Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae.

S M Murphy; M Bergman; D O Morgan

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Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae.

机译：C端Src激酶抑制c-Src活性涉及c-Src SH2和SH3结构域：用酿酒酵母进行分析。

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The kinase activity of c-Src is normally repressed in vertebrate cells by extensive phosphorylation of Y-527. C-terminal Src kinase (CSK) is a candidate for the enzyme that catalyzes this phosphorylation. We have used budding yeast to study the regulation of c-Src activity by CSK in intact cells. Expression of c-Src in Saccharomyces cerevisiae, which lacks endogenous c-Src and Y-527 kinases, induces a kinase-dependent growth inhibition. Coexpression of CSK in these cells results in phosphorylation of c-Src on Y-527 and suppression of the c-Src phenotype. CSK does not fully suppress the activity of c-Src mutants lacking portions of the SH2 or SH3 domains, even though these mutant proteins are phosphorylated on Y-527 by CSK both in vivo and in vitro. These results suggest that both the SH2 and SH3 domains of c-Src are required for the suppression of c-Src activity by Y-527 phosphorylation.

机译：在脊椎动物细胞中，通常通过Y-527的广泛磷酸化来抑制c-Src的激酶活性。 C端Src激酶（CSK）是催化这种磷酸化的酶的候选物。我们已经使用出芽酵母来研究CSK在完整细胞中对c-Src活性的调节。缺乏内源性c-Src和Y-527激酶的酿酒酵母中c-Src的表达诱导了激酶依赖性的生长抑制。这些细胞中CSK的共表达导致c-Src在Y-527上的磷酸化和c-Src表型的抑制。 CSK不能完全抑制缺少SH2或SH3结构域部分的c-Src突变体的活性，即使这些突变体蛋白在体内和体外都被CSK在Y-527上磷酸化了。这些结果表明，c-Src的SH2和SH3结构域都是通过Y-527磷酸化抑制c-Src活性所必需的。

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《Molecular and Cellular Biology》 |1993年第9期|共11页
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S M Murphy; M Bergman; D O Morgan;
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1. IN VITRO PHOSPHORYLATION OF THE EPIDERMAL GROWTH FACTOR RECEPTOR AUTOPHOSPHORYLATION DOMAIN BY C-SRC - IDENTIFICATION OF PHOSPHORYLATION SITES AND C-SRC SH2 DOMAIN BINDING SITES [J] . Lombardo CR, Consler TG, Kassel DB Biochemistry . 1995,第50期

机译：C-SRC体外表皮生长因子受体自磷酸化域的磷酸化-磷酸化位点和C-SRC SH2结合位点的鉴定
2. The N2-Src neuronal splice variant of C-Src has altered SH3 domain ligand specificity and a higher constitutive activity than N1-Src [J] . Keenan Sarah, Lewis Philip A., Wetherill Sarah J., FEBS letters. . 2015,第15期

机译：C2-Src的N2-Src神经元剪接变体比N1-Src改变了SH3域配体的特异性并具有更高的组成活性
3. Molecular basis for the interaction between human choline kinase alpha and the SH3 domain of the c-Src tyrosine kinase [J] . Stefanie L. Kall, Kindra Whitlatch, Thomas E. Smithgall, Scientific reports. . 2019,第1期

机译：对C-SRC酪氨酸激酶的人胆碱激酶α和SH3结构域之间的相互作用的分子基础
4. Development of peptidomimetic substrates and inhibitors that bind to the peptide binding pocket of the catalytic site of p60~(C-src) protein tyrosine kinase [C] . Jayesh R.Kamath, Ruiwu Liu, Amanda M.Enstrom, the International Peptide Symposium . 2001

机译：拟肽底物和抑制剂的研制与P60〜（C-SRC）蛋白酪氨酸激酶催化位点的肽结合口袋结合
5. Dioxin toxicology: A study of C-SRC kinase and tyrosine phosphatase activities associated with the AH receptor. [D] . Remillard, Rene Bernard Joseph. 2001

机译：二恶英毒理学：与AH受体相关的C-SRC激酶和酪氨酸磷酸酶活性的研究。
6. Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae. [O] . S M Murphy, M Bergman, D O Morgan 1985

机译：C末端Src激酶抑制c-Src活性涉及c-Src SH2和SH3结构域：用酿酒酵母进行分析。
7. Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae. [O] . Murphy, S M, Bergman, M, Morgan, D O 1993

机译：C末端Src激酶抑制c-Src活性涉及c-Src SH2和SH3结构域：用酿酒酵母进行分析。

Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae.

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