Phosphorylation regulates the microtubule-destabilizing activity of stathmin and its interaction with tubulin

被引：73

作者：

DiPaolo, G

Antonsson, B

Kassel, D

Riederer, BM

Grenningloh, G

机构：

[1] UNIV LAUSANNE, INST BIOL CELLULAIRE & MORPHOL, CH-1005 LAUSANNE, SWITZERLAND

[2] GLAXO WELLCOME RES & DEV LTD, GENEVA BIOMED RES INST, CH-1228 PLAN LES OUATES, GENEVA, SWITZERLAND

[3] GLAXO INC, RES TRIANGLE PK, NC 27709 USA

来源：

FEBS LETTERS | 1997年 / 416卷 / 02期

基金：

美国国家科学基金会;

关键词：

stathmin; microtubule; cytoskeleton; phosphorylation;

D O I：

10.1016/S0014-5793(97)01188-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：149 / 152

页数：4

共 27 条

[1] Purification, characterization, and in vitro phosphorylation of the neuron-specific membrane-associated protein SCG10 [J].