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Dynamin I phosphorylation by GSK3 controls activity-dependent bulk endocytosis of synaptic vesicles.

Clayton, EL and Sue, N and Smillie, KJ and O'Leary, T and Bache, N and Cheung, G and Cole, AR and Wyllie, DJ and Sutherland, C and Robinson, PJ and Cousin, MA (2010) Dynamin I phosphorylation by GSK3 controls activity-dependent bulk endocytosis of synaptic vesicles. Nat Neurosci, 13. pp. 845-851.

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Abstract

Glycogen synthase kinase 3 (GSK3) is a critical enzyme in neuronal physiology; however, it is not yet known whether it has any specific role in presynaptic function. We found that GSK3 phosphorylates a residue on the large GTPase dynamin I (Ser-774) both in vitro and in primary rat neuronal cultures. This was dependent on prior phosphorylation of Ser-778 by cyclin-dependent kinase 5. Using both acute inhibition with pharmacological antagonists and silencing of expression with short hairpin RNA, we found that GSK3 was specifically required for activity-dependent bulk endocytosis (ADBE) but not clathrin-mediated endocytosis. Moreover we found that the specific phosphorylation of Ser-774 on dynamin I by GSK3 was both necessary and sufficient for ADBE. These results demonstrate a presynaptic role for GSK3 and they indicate that a protein kinase signaling cascade prepares synaptic vesicles for retrieval during elevated neuronal activity.

Item Type: Article
Uncontrolled Keywords: Animals Cells, Cultured Cerebellum Cyclin-Dependent Kinase 5 Dynamin I Endocytosis Glycogen Synthase Kinase 3 Hippocampus In Vitro Techniques Male Neurons Phosphorylation Presynaptic Terminals Rats Rats, Sprague-Dawley Signal Transduction Synaptic Vesicles
Subjects: UNSPECIFIED
Divisions: Div F > Control
Depositing User: Cron Job
Date Deposited: 17 Jul 2017 18:58
Last Modified: 18 Nov 2017 21:46
DOI: