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Oncogene. 1996 Apr 4;12(7):1577-81.

SH3 domain-dependent interaction of the proto-oncogene product Vav with the focal contact protein zyxin.

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Department of Molecular Biology, Max-Planck-Institut für Biochemie, Martinsried, Germany.


Scr homology 3 (SH3) domain-mediated protein-protein interactions have been implicated in the localization of proteins to specific sites within the cell. We present evidence that the product of the vav proto-oncogene, p95vav, interacts specifically with the focal adhesion protein zyxin both in vitro and in yeast two hybrid system. Solution binding and two-hybrid system experiments demonstrate that association of Vav with the LIM domain protein zyxin is mediated by the C-terminal SH3 domain of the Vav and involves the proline-rich N-terminus of zyxin. The interaction appears to be selective, since no binding of the proline-rich N-terminus of zyxin with other SH3 domain-containing proteins such as GRB-2, phospholipase C gamma, GTPase-activating protein, or p85 was detected.

[Indexed for MEDLINE]

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