Phosphorylation of dynamin by cdc2 kinase.
A 100kD microtubule-bundling protein dynamin was phosphorylated in vitro by cdc2 kinase to approximately 1 mol of phosphate/mol of dynamin at a serine residue. These phosphorylations of dynamin greatly reduced its binding ability to microtubules.
Hosoya
H
H
Department of Biological Science, Faculty of Science, Hiroshima University, Japan.
Komatsu
S
S
Shimizu
T
T
Inagaki
M
M
Ikegami
M
M
Yazaki
K
K
D000818:Animals; D001665:Binding Sites; D001923:Brain Chemistry; D016203:CDC2 Protein Kinase / Q000378:metabolism*; D034281:Dynamins; D004591:Electrophoresis, Polyacrylamide Gel; D020558:GTP Phosphohydrolases / Q000737:chemistry / Q000378:metabolism*; D006367:HeLa Cells / Q000201:enzymology; D006801:Humans; D008854:Microscopy, Electron; D008870:Microtubules / Q000378:metabolism; D010710:Phosphates / Q000378:metabolism*; D010766:Phosphorylation; D010768:Phosphoserine / Q000378:metabolism; D051381:Rats
D010710:Phosphates; D010768:Phosphoserine; D016203:CDC2 Protein Kinase; D020558:GTP Phosphohydrolases; D034281:Dynamins