellular Biology, August 2001, p. 5276-5285, Vol. 21, No. 15
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.15.5276-5285.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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