TY - JOUR
T1 - Direct association between the Ret receptor tyrosine kinase and the Src homology 2-containing adapter protein Grb7
AU - Pandey, Akhilesh
AU - Liu, Xin
AU - Dixon, Jack E.
AU - Di Fiore, Pier Paolo
AU - Dixit, Vishva M.
PY - 1996
Y1 - 1996
N2 - Adapter proteins containing Src homology 2 (SH2) domains link transmembrane receptor protein-tyrosine kinases to downstream signal transducing molecules. A family of SH2 containing adapter proteins including Grb7 and Grb10 has been recently identified. We had previously shown that Grb10 associates with Ret via its SH2 domain in an activation-dependent manner (Pandey, A., Duan, H., Di Fiore, P. P., and Dixit, V. M. (1995) J. Biol. Chem. 270, 21461-21463). We now demonstrate that the related adapter molecule Grb7 also associates with Ret in vitro and in vivo, and that the binding of the SH2 domain of Grb7 to Ret is direct. This binding is dependent upon Ret autophosphorylation since Grb7 is incapable of binding a kinase- defective mutant of Ret. Thus two members of the Grb family, Grb7 and Grb10, likely relay signals emanating from Ret to other, as yet, unidentified targets within the cell.
AB - Adapter proteins containing Src homology 2 (SH2) domains link transmembrane receptor protein-tyrosine kinases to downstream signal transducing molecules. A family of SH2 containing adapter proteins including Grb7 and Grb10 has been recently identified. We had previously shown that Grb10 associates with Ret via its SH2 domain in an activation-dependent manner (Pandey, A., Duan, H., Di Fiore, P. P., and Dixit, V. M. (1995) J. Biol. Chem. 270, 21461-21463). We now demonstrate that the related adapter molecule Grb7 also associates with Ret in vitro and in vivo, and that the binding of the SH2 domain of Grb7 to Ret is direct. This binding is dependent upon Ret autophosphorylation since Grb7 is incapable of binding a kinase- defective mutant of Ret. Thus two members of the Grb family, Grb7 and Grb10, likely relay signals emanating from Ret to other, as yet, unidentified targets within the cell.
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U2 - 10.1074/jbc.271.18.10607
DO - 10.1074/jbc.271.18.10607
M3 - Article
C2 - 8631863
AN - SCOPUS:15844375862
SN - 0021-9258
VL - 271
SP - 10607
EP - 10610
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 18
ER -