Dynamin I phosphorylation and the control of synaptic vesicle endocytosis

Karen J. Smillie, Michael A. Cousin*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

Abstract / Description of output

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.

Original languageEnglish
Pages (from-to)87-97
Number of pages11
JournalBiochemical Society Symposium
Publication statusPublished - 2005


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