Crossref journal-article
Wiley
FEBS Letters (311)
Abstract

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.

Bibliography

Di Paolo, G., Antonsson, B., Kassel, D., Riederer, B. M., & Grenningloh, G. (1997). Phosphorylation regulates the microtubule‐destabilizing activity of stathmin and its interaction with tubulin. FEBS Letters, 416(2), 149–152. Portico.

Dates
Type When
Created 23 years ago (July 25, 2002, 3:16 p.m.)
Deposited 1 year, 11 months ago (Sept. 16, 2023, 6:08 a.m.)
Indexed 3 weeks, 3 days ago (July 30, 2025, 10:04 a.m.)
Issued 27 years, 10 months ago (Oct. 20, 1997)
Published 27 years, 10 months ago (Oct. 20, 1997)
Published Online 27 years, 8 months ago (Nov. 25, 1997)
Published Print 27 years, 10 months ago (Oct. 20, 1997)
Funders 0

None

@article{Di_Paolo_1997, title={Phosphorylation regulates the microtubule‐destabilizing activity of stathmin and its interaction with tubulin}, volume={416}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/s0014-5793(97)01188-5}, DOI={10.1016/s0014-5793(97)01188-5}, number={2}, journal={FEBS Letters}, publisher={Wiley}, author={Di Paolo, Gilbert and Antonsson, Bruno and Kassel, Daniel and Riederer, Beat M and Grenningloh, Gabriele}, year={1997}, month=oct, pages={149–152} }