By A.R. Bellve (Eds.)

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Given the difference in biological activity between pp60 v s r c and pp60 c s r c , one would predict that there must be discernible biochemical differences between these proteins. pp60 v_src does, in fact, prove to have considerably greater protein kinase activity than pp60 c_src both in vitro and in vivo (9,10), and there is every reason to believe that the increased protein kinase activity is responsible for its transforming activity. This difference in activity is now realized to be due in part to the C-terminal truncation of pp60 c s r c and the resultant loss of a negative regulatory tyrosine phosphorylation site present in pp60 c_src (5).

Yonemoto and J. S. Brugge, personal communication). We find that this tyrosine phosphorylation site differs from that in pp60 c s r c isolated from PDGF-treated cells. Whether this tyrosine phosphorylation plays any role in the activation of pp60c~src is unclear, since the bulk of pp60 c s r c associated with mT antigen is not phosphorylated at this site. Nevertheless the mutation of Tyr-90 to Phe converts pp60c~src to a transforming protein, suggesting that this region of pp60 c s r c may have a regulatory function.

All three different pp60 v_src species lack the region containing Tyr-527 and are therefore not subject to negative regulation (5). This would 4. PHOSPHORYLATION OF pp60 c s r c 33 explain their increased protein kinase activity, which in turn is essential for the transforming activity of pp60 v_src . Likewise, the increased protein kinase activity of the Phe-527 mutant of pp60 c s r c is presumably responsible for its ability to transform NIH 3T3 cells. This negative regulation model for pp60 c s r c raises the critical question of how Tyr-527 is phosphorylated and how it inhibits protein kinase activity.

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