Activation of Protein Kinase Czeta  Induces Serine Phosphorylation of VAMP2 in the GLUT4 Compartment and Increases Glucose Transport in Skeletal Muscle

doi:10.1128/MCB.21.22.7852-7861.2001

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Molecular and Cellular Biology, November 2001, p. 7852-7861, Vol. 21, No. 22
0270-7306/01/$04.00+0 DOI: 10.1128/MCB.21.22.7852-7861.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Activation of Protein Kinase C $zeta$ Induces Serine Phosphorylation of VAMP2 in the GLUT4 Compartment and Increases Glucose Transport in Skeletal Muscle

Liora Braiman,¹ Addy Alt,¹ Toshio Kuroki,² Motoi Ohba,³ Asia Bak,¹ Tamar Tennenbaum,¹ and Sanford R. Sampson¹^,^*

Faculty of Life Sciences, Gonda-Goldschmied Center, Bar-Ilan University, Ramat-Gan 52900, Israel,¹ and Institute of Molecular Oncology² and Department of Microbiology,³ Showa University, Shinagawa-ku, Tokyo 142-8555, Japan

Received 14 February 2001/Returned for modification 30 March 2001/Accepted 20 August 2001

Insulin stimulates glucose uptake into skeletal muscle tissue mainly through the translocation of glucose transporter 4 (GLUT4)to the plasma membrane. The precise mechanism involved in thisprocess is presently unknown. In the cascade of events leadingto insulin-induced glucose transport, insulin activates specificprotein kinase C (PKC) isoforms. In this study we investigatedthe roles of PKC $zeta$ in insulin-stimulated glucose uptake and GLUT4translocation in primary cultures of rat skeletal muscle. We foundthat insulin initially caused PKC $zeta$ to associate specifically withthe GLUT4 compartments and that PKC $zeta$ together with the GLUT4 compartmentswere then translocated to the plasma membrane as a complex. PKC $zeta$ and GLUT4 recycled independently of one another. To further establishthe importance of PKC $zeta$ in glucose transport, we used adenovirusconstructs containing wild-type or kinase-inactive, dominant-negativePKC $zeta$ (DNPKC $zeta$ ) cDNA to overexpress this isoform in skeletal musclemyotube cultures. We found that overexpression of PKC $zeta$ was associatedwith a marked increase in the activity of this isoform. The overexpressed,active PKC $zeta$ coprecipitated with the GLUT4 compartments. Moreover,overexpression of PKC $zeta$ caused GLUT4 translocation to the plasmamembrane and increased glucose uptake in the absence of insulin.Finally, either insulin or overexpression of PKC $zeta$ induced serinephosphorylation of the GLUT4-compartment-associated vesicle-associatedmembrane protein 2. Furthermore, DNPKC $zeta$ disrupted the GLUT4 compartmentintegrity and abrogated insulin-induced GLUT4 translocation andglucose uptake. These results demonstrate that PKC $zeta$ regulatesinsulin-stimulated GLUT4 translocation and glucose transport throughthe unique colocalization of this isoform with the GLUT4compartments.

^* Corresponding author. Mailing address: Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan 52900, Israel. Phone: 9723 531 8203. Fax: 972 3 736 9929. E-mail: sampsos{at}mail.biu.ac.il.

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Activation of Protein Kinase C Induces Serine Phosphorylation of VAMP2 in the GLUT4 Compartment and Increases Glucose Transport in Skeletal Muscle

Activation of Protein Kinase C $zeta$ Induces Serine Phosphorylation of VAMP2 in the GLUT4 Compartment and Increases Glucose Transport in Skeletal Muscle