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Published 27 February 2006. doi:10.1083/jcb.200512115
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 172, Number 5, 771-782
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Article

 Genetic ablation of zyxin causes Mena/VASP mislocalization, increased motility, and deficits in actin remodeling

Laura M. Hoffman1,2, Christopher C. Jensen1, Susanne Kloeker1, C.-L. Albert Wang5, Masaaki Yoshigi1,4, and Mary C. Beckerle1,2,3

1 The Huntsman Cancer Institute and the 2 Department of Biology, 3 Department of Oncological Sciences, and 4 Department of Pediatrics, University of Utah, Salt Lake City, UT 84112
5 Boston Biomedical Research Institute, Watertown, MA 02472

Correspondence to Mary C. Beckerle: mary.beckerle{at}hci.utah.edu

Focal adhesions are specialized regions of the cell surface where integrin receptors and associated proteins link the extracellular matrix to the actin cytoskeleton. To define the cellular role of the focal adhesion protein zyxin, we characterized the phenotype of fibroblasts in which the zyxin gene was deleted by homologous recombination. Zyxin-null fibroblasts display enhanced integrin-dependent adhesion and are more migratory than wild-type fibroblasts, displaying reduced dependence on extracellular matrix cues. We identified differences in the profiles of 75- and 80-kD tyrosine-phosphorylated proteins in the zyxin-null cells. Tandem array mass spectrometry identified both modified proteins as isoforms of the actomyosin regulator caldesmon, a protein known to influence contractility, stress fiber formation, and motility. Zyxin-null fibroblasts also show deficits in actin stress fiber remodeling and exhibit changes in the molecular composition of focal adhesions, most notably by severely reduced accumulation of Ena/VASP proteins. We postulate that zyxin cooperates with Ena/VASP proteins and caldesmon to influence integrin-dependent cell motility and actin stress fiber remodeling.

Abbreviations used in this paper: 2D, two-dimensional; h, high molecular weight; ILK, integrin-linked kinase; l, low molecular weight; LPP, lipoma preferred partner; MEF, mouse embryonic fibroblast; pY, phosphotyrosine; SFTI, stress fiber thickness index; TRIP, thyroid receptor-interacting protein.


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