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Phosphorylation regulates the microtubule‐destabilizing activity of stathmin and its interaction with tubulin
Author(s) -
Di Paolo Gilbert,
Antonsson Bruno,
Kassel Daniel,
Riederer Beat M,
Grenningloh Gabriele
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01188-5
Subject(s) - stathmin , phosphorylation , kinase , microtubule , microbiology and biotechnology , tubulin , protein kinase a , phosphorylation cascade , protein phosphorylation , chemistry , cyclin dependent kinase 2 , cyclin dependent kinase 5 , cyclin dependent kinase , biology , biochemistry , cell cycle , cell
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.