Molecular Biology of the Cell Sign up for new MBC in Press e-TOCs!

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
QUICK SEARCH:   [advanced]


     

MBC in Press, published online ahead of print March 8, 2006
Mol. Biol. Cell 10.1091/mbc.E05-10-0969

A more recent version of this article appeared on May 1, 2006
This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
E05-10-0969v1
17/5/2322    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Liu, L.-Z.
Right arrow Articles by Tong, P. C.Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Liu, L.-Z.
Right arrow Articles by Tong, P. C.Y.

Submitted on October 24, 2005
Revised on January 23, 2006
Accepted on March 1, 2006

PKC {zeta} Mediates Insulin-induced Glucose Transport through Actin Remodeling in L6 Muscle Cells

Li-Zhong Liu,*{dagger} Hai-Lu Zhao,{dagger} Jin Zuo,* Stanley K.S. Ho,{dagger} Juliana C.N. Chan,{dagger} Yan Meng,{dagger} Fu-De Fang,* and Peter C.Y. Tong{dagger}

*Department of Biochemistry, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and Peking Union Medical College, 100005 Beijing, China; {dagger}Department of Medicine and Therapeutics, Prince of Wales Hospital, Chinese University of Hong Kong, Shatin, N.T., Hong Kong, China

Monitoring Editor: Carl-Henrik Heldin

PKC {zeta} has been implicated in insulin-induced glucose uptake in skeletal muscle cell, though the underlying mechanism remains unknown. In this study, we investigated the effect of PKC{zeta} on actin remodeling and glucose transport in differentiated rat L6 muscle cells expressing myc-tagged glucose transporter 4 (GLUT4). On insulin stimulation, PKC{zeta} 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 PKC{zeta} with the small GTPase Rac-1, actin and GLUT4 after insulin stimulation. The insulin-mediated colocalization, PKC{zeta} distribution, GLUT4 translocation and glucose uptake were inhibited by wortmannin and cell-permeable PKC{zeta} pseudosubstrate peptide. In stable transfected cells, overexpression of PKC{zeta} 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 PKC{zeta} overexpression were abolished by cell-permeable PKC{zeta} pseudosubstrate peptide, but not wortmannin. Transient transfection of constitutive active Rac-1 recruited PKC{zeta} to new structures resembling of actin remodeling, while dominant negative Rac-1 prevented the insulin-mediated PKC{zeta} translocation. Taken together, these results suggest that PKC{zeta} mediates insulin effect on glucose transport through actin remodeling in muscle cells.

Address correspondence to: Yan Meng (ymengsmile{at}yahoo.com) or Fu-De Fang (fangfd{at}public3.bta.net.cn) or Peter C.Y. Tong (ptong{at}cuhk.edu.hk)




This article has been cited by other articles:


Home page
 Endocr. Rev.Home page
W. L. Holland and S. A. Summers
Sphingolipids, Insulin Resistance, and Metabolic Disease: New Insights from in Vivo Manipulation of Sphingolipid Metabolism
Endocr. Rev., June 1, 2008; 29(4): 381 - 402.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
P. Song, Z. Xie, Y. Wu, J. Xu, Y. Dong, and M.-H. Zou
Protein Kinase C{zeta}-dependent LKB1 Serine 428 Phosphorylation Increases LKB1 Nucleus Export and Apoptosis in Endothelial Cells
J. Biol. Chem., May 2, 2008; 283(18): 12446 - 12455.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Miele, F. Paturzo, R. Teperino, F. Sakane, F. Fiory, F. Oriente, P. Ungaro, R. Valentino, F. Beguinot, and P. Formisano
Glucose Regulates Diacylglycerol Intracellular Levels and Protein Kinase C Activity by Modulating Diacylglycerol Kinase Subcellular Localization
J. Biol. Chem., November 2, 2007; 282(44): 31835 - 31843.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Pharmacol.Home page
L. Moreno, G. Frazziano, A. Cogolludo, L. Cobeno, J. Tamargo, and F. Perez-Vizcaino
Role of Protein Kinase C{zeta} and Its Adaptor Protein p62 in Voltage-Gated Potassium Channel Modulation in Pulmonary Arteries
Mol. Pharmacol., November 1, 2007; 72(5): 1301 - 1309.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2006 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.