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Vol. 13, Issue 9, 3203-3217, September 2002

41 Integrin Regulates Lamellipodia Protrusion via a Focal Complex/Focal Adhesion-independent Mechanism

Karen A. Pinco, Wei He, and Joy T. Yang^*

Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205

41 integrin plays an important role in cell migration. We show that when ectopically expressed in Chinese hamster ovary cells, 41 is sufficient and required for promoting protrusion of broad lamellipodia in response to scratch-wounding, whereas 51 does not have this effect. By time-lapse microscopy of cells expressing an 4/green fluorescent protein fusion protein, we show that 41 forms transient puncta at the leading edge of cells that begin to protrude lamellipodia in response to scratch-wounding. The cells expressing a mutant 4/green fluorescent protein that binds paxillin at a reduced level had a faster response to scratch-wounding, forming 4-positive puncta and protruding lamellipodia much earlier. While enhancing lamellipodia protrusion, this mutation reduces random motility of the cells in Transwell assays, indicating that lamellipodia protrusion and random motility are distinct types of motile activities that are differentially regulated by interactions between 41 and paxillin. Finally, we show that, at the leading edge, 4-positive puncta and paxillin-positive focal complexes/adhesions do not colocalize, but 41 and paxillin colocalize partially in ruffles. These findings provide evidence for a specific role of 41 in lamellipodia protrusion that is distinct from the motility-promoting functions of 51 and other integrins that mediate cell adhesion and signaling events through focal complexes and focal adhesions.

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^* Corresponding author: E-mail address: jyang{at}jhmi.edu.

Online version of this article contains video material for some figures. Online version available at www.molbiolcell.org.

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Molecular Biology of the Cell
Vol. 13, 3203-3217, September 2002
Copyright © 2002 by The American Society for Cell Biology

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