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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Binding Sites
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Brain / ultrastructure
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Calcium-Calmodulin-Dependent Protein Kinases / metabolism
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Cell Cycle
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Cloning, Molecular
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Cross-Linking Reagents
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Cyclic AMP-Dependent Protein Kinases / metabolism
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Cyclin-Dependent Kinases / metabolism
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Humans
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Kinetics
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Microtubule Proteins*
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Microtubules / physiology*
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Microtubules / ultrastructure
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Phosphoproteins / metabolism*
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Phosphorylation
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Phosphoserine
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Proline
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Protein Kinases / metabolism*
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Recombinant Proteins / metabolism
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Serine
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Stathmin
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Swine
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Tubulin / metabolism*
Substances
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Cross-Linking Reagents
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Microtubule Proteins
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Phosphoproteins
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Recombinant Proteins
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STMN1 protein, human
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Stathmin
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Tubulin
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Phosphoserine
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Serine
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Proline
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Protein Kinases
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Cyclic AMP-Dependent Protein Kinases
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Calcium-Calmodulin-Dependent Protein Kinases
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Cyclin-Dependent Kinases