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

Abstract

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.

050100'98'00'02'04'06'08'10'12'14'16
Citations per Year

412 Citations

Semantic Scholar estimates that this publication has 412 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{Hobert1996SH3DI, title={SH3 domain-dependent interaction of the proto-oncogene product Vav with the focal contact protein zyxin.}, author={Oliver Hobert and James W. Schilling and Mary C. Beckerle and Angelika Ullrich and Bahija Jallal}, journal={Oncogene}, year={1996}, volume={12 7}, pages={1577-81} }