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

FEBS Letters

Grenningloh, Gabriele²  Kassel, Daniel³  Riederer, Beat M²  Di Paolo, Gilbert²  Antonsson, Bruno¹ 

[1]Geneva Biomedical Research Institute, Glaxo Wellcome Research and Development S.A., 1228 Plan-les-Ouates, Geneva, Switzerland

[2]Institut de Biologie Cellulaire et de Morphologie, University of Lausanne, Rue du Bugnon 9, 1005 Lausanne, Switzerland

[3]Glaxo Inc., Research Triangle Park, NC 27709, USA

关键词: Stathmin;    Microtubule;    Cytoskeleton;    Phosphorylation;    MAP kinase;    mitogen-activated protein kinase;    MAPs;    microtubule-associated proteins;    PKA;    cAMP-dependent protein kinase;    MT;    microtubules;    mAB;    monoclonal antibody;    PAGE;    polyacrylamide gel electrophoresis;    EDC;    1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide;   

DOI  :  10.1016/S0014-5793(97)01188-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown