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首页> 外文期刊>Molecular and Cellular Biology >Mutation of amino acids in pp60c-src that are phosphorylated by protein kinases C and A.
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Mutation of amino acids in pp60c-src that are phosphorylated by protein kinases C and A.

机译：pp60c-src中被蛋白激酶C和A磷酸化的氨基酸突变。

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The product of the c-src proto-oncogene, pp60c-src, is phosphorylated at Ser-17 by cyclic AMP-dependent protein kinase A and at Ser-12 by calcium-phospholipid-dependent protein kinase C (when stimulated by 12-O-tetradecanoyl phorbol acetate). We tested the effects of Ser----Ala and Ser----Glu mutations at these sites in pp60c-src and in pp60c-src(F527) (a mutant whose transforming activities are enhanced by Tyr-527----Phe mutation) by transfecting single-, double-, and triple-mutant src expression plasmids into NIH 3T3 cells. Tryptic phosphopeptide analyses of the mutant proteins confirmed prior biochemical identifications of the phosphorylation sites and showed that neither separate nor coordinate mutations at Ser-12 and Ser-17 affected Tyr-416, Tyr-527, or Ser-48 phosphorylation or prevented mitosis-specific phosphorylations of either pp60c-src or pp60c-src(F527). Ser-12 mutation did not affect phosphorylation of the Ser-17-containing peptide, but mutation of Ser-17 significantly increased phosphorylation at Ser-12. Specific kinase activities (both with and without in vivo 12-O-tetradecanoyl phorbol acetate treatment) and the abilities of pp60c-src and pp60c-src(F527) to induce foci, transformed morphologies, and anchorage-independent growth were unaffected by any of the serine mutations. Thus, pp60c-src transforming activity in NIH 3T3 cells is relatively insensitive to phosphorylation at these sites, but there is a suggestion that Ser-17 phosphorylation may have a subtle regulatory effect.
机译：c-src原癌基因产物pp60c-src在SER-17处被环AMP依赖性蛋白激酶A磷酸化，在Ser-12处被钙磷脂依赖性蛋白激酶C磷酸化（当受12-O刺激时） -十四烷酰佛波醇乙酸酯）。我们在pp60c-src和pp60c-src（F527）（通过Tyr-527 ----增强转化活性的突变体----）的这些位点上测试了Ser ---- Ala和Ser ---- Glu突变的作用将单，双和三突变src表达质粒转染到NIH 3T3细胞中。突变蛋白的胰蛋白酶磷酸肽分析证实了先前对磷酸化位点的生化鉴定，并表明Ser-12和Ser-17上的单独突变或不协调的突变都不会影响Tyr-416，Tyr-527或Ser-48磷酸化或防止有丝分裂特异性pp60c-src或pp60c-src的磷酸化（F527）。 Ser-12突变不会影响含Ser-17的肽的磷酸化，但Ser-17的突变会显着增加Ser-12的磷酸化。特定的激酶活性（有或没有体内12-O-十四烷酰佛波酯乙酸盐处理）以及pp60c-src和pp60c-src（F527）诱导病灶，转化形态和锚定非依赖性生长的能力不受以下任何因素的影响丝氨酸突变。因此，NIH 3T3细胞中的pp60c-src转化活性对这些位点的磷酸化相对不敏感，但有人暗示Ser-17磷酸化可能具有微妙的调节作用。

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