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Cdk5 is essential for synaptic vesicle endocytosis

Abstract

Synaptic vesicle endocytosis (SVE) is triggered by calcineurin-mediated dephosphorylation of the dephosphin proteins. SVE is maintained by the subsequent rephosphorylation of the dephosphins by unidentified protein kinases. Here, we show that cyclin-dependent kinase 5 (Cdk5) phosphorylates dynamin I on Ser 774 and Ser 778 in vitro, which are identical to its endogenous phosphorylation sites in vivo. Cdk5 antagonists and expression of dominant-negative Cdk5 block phosphorylation of dynamin I, but not of amphiphysin or AP180, in nerve terminals and inhibit SVE. Thus Cdk5 has an essential role in SVE and is the first dephosphin kinase identified in nerve terminals.

Type Journal
ISBN 1465-7392 (Print)
Authors Tan, T. C.;Valova, V. A.;Malladi, C. S.;Graham, M. E.;Berven, L. A.;Jupp, O. J.;Hansra, G.;McClure, S. J.;Sarcevic, B.;Boadle, R. A.;Larsen, M. R.;Cousin, M. A.;Robinson, P. J. :
Publisher Name NAT CELL BIOL
Published Date 2003-01-01 00:00:00
Published Volume 5
Published Issue 8
Published Pages 701-10
URL http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12855954
Status Published In-print