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Published online December 17, 2007
doi:10.1083/jcb.200706206
The Journal of Cell Biology, Vol. 179, No. 6, 1247-1259
The Rockefeller University Press, 0021-9525 $30.00
© 2007 van Rheenen et al.
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Article

EGF-induced PIP2 hydrolysis releases and activates cofilin locally in carcinoma cells



Jacco van Rheenen1,4, Xiaoyan Song1, Wies van Roosmalen1, Michael Cammer3, Xiaoming Chen1, Vera DesMarais1, Shu-Chin Yip2, Jonathan M. Backer2, Robert J. Eddy1, and John S. Condeelis1,3,4

1 Department of Anatomy and Structural Biology, 2 Department of Molecular Pharmacology, 3 Analytical Imaging Facility, and 4 Gruss Lipper Center for Biophotonics, Albert Einstein College of Medicine of Yeshiva University, Bronx, NY 10461

Correspondence to Jacco van Rheenen: jvanrhee{at}aecom.yu.edu

Lamellipodial protrusion and directional migration of carcinoma cells towards chemoattractants, such as epidermal growth factor (EGF), depend upon the spatial and temporal regulation of actin cytoskeleton by actin-binding proteins (ABPs). It is generally hypothesized that the activity of many ABPs are temporally and spatially regulated by PIP2; however, this is mainly based on in vitro–binding and structural studies, and generally in vivo evidence is lacking. Here, we provide the first in vivo data that directly visualize the spatial and temporal regulation of cofilin by PIP2 in living cells. We show that EGF induces a rapid loss of PIP2 through PLC activity, resulting in a release and activation of a membrane-bound pool of cofilin. Upon release, we find that cofilin binds to and severs F-actin, which is coincident with actin polymerization and lamellipod formation. Moreover, our data provide evidence for how PLC is involved in the formation of protrusions in breast carcinoma cells during chemotaxis and metastasis towards EGF.

Abbreviations used in this paper: ABP, actin-binding protein; FLIP, fluorescence loss in photobleaching; PM, plasma membrane.


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