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. Author manuscript; available in PMC: 2010 Sep 1.
Published in final edited form as: Cell Signal. 2009 May 18;21(9):1423–1435. doi: 10.1016/j.cellsig.2009.05.006

Fig. 5. AND-34/BCAR3's SH2 and proline/serine-rich domains are required for induction of phosphorylation of p130Cas while its p130Cas-binding GEF-like domain is not.

Fig. 5

Panel A: Wildtype HA-AND-34, mutants lacking the SH2 domain (ΔSH2) or the carboxy-terminal 400 amino acids of AND-34 (SH2-PS), or a chimeric construct in which the SH2 domain and the proline/serine-rich domains of NSP3 were replaced by the corresponding domains of AND-34 (SH2PS/N3), were transfected into MCF-7 cells with HA-p130Cas. Either whole cell lysates or anti-p130Cas immunoprecipitates were then assessed by Western analysis with anti-HA to determine the ability of these AND-34 expression constructs or chimera to associate with p130Cas and to induce HA-p130Cas phosphorylation as judged by a reduction in PAGE mobility. Panel B: AND-34 mutants or chimeric expression constructs in which the SH2 domain, the proline/serine-rich domain or both domains of NSP3 were replaced with those of AND-34, were transfected along with an HA-p130Cas construct into MCF-7 cells. The ability of the AND-34 expression constructs to induce phosphorylation of p130Cas was assessed by Western analysis of whole cell lysates with anti-HA. Panel C: Cartoon depicting the HA-AND-34 mutants and the AND-34/NSP3 chimeras utilized in Panels A and B.