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Phosphorylation regulates the microtubule-destabilizing activity of stathmin and its interaction with tubulin.
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.
Animals, Binding Sites, Brain/ultrastructure, Calcium-Calmodulin-Dependent Protein Kinases/metabolism, Cell Cycle, Cloning, Molecular, Cross-Linking Reagents, Cyclic AMP-Dependent Protein Kinases/metabolism, Cyclin-Dependent Kinases/metabolism, Humans, Kinetics, Microtubule Proteins, Microtubules/physiology, Microtubules/ultrastructure, Phosphoproteins/metabolism, Phosphorylation, Phosphoserine, Proline, Protein Kinases/metabolism, Recombinant Proteins/metabolism, Serine, Stathmin, Swine, Tubulin/metabolism
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