Abstract

P130Cas is a major Src substrate in cell‐ECM adhesions implicated in cell motility. The objective of this study was to measure the dynamics of p130Cas localization to adhesions, while also assessing domain requirements for this targeting. Variants of YFP‐tagged p130Cas were stably expressed in p130Cas‐null fibroblasts. In addition to full‐length p130Cas, deletion mutants lacking either the SH3 domain or the highly conserved "Cas‐family C‐terminal homology" (CCH) domain were analyzed. Total internal reflection fluorescence microscopy of live cells revealed that p130Cas localizes to adhesions with a kinetic profile similar to paxillin ‐ a standard marker for monitoring adhesion dynamics. Variants lacking either the SH3 or CCH domain localized poorly to adhesions, while deletion of both domains completely abrogated the localization. The CCH domain was also found to be sufficient for adhesion targeting. Deletion of the CCH domain was further linked to defects in p130Cas tyrosine phosphorylation and wound healing cell migration. Thus both the SH3 and CCH domains play important roles in p130Cas adhesion site targeting and this localization is critical for p130Cas signaling leading to cell motility.

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