Mutations in v-Src SH3 and catalytic domains that jointly confer temperature-sensitive transformation with minimal temperature-dependent changes in cellular tyrosine phosphorylation.

Abstract excerpt

We have analyzed two functionally significant amino acid alterations encoded by the temperature-sensitive (ts) v-src mutant of Rous sarcoma virus, LA32. The G-to-V change at residue 300 in the catalytic domain nonconditionally impairs morphological transformation, in vitro kinase activity, in vivo tyrosine phosphorylation, and the cytoskeletal association of v-Src while rendering anchorage- and serum-independent...

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