TY - JOUR
T1 - pp60c-src and related tyrosine kinases
T2 - A role in the assembly and reorganization of matrix adhesions
AU - Volberg, Tova
AU - Romer, Lewis
AU - Zamir, Eli
AU - Geiger, Benjamin
N1 - Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.
PY - 2001
Y1 - 2001
N2 - Activation of tyrosine kinases during integrin-mediated cell-matrix adhesion is involved both in the regulation of focal contact assembly and in the initiation of signaling processes at the cell-matrix adhesive interface. In order to determine the role of pp60c-src and related kinases in these processes, we have compared the dynamic reorganization of phosphotyrosine, vinculin, focal adhesion kinase and tensin in cells with altered expression of Src-family kinases. Both null cells for pp60c-src and triple knockout cells for pp60c-src, pp59fyn, and pp62c-src exhibited decreased phosphotyrosine levels in focal contacts when compared with wild-type cells. pp60c-src-null cells also exhibited faster assembly of cell-matrix adhesions and a more exuberant recruitment of FAK to these sites. Tensin, which normally segregates into fibrillar adhesions was localized in large focal contacts in the two mutant cell lines, suggesting involvement of pp60c-src in the segregation of focal contacts and fibrillar adhesions. Moreover, treatment of wild-type cells with tyrphostin AG1007, which inhibits both pp60c-src and FAK activity, induced accumulation of tensin in peripheral focal adhesions. These findings demonstrate that Src family kinases, and pp60c-src in particular, have a central role in regulating protein dynamics at cell-matrix interfaces, both during early stages of interaction and in mature focal contacts.
AB - Activation of tyrosine kinases during integrin-mediated cell-matrix adhesion is involved both in the regulation of focal contact assembly and in the initiation of signaling processes at the cell-matrix adhesive interface. In order to determine the role of pp60c-src and related kinases in these processes, we have compared the dynamic reorganization of phosphotyrosine, vinculin, focal adhesion kinase and tensin in cells with altered expression of Src-family kinases. Both null cells for pp60c-src and triple knockout cells for pp60c-src, pp59fyn, and pp62c-src exhibited decreased phosphotyrosine levels in focal contacts when compared with wild-type cells. pp60c-src-null cells also exhibited faster assembly of cell-matrix adhesions and a more exuberant recruitment of FAK to these sites. Tensin, which normally segregates into fibrillar adhesions was localized in large focal contacts in the two mutant cell lines, suggesting involvement of pp60c-src in the segregation of focal contacts and fibrillar adhesions. Moreover, treatment of wild-type cells with tyrphostin AG1007, which inhibits both pp60c-src and FAK activity, induced accumulation of tensin in peripheral focal adhesions. These findings demonstrate that Src family kinases, and pp60c-src in particular, have a central role in regulating protein dynamics at cell-matrix interfaces, both during early stages of interaction and in mature focal contacts.
KW - Cell-matrix adhesions
KW - Fibrillar adhesions
KW - Focal contracts
KW - Tensin
KW - Tyrosine phosphorylation
KW - pp60
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UR - http://www.scopus.com/inward/citedby.url?scp=0034941053&partnerID=8YFLogxK
M3 - Article
C2 - 11493667
AN - SCOPUS:0034941053
SN - 0021-9533
VL - 114
SP - 2279
EP - 2289
JO - Journal of cell science
JF - Journal of cell science
IS - 12
ER -