Dynamin I phosphorylation and the control of synaptic vesicle endocytosis.
The GTPase dynamin I is essential for synaptic vesicle endocytosis in nerve terminals. It is a nerve terminal phosphoprotein that is dephosphorylated on nerve terminal stimulation by the calcium-dependent protein phosphatase calcineurin and then rephosphorylated by cyclin-dependent kinase 5 on termination of the stimulus. Because of its unusual phosphorylation profile, the phosphorylation status of dynamin I was assumed to be inexorably linked to synaptic vesicle endocytosis; however, direct proof of this link has been elusive until very recently. This review will describe current knowledge regarding dynamin I phosphorylation in nerve terminals and how this regulates its biological function with respect to synaptic vesicle endocytosis.
Smillie
Karen J
KJ
Membrane Biology Group, Division of Biomedical Sciences, University of Edinburgh, George Square, Edinburgh EH8 9XD, U.K.
Cousin
Michael A
MA
D000595:Amino Acid Sequence; D000818:Animals; D019703:Calcineurin / Q000378:metabolism; D051360:Cyclin-Dependent Kinase 5; D018844:Cyclin-Dependent Kinases / Q000378:metabolism; D034284:Dynamin I / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004705:Endocytosis / Q000502:physiology*; D006801:Humans; D008959:Models, Neurological; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010766:Phosphorylation; D017434:Protein Structure, Tertiary; D013572:Synaptic Vesicles / Q000502:physiology*
D051360:Cyclin-Dependent Kinase 5; C495905:CDK5 protein, human; D018844:Cyclin-Dependent Kinases; D019703:Calcineurin; D034284:Dynamin I