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Title: AMP-activated protein kinase induces actin cytoskeleton reorganization in epithelial cells

Journal Article · · Biochemical and Biophysical Research Communications
; ; ; ; ; ; ; ; ; ;  [1];  [2]
  1. de Duve Institute, Universite catholique de Louvain, Avenue Hippocrate, B-1200 Brussels (Belgium)
  2. Institute of Experimental and Clinical Research - Pole of Cardiovascular Research, Universite catholique de Louvain, Avenue Hippocrate, B-1200 Brussels (Belgium)

AMP-activated protein kinase (AMPK), a known regulator of cellular and systemic energy balance, is now recognized to control cell division, cell polarity and cell migration, all of which depend on the actin cytoskeleton. Here we report the effects of A769662, a pharmacological activator of AMPK, on cytoskeletal organization and signalling in epithelial Madin-Darby canine kidney (MDCK) cells. We show that AMPK activation induced shortening or radiation of stress fibers, uncoupling from paxillin and predominance of cortical F-actin. In parallel, Rho-kinase downstream targets, namely myosin regulatory light chain and cofilin, were phosphorylated. These effects resembled the morphological changes in MDCK cells exposed to hyperosmotic shock, which led to Ca{sup 2+}-dependent AMPK activation via calmodulin-dependent protein kinase kinase-{beta}(CaMKK{beta}), a known upstream kinase of AMPK. Indeed, hypertonicity-induced AMPK activation was markedly reduced by the STO-609 CaMKK{beta} inhibitor, as was the increase in MLC and cofilin phosphorylation. We suggest that AMPK links osmotic stress to the reorganization of the actin cytoskeleton.

OSTI ID:
22202635
Journal Information:
Biochemical and Biophysical Research Communications, Vol. 396, Issue 3; Other Information: Copyright (c) 2010 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
Country of Publication:
United States
Language:
English