Implication of phosphorylation of the myosin II regulatory light chain in insulin-stimulated GLUT4 translocation in 3T3-F442A adipocytes

In adipocytes, insulin stimulates glucose transport primarily by promoting the translocation of GLUT4 to the plasma membrane. Requirements for Ca(2+)/calmodulin during insulin-stimulated GLUT4 translocation have been demonstrated; however, the mechanism of action of Ca(2+) in this process is unknown...

Full description

Saved in:
Bibliographic Details
Published in:Experimental & molecular medicine 2006-04, Vol.38 (2), p.180-189
Main Authors: Choi, Young Ok, Ryu, Hee Jeong, Kim, Hye Rim, Song, Young Sook, Kim, Cheonghwan, Lee, Wan, Choe, Han, Leem, Chae Hun, Jang, Yeon Jin
Format: Article
Language:English
Subjects:
3T3 Cells
Adipocytes - cytology
Adipocytes - drug effects
Adipocytes - metabolism
Animals
Azepines - pharmacology
Calmodulin - antagonists & inhibitors
Calmodulin - physiology
Dose-Response Relationship, Drug
Enzyme Inhibitors - pharmacology
Glucose Transporter Type 4 - metabolism
Insulin - pharmacology
Mice
Myosin Type II - metabolism
Myosin-Light-Chain Kinase - antagonists & inhibitors
Myosin-Light-Chain Kinase - metabolism
Naphthalenes - pharmacology
Phosphorylation
Protein Transport - drug effects
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:In adipocytes, insulin stimulates glucose transport primarily by promoting the translocation of GLUT4 to the plasma membrane. Requirements for Ca(2+)/calmodulin during insulin-stimulated GLUT4 translocation have been demonstrated; however, the mechanism of action of Ca(2+) in this process is unknown. Recently, myosin II, whose function in non-muscle cells is primarily regulated by phosphorylation of its regulatory light chain by the Ca(2+)/calmodulin-dependent myosin light chain kinase (MLCK), was implicated in insulin-stimulated GLUT4 translocation. The present studies in 3T3-F442A adipocytes demonstrate the novel finding that insulin significantly increases phosphorylation of the myosin II RLC in a Ca(2+)-dependent manner. In addition, ML-7, a selective inhibitor of MLCK, as well as inhibitors of myosin II, such as blebbistatin and 2,3-butanedione monoxime, block insulin-stimulated GLUT4 translocation and subsequent glucose transport. Our studies suggest that MLCK may be a regulatory target of Ca(2+)/calmodulin and may play an important role in insulin-stimulated glucose transport in adipocytes.
ISSN:1226-3613
2092-6413
2092-6413
DOI:10.1038/emm.2006.22