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Published online 22 February 2005. doi:10.1083/jcb.200406083
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 168, Number 5, 813-824
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Article

The LIM protein Ajuba influences p130Cas localization and Rac1 activity during cell migration



Stephen J. Pratt1,2, Holly Epple1,2, Michael Ward2,3, Yunfeng Feng1,2, Vania M. Braga4, and Gregory D. Longmore1,2

1 Department of Medicine, Washington University, St. Louis, MO 63130
2 Department of Cell Biology, Washington University, St. Louis, MO 63130
3 Department of Anatomy and Neurobiology, Washington University, St. Louis, MO 63130
4 Imperial College London, London SW7 2AZ, England, UK

Correspondence to Gregory D. Longmore: glongmor{at}im.wustl.edu

Cell migration requires extension of lamellipodia that are stabilized by formation of adhesive complexes at the leading edge. Both processes are regulated by signaling proteins recruited to nascent adhesive sites that lead to activation of Rho GTPases. The Ajuba/Zyxin family of LIM proteins are components of cellular adhesive complexes. We show that cells from Ajuba null mice are inhibited in their migration, without associated abnormality in adhesion to extracellular matrix proteins, cell spreading, or integrin activation. Lamellipodia production, or function, is defective and there is a selective reduction in the level and tyrosine phosphorylation of FAK, p130Cas, Crk, and Dock180 at nascent focal complexes. In response to migratory cues Rac activation is blunted in Ajuba null cells, as detected biochemically and by FRET analysis. Ajuba associates with the focal adhesion-targeting domain of p130Cas, and rescue experiments suggest that Ajuba acts upstream of p130Cas to localize p130Cas to nascent adhesive sites in migrating cells thereby leading to the activation of Rac.

Abbreviations used in this paper: ES, embryonal stem; GEF, guanine nucleotide exchange factor; wt, wild-type.


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