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.
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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) |
@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} }