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Journal of Oncology
Volume 2010, Article ID 932803, 10 pages
Research Article

Hyperphosphorylated FAK Delocalizes from Focal Adhesions to Membrane Ruffles

1Laboratoire de Biophotonique et Pharmacologie, CNRS, UMR 7213, 74 rte du Rhin, 67401 Illkirch, France
2Faculté de Pharmacie, Université de Strasbourg, 67401 Illkirch, France

Received 15 February 2010; Revised 16 June 2010; Accepted 6 July 2010

Academic Editor: Geraldine M. O'Neill

Copyright © 2010 Abdelkader Hamadi et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Cell adhesion and migration are key determinants in tumor metastasis. Adherence of tumor cell to the extracellular matrix is mediated via integrin containing focal adhesions (FAs). Binding of integrins to ECM triggers phosphorylation of two major components of FAs, focal adhesion kinase (FAK) and Src, activating downstream signaling pathway which leads to FA disassembly and cell migration. In this paper, we analyze how phosphorylation of FAK regulates its trafficking at FAs in living human astrocytoma cells. Upon pervanadate-induced FAK phosphorylation, phosphorylated FAK appeared highly expressed at newly formed membrane ruffles. This effect was abolished in presence of the specific Src inhibitor PP2. Our findings demonstrate that upon phosphorylation, FAK delocalizes from FAs to membrane ruffles.