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Protein kinase Czeta mediates insulin-induced glucose transport through actin remodeling in L6 muscle cells.

Authors: Liu, LZ  Zhao, HL  Zuo, J  Ho, SK  Chan, JC  Meng, Y  Fang, FD  Tong, PC 
Citation: Liu LZ, etal., Mol Biol Cell. 2006 May;17(5):2322-30. Epub 2006 Mar 8.
Pubmed: (View Article at PubMed) PMID:16525020
DOI: Full-text: DOI:10.1091/mbc.E05-10-0969

Protein kinase C (PKC) zeta has been implicated in insulin-induced glucose uptake in skeletal muscle cell, although the underlying mechanism remains unknown. In this study, we investigated the effect of PKCzeta on actin remodeling and glucose transport in differentiated rat L6 muscle cells expressing myc-tagged glucose transporter 4 (GLUT4). On insulin stimulation, PKCzeta translocated from low-density microsomes to plasma membrane accompanied by increase in GLUT4 translocation and glucose uptake. Z-scan confocal microscopy revealed a spatial colocalization of relocated PKCzeta with the small GTPase Rac-1, actin, and GLUT4 after insulin stimulation. The insulin-mediated colocalization, PKCzeta distribution, GLUT4 translocation, and glucose uptake were inhibited by wortmannin and cell-permeable PKCzeta pseudosubstrate peptide. In stable transfected cells, overexpression of PKCzeta caused an insulin-like effect on actin remodeling accompanied by a 2.1-fold increase in GLUT4 translocation and 1.7-fold increase in glucose uptake in the absence of insulin. The effects of PKCzeta overexpression were abolished by cell-permeable PKCzeta pseudosubstrate peptide, but not wortmannin. Transient transfection of constitutively active Rac-1 recruited PKCzeta to new structures resembling actin remodeling, whereas dominant negative Rac-1 prevented the insulin-mediated PKCzeta translocation. Together, these results suggest that PKCzeta mediates insulin effect on glucose transport through actin remodeling in muscle cells.


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CRRD Object Information
CRRD ID: 1642671
Created: 2007-10-08
Species: All species
Last Modified: 2007-10-08
Status: ACTIVE


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