通过p34cdc2-关联蛋白激酶对p60c-src进行线性酸化
D O Morgan1, J M Kaplan, J M Bishop
1Department of Microbiology, University of California, San Francisco 94143.
Cell
|June 2, 1989
概括
在细胞分裂过程中,一种新型的突变特异性蛋白质激酶化了p60c-src在氨酸上. 这种激酶活性与p34cdc2有关,这表明p60c-src在线粒分裂中起到p34cdc2的作用.
科学领域:
- 细胞生物学 细胞生物学
- 分子生物学分子生物学
- 生物化学 生物化学
背景情况:
- p60c-src是一种蛋白质-铁氨酸激酶,在线粒分裂过程中在其氨基末端区域经历了三氨酸酸化.
- 确定负责这种特定的线粒体酸化的激酶对于理解细胞循环调节至关重要.
研究的目的:
- 为了识别和描述负责p60c-src的线性特异性三氨酸酸化的蛋白质激酶.
- 调查这种激酶活性与已知的线粒调节剂,特别是p34cdc2.2.c之间的关系.
主要方法:
- 来自HeLa细胞和Xenopus蛋的线粒细胞提取物被用于寻找酶活性.
- 用纯化的p60c-src进行了体外酸化试验.
- 用三式光图绘制来分析酸化部位.
- 凝过色谱被用于评估酶共聚.
- 使用对p34cdc2的抗体进行免疫减弱.
主要成果:
- 在HeLa细胞和Xenopus蛋中确定了一种特定于线粒分裂的蛋白激酶活性,能够在体外氧化p60c-src在氨酸残留物上.
- 类的测绘证实,鉴定到的酶酸化了与化过程中在体内修饰的同一个位点.
- 线性HeLa激酶活性与p34cdc2-关联的素H1激酶结合.
- 对p34cdc2的抗体削弱了来自线粒体提取物的p60c-src-酸化活性.
结论:
- 结果确定了一种新的线粒分裂特异性激酶,该激酶在氨酸上酸化p60c-src.
- 这种激酶活性与p34cdc2相关,表明存在功能联系.
- p60c-src可能在特定的线粒体过程中起到p34cdc2的作用,有助于细胞循环调节.
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