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Molecular and Cellular Biology, June 1999, p. 4008-4018, Vol. 19, No. 6
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Protein Kinase B/Akt Participates in GLUT4 Translocation by Insulin in L6 Myoblasts

Qinghua Wang,1 Romel Somwar,1,2 Philip J. Bilan,1 Zhi Liu,1 Jing Jin,3 James R. Woodgett,3 and Amira Klip1,2,*

Programme in Cell Biology, The Hospital for Sick Children, Toronto, Ontario M5G 1X8,1 Department of Biochemistry, The University of Toronto, Toronto, Ontario M5S 1A8,2 and Experimental Therapeutics, Ontario Cancer Institute, Toronto, Ontario M5G 2M9,3 Canada

Received 5 November 1998/Returned for modification 15 December 1998/Accepted 22 March 1999

L6 myoblasts stably transfected with a GLUT4 cDNA harboring an exofacial myc epitope tag (L6-GLUT4myc myoblasts) were used to study the role of protein kinase B alpha (PKBalpha )/Akt1 in the insulin-induced translocation of GLUT4 to the cell surface. Surface GLUT4myc was detected by immunofluorescent labeling of the myc epitope in nonpermeabilized cells. Insulin induced a marked translocation of GLUT4myc to the plasma membrane within 20 min. This was prevented by transient transfection of a dominant inhibitory construct of phosphatidylinositol (PI) 3-kinase (Delta p85alpha ). Transiently transfected cells were identified by cotransfection of green fluorescent protein. A constitutively active PKBalpha , created by fusion of a viral Gag protein at its N terminus (GagPKB), increased the cell surface density of GLUT4myc compared to that of neighboring nontransfected cells. A kinase-inactive, phosphorylation-deficient PKBalpha /Akt1 construct with the mutations K179A (substitution of alanine for the lysine at position 179), T308A, and S473A (AAA-PKB) behaved as a dominant-negative inhibitor of insulin-dependent activation of cotransfected wild-type hemagglutinin (HA)-tagged PKB. Furthermore, AAA-PKB markedly inhibited the insulin-induced phosphorylation of cotransfected BAD, demonstrating inhibition of the endogenous PKB/Akt. Under the same conditions, AAA-PKB almost entirely blocked the insulin-dependent increase in surface GLUT4myc. PKBalpha with alanine substitutions T308A and S473A (AA-PKB) or K179A (A-PKB) alone was a less potent inhibitor of insulin-dependent activation of wild-type HA-PKB or GLUT4myc translocation than was AAA-PKB. Cotransfection of AAA-PKB with a fourfold DNA excess of HA-PKB rescued insulin-stimulated GLUT4myc translocation. AAA-PKB did not prevent actin bundling (membrane ruffling), though this response was PI 3-kinase dependent. Therefore, it is unlikely that AAA-PKB acted by inhibiting PI 3-kinase signaling. These results outline an important role for PKBalpha /Akt1 in the stimulation of glucose transport by insulin in muscle cells in culture.

* Corresponding author. Mailing address: Programme in Cell Biology, The Hospital for Sick Children, 555 University Ave., Toronto, ON M5G 1X8, Canada. Phone: (416) 813-6392. Fax: (416) 813-5028. E-mail: amira{at}sickkids.on.ca.

Molecular and Cellular Biology, June 1999, p. 4008-4018, Vol. 19, No. 6
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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