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Published online
doi:10.1083/jcb.200712050
The Journal of Cell Biology, Vol. 182, No. 4, 777-790
The Rockefeller University Press, 0021-9525 $30.00
© Smith et al.
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Article

uPAR promotes formation of the p130Cas–Crk complex to activate Rac through DOCK180



Harvey W. Smith, Pierfrancesco Marra, and Christopher J. Marshall

Cancer Research UK Centre for Cell and Molecular Biology, Institute of Cancer Research, London SW3 6JB, England, UK

Correspondence to Christopher J. Marshall: Chris.Marshall{at}icr.ac.uk

The urokinase-type plasminogen activator receptor (uPAR) drives tumor cell membrane protrusion and motility through activation of Rac; however, the pathway leading from uPAR to Rac activation has not been described. In this study we identify DOCK180 as the guanine nucleotide exchange factor acting downstream of uPAR. We show that uPAR cooperates with integrin complexes containing β3 integrin to drive formation of the p130Cas–CrkII signaling complex and activation of Rac, resulting in a Rac-driven elongated-mesenchymal morphology, cell motility, and invasion. Our findings identify a signaling pathway underlying the morphological changes and increased cell motility associated with uPAR expression.

Abbreviations used in this paper: ERK, extracellular signal–regulated kinase; GEF, guanine nucleotide exchange factor; GPI, glycosylphosphatidylinositol; HEK, human embryonic kidney; MEK, MAPK/ERK kinase; SD, substrate domain; uPAR, urokinase-type plasminogen activator receptor.

© 2008 Smith et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).


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