Phosphorylation of dynamin by ERK2 inhibits the dynamin-microtubule interaction.
In the present study we show that purified bovine brain dynamin can be phosphorylated by MAP kinase, ERK2, with a stoichiometry of 1 mol phosphate/mol dynamin. The phosphorylated serine residue is located within the C-terminal 10 kDa of dynamin. Dynamin I phosphorylated by ERK2 can be specifically dephosphorylated by calcineurin but not by protein phosphatase 2A (PP2A). Phosphorylation of dynamin by ERK2 weakens the binding of dynamin to microtubules and inhibits dynamin's microtubule-activated GTPase activity. Stimulation of GTPase activity by either Grb2 or phospholipids was not affected by ERK2 phosphorylation, suggesting that the binding sites for Grb2 and phospholipids do not overlap with that for microtubules.
Earnest
S
S
Department of Pharmacology, U.T. Southwestern Medical Center at Dallas, TX 75235-9041, USA.
Khokhlatchev
A
A
Albanesi
J P
JP
Barylko
B
B
D001665:Binding Sites; D019703:Calcineurin; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000378:metabolism*; D002148:Calmodulin-Binding Proteins / Q000378:metabolism; D034284:Dynamin I; D034281:Dynamins; D020558:GTP Phosphohydrolases / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism*; D019950:Mitogen-Activated Protein Kinase 1; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D010766:Phosphorylation; D054648:Protein Phosphatase 2
D002148:Calmodulin-Binding Proteins; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D019950:Mitogen-Activated Protein Kinase 1; D019703:Calcineurin; D010749:Phosphoprotein Phosphatases; D054648:Protein Phosphatase 2; D034284:Dynamin I; D020558:GTP Phosphohydrolases; D034281:Dynamins