CHARACTERIZATION OF SITES FOR TYROSINE PHOSPHORYLATION IN THE TRANSFORMING PROTEIN OF ROUS-SARCOMA VIRUS (PP60V-SRC) AND ITS NORMAL CELLULAR HOMOLOG (PP60C-SRC)
CHARACTERIZATION OF SITES FOR TYROSINE PHOSPHORYLATION IN THE TRANSFORMING PROTEIN OF ROUS-SARCOMA VIRUS (PP60V-SRC) AND ITS NORMAL CELLULAR HOMOLOG (PP60C-SRC)
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DOI：
10.1073/pnas.78.10.6013
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发表时间：
1981-01-01
期刊：
影响因子：
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通讯作者：
BISHOP, JM
中科院分区：
文献类型：
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作者：
SMART, JE;OPPERMANN, H;BISHOP, JM
劳斯肉瘤病毒的转化蛋白（pp 60 v-src）及其正常细胞同源物（pp 60 c-src）似乎是在多种蛋白底物中磷酸化酪氨酸的蛋白激酶。此外，pp 60 v-src和pp 60 c-src本身在丝氨酸和酪氨酸上被磷酸化。这些磷酸化似乎调节pp 60 v-src和pp 60 c-src的功能。对这两种蛋白质的酪氨酸磷酸化位点进行了表征。感染细胞中pp 60 v-src的酪氨酸磷酸化主要发生在（如果不是全部的话）蛋白质的推导氨基酸序列中的残基419处。围绕该残基的是序列Leu-Ile-Glu-Asp-Asn-Glu-Tyr（P）-Thr-Ala-Arg。这种肽的区别在于磷酸化酪氨酸之前的4个氨基酸中有3个是酸性的。这些结果定义了什么可能被证明是一个广泛使用的网站酪氨酸磷酸化的调节细胞功能。当部分纯化的pp 60 v-src用于体外磷酸转移反应时，相同的位点被磷酸化。pp 60 c-src的结果更为复杂。体外酪氨酸磷酸化位点与pp 60 v-src相同。pp 60 c-src在体内的磷酸化显然发生在不同的，目前尚未确定的酪氨酸残基。PP 60 V-SRC和PP 60 C-SRC对完整细胞中的调节影响的反应明显不同。
The transforming protein of Rous sarcoma virus (pp60v-src) and its normal cellular homologue (pp60c-src appear to be protein kinases that phosphorylate tyrosine in a variety of protein substrates. In addition, pp60v-src and pp60c-src and are themselves phosphorylated on serine and tyrosine. These phosphorylations seem to regulate the function(s) of pp60v-src and pp60c-src. The sites of tyrosine phosphorylation in the 2 proteins were characterized. Tyrosine phosphorylation of pp60v-src in infected cells occurs mainly (if not entirely) at residue 419 in the deduced amino acid sequence of the protein. Surrounding this residue is the sequence Leu-Ile-Glu-Asp-Asn-Glu-Tyr(P)-Thr-Ala-Arg. This peptide is distinguished by the fact that 3 of 4 amino acids that precede the phosphorylated tyrosine are acidic in nature. These results define what may prove to be a widely used site for tyrosine phosphorylation in the regulation of cellular function. The same site was phosphorylated when partially purified pp60v-src was used in a phosphotransfer reaction in vitro. The results with pp60c-src were more complex. The site of tyrosine phosphorylatieon in vitro appeared to be the same as that found in pp60v-src. Phosphorylation of pp60c-src in vivo apparently occurred at a different, and currently unidentified tyrosine residue. pp60v-src and pp60c-src apparently respond differently to regulatory influences in the intact cell.