微管蛋白通过ATP和GTP进行的差异磷酸化作用。
Differential phosphorylation of microtubule proteins by ATP and GTP.
作者信息
Diaz-Nido J, Serrano L, Avila J
机构信息
Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma, Madrid, Spain.
出版信息
Mol Cell Biochem. 1988 Jan;79(1):73-9. doi: 10.1007/BF00229400.
PMID:3374479
Abstract
Purified brain microtubule protein is phosphorylated by endogenous protein kinase activities in the presence of [gamma-32P] ATP or [gamma-32P] GTP. Here we show that certain microtubule-associated proteins are phosphorylated differently by GTP or ATP as direct phosphoryl donors, suggesting the presence of distinct kinase activities, with different specificities, associated with microtubule protein.
摘要
在[γ-32P]ATP或[γ-32P]GTP存在的情况下，纯化的脑微管蛋白可被内源性蛋白激酶活性磷酸化。在此我们表明，某些微管相关蛋白作为直接磷酸供体，被GTP或ATP磷酸化的方式不同，这表明与微管蛋白相关的存在具有不同特异性的独特激酶活性。
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