TYR527 IS PHOSPHORYLATED IN PP60C-SRC - IMPLICATIONS FOR REGULATION
TYR527 IS PHOSPHORYLATED IN PP60C-SRC - IMPLICATIONS FOR REGULATION
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DOI:
10.1126/science.2420005
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发表时间:
1986-03-21
期刊:
影响因子:
56.9
通讯作者:
HUNTER, T
中科院分区:
文献类型:
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作者:
COOPER, JA;GOULD, KL;HUNTER, T
The Rous sarcoma virus oncogene product, pp60v-src, transforms cultured fibroblasts but its corresponding proto-oncogene product, pp60c-src, does not. Both proteins are known to be protein-tyrosine kinases. Published results suggest that the kinase activity of pp60c-src is inhibited relative to that of pp60v-src, due perhaps to phosphorylation of a tyrosine in pp60c-src that is not phosphorylated in pp60v-src. In this study, it was observed that the tyrosine phosphorylated in pp60c-src is Tyr527, six residues from the COOH-terminus of the protein. The region of pp60c-src from residue 515 to the COOH-terminus, including Tyr527, has been replaced with a different sequence in pp60v-src. Thus, the increase in transforming ability and kinase activity that occurred in the genesis of pp60v-src may have resulted from the loss of a tyrosine involved in negative regulation.