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MBC in Press, published online ahead of print October 25, 2006
Mol. Biol. Cell 10.1091/mbc.E06-08-0684

A more recent version of this article appeared on January 1, 2007
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Submitted on August 7, 2006
Revised on October 2, 2006
Accepted on October 13, 2006

Fibronectin Matrix Assembly Requires Distinct Contributions from Rho Kinases I and II

Atsuko Yoneda, Dmitriy Ushakov, Hinke A.B. Multhaupt, and John R. Couchman

Division of Biomedical Sciences, Imperial College London, Sir Alexander Fleming Building, Exhibition Road, London SW7 2AZ, United Kingdom

Monitoring Editor: Richard Assoian

Extracellular matrix is integral to tissue architecture and regulates many aspects of cell behavior. Fibronectin matrix assembly involves the actin cytoskeleton and the small GTPase RhoA but downstream signaling is not understood. Here, down-regulation of either rho kinase isoform (ROCK I or II) by siRNA treatment blocked fibronectin matrix assembly although the phenotypes were distinct and despite persistence of the alternate kinase. Remnant fibronectin on ROCK-deficient fibroblasts was mostly punctate and more deoxycholate soluble compared with controls. Fibronectin matrix assembly defects in ROCK-deficient cells did not result from decreased synthesis/secretion, altered fibronectin mRNA splicing, metalloproteinase activity or {alpha}5{beta}1 integrin dysfunction. Rescue could be effected by ROCK protein restoration or phosphomimetic myosin light chain expression. However, the effect of ROCK I deficiency on fibronectin matrix assembly was secondary to altered-cell surface morphology, rich in filopodia, resulting from high GTP-Cdc42 levels. Total internal reflection microscopy revealed that a submembranous pool of myosin light chain in control cells was missing in ROCK II-deficient cells and replaced by stress fibers. Taken together, two rho kinases contribute to fibronectin matrix assembly in a different manner and cortical myosin II-driven contractility, but not stress fibers, may be critical in this activity.

Address correspondence to: John R. Couchman (j.couchman{at}imperial.ac.uk)




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