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(Received for publication, December 22, 1995, and in revised form, March 21, 1996)
,
,
and¶
From the Molecular Oncology Group, Royal Victoria Hospital,
Departments of The Tpr-Met oncoprotein, which is a member of a
family of tyrosine kinase oncoproteins generated following genomic
rearrangement, consists of the catalytic kinase domain of the
hepatocyte growth factor/scatter factor receptor tyrosine kinase (Met)
fused downstream from sequences encoded by the tpr gene. We
have previously demonstrated that a single tyrosine residue in the
carboxyl terminus, Tyr489, is highly phosphorylated and is
essential for efficient transformation of Fr3T3 fibroblasts by Tpr-Met
and for the association of Tpr-Met with the Grb2 adaptor protein and
phosphatidylinositol 3
Medicine,
Oncology, and ¶ Biochemistry, McGill
University, Montreal, Quebec, H3A 1A1 Canada
-kinase. We show here that Tyr489 is
also required for association of Tpr-Met with phospholipase C
and
the tyrosine phosphatase, SHPTP2/Syp. To distinguish which of these
substrates are required for cell transformation by the Tpr-Met
oncoprotein, we generated a novel Tpr-Met mutant that selectively fails
to associate with the Grb2 adaptor protein. Utilizing this mutant,
together with additional Tpr-Met mutants containing Tyr to Phe
substitutions, we have demonstrated that transformation of Fr3T3
fibroblasts by the Tpr-Met oncoprotein is dependent upon pathways
downstream of Shc and Grb2 and that pathways downstream of
phosphatidylinositol 3-kinase, phospholipase C, and
SHPTP2/Syp are insufficient for transformation.
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