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Phosphorylation of dynamin by cdc2 kinase
H Hosoya1, S Komatsu, T Shimizu
1Department of Biological Science, Faculty of Science, Hiroshima University, Japan.
Biochemical and Biophysical Research Communications
|July 29, 1994
Summary
Phosphorylation of the microtubule-bundling protein dynamin by cdc2 kinase significantly impairs its ability to bind microtubules. This key modification occurs at a specific serine residue, affecting microtubule dynamics.
Area of Science:
- Cell Biology
- Molecular Biology
- Protein Biochemistry
Background:
- Dynamin is a crucial microtubule-bundling protein involved in cellular processes.
- Protein phosphorylation is a key regulatory mechanism in cell signaling.
- cdc2 kinase is a critical regulator of the cell cycle.
Purpose of the Study:
- To investigate the effect of cdc2 kinase-mediated phosphorylation on dynamin's microtubule-binding activity.
- To identify the specific site of phosphorylation on dynamin.
Main Methods:
- In vitro phosphorylation assays using purified dynamin and cdc2 kinase.
- Quantification of phosphate incorporation into dynamin.
- Assessment of dynamin's microtubule-binding ability following phosphorylation.
Main Results:
- Dynamin was phosphorylated by cdc2 kinase, with approximately 1 mole of phosphate incorporated per mole of dynamin.
- Phosphorylation occurred at a specific serine residue.
- The phosphorylation significantly reduced dynamin's binding affinity for microtubules.
Conclusions:
- Serine residue phosphorylation by cdc2 kinase negatively regulates dynamin's microtubule-binding function.
- This regulatory mechanism may play a role in controlling microtubule dynamics during the cell cycle.