Abstract：
:A mutant in src, the oncogene of Rous sarcoma virus, has been constructed in which the major phosphorylated tyrosine (Tyr-416, located in the carboxy-terminal half of the protein) has been replaced by phenylalanine. Mouse cells transformed with this mutant src form foci and grow in soft agar, indicative of a transformed state. Also, the mutant protein retains the wild-type ability to phosphorylate proteins on tyrosine. Partial proteolysis revealed that the carboxy-terminal half of the mutant protein was still phosphorylated, although apparently to a lesser extent. Analysis indicated that this residual phosphorylation was on tyrosine. We conclude that the major tyrosine phosphorylation in pp60v-src is not required for two of the protein's notable properties--protein kinase activity and transformation of cultured cells.
journal_name
Celljournal_title
Cellauthors
Snyder MA,Bishop JM,Colby WW,Levinson ADdoi
10.1016/0092-8674(83)90074-0subject
Has Abstractpub_date
1983-03-01 00:00:00pages
891-901issue
3eissn
0092-8674issn
1097-4172pii
0092-8674(83)90074-0journal_volume
32pub_type
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