Phosphorylation regulates the microtubule-destabilizing activity of stathmin and its interaction with tubulin
Phosphorylation regulates the microtubule-destabilizing activity of stathmin and its interaction with tubulin
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DOI：
10.1016/s0014-5793(97)01188-5
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发表时间：
1997-10-20
期刊：
影响因子：
3.5
通讯作者：
Grenningloh, G
中科院分区：
文献类型：
--
作者：
DiPaolo, G;Antonsson, B;Grenningloh, G
Stathmin is a regulator of microtubule dynamics which undergoes extensive phosphorylation during the cell cycle as well as in response to various extracellular factors. Four serine residues are targets for protein kinases: Ser-25 and Ser-38 for proline-directed kinases such as mitogen-activated protein kinase and cyclin-dependent protein kinase, and Ser-16 and Ser-63 for cAMP-dependent protein kinase. We studied the effect of phosphorylation on the microtubule-destabilizing activity of stathmin and on its interaction with tubulin in vitro, We show that triple phosphorylation on Ser-16, Ser-25, and Ser-38 efficiently inhibits its activity and prevents its binding to tubulin. (C) 1997 Federation of European Biochemical Societies.
