| Literature DB >> 15649133 |
Karen J Smillie1, Michael A Cousin.
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.Entities:
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Year: 2005 PMID: 15649133 PMCID: PMC2077358 DOI: 10.1042/bss0720087
Source DB: PubMed Journal: Biochem Soc Symp ISSN: 0067-8694