Dynamin I phosphorylation and the control of synaptic vesicle endocytosis |
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Authors: | Smillie Karen J Cousin Michael A |
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Affiliation: | Membrane Biology Group, Division of Biomedical Sciences, University of Edinburgh, George Square, Edinburgh EH8 9XD, U.K. |
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Abstract: | 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. |
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