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Networks of interaction of p120(cbl) and p130(cas) with Crk and Grb2 adaptor proteins

Khwaja, A; Hallberg, B; Warne, PH; Downward, J; (1996) Networks of interaction of p120(cbl) and p130(cas) with Crk and Grb2 adaptor proteins. ONCOGENE , 12 (12) 2491 - 2498.

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Abstract

P120(cbl), the product of the c-cbl proto-oncogene, has previously been shown to become tyrosine phosphorylated following EGF stimulation of cells, and to bind constitutively to the SH3 domain of the adaptor protein Grb2. Here we show that another adaptor protein, Crk, binds through its SH2 domain to tyrosine phosphorylated p120(cbl). In addition, Crk becomes phosphorylated on tyrosine and serine following EGF treatment of PC12 and other cell lines. In unstimulated cells, while Grb2 is not bound to any tyrosine phosphoprotein, Crk is bound via its SH2 domain to tyrosine phosphorylated p130(cas), the Crk-associated v-Src substrate. Following EGF treatment, Crk dissociates from p130(cas), possibly due to a higher affinity of Crk SH2 for p120(cbl) compared with p130(cas). Interaction between Grb2 and p120(cbl) increases threefold following EGF treatment of cells; in vitro, this induction of Grb2 association with unphosphorylated p120(cbl) can be mimicked by the addition of tyrosine phosphorylated She, suggesting a transfer of information between the SH2 and SH3 domains of Grb2. These data indicate that adaptor proteins can exchange binding partners in response to stimuli, and that different adaptor proteins can bind to the same partners by different mechanisms.

Type: Article
Title: Networks of interaction of p120(cbl) and p130(cas) with Crk and Grb2 adaptor proteins
Keywords: Cb1, Grb2, Crk, oncogene, tyrosine phosphorylation, RECEPTOR TYROSINE KINASES, V-CBL ONCOGENE, SH3 DOMAINS, IDENTIFICATION, TRANSFORMATION, ASSOCIATION, TRUNCATION, BINDS, CELLS
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Cancer Institute
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Cancer Institute > Research Department of Haematology
URI: http://discovery.ucl.ac.uk/id/eprint/88696
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