Dissemin is shutting down on January 1st, 2025

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Nature Research, Nature Neuroscience, 7(13), p. 845-851, 2010

DOI: 10.1038/nn.2571

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

Journal article published in 2010 by Emma Louise Clayton, Nancy Sue, Karen Janet Smillie ORCID, Timothy O’Leary, Nicolai Bache, Giselle Cheung, Adam Robert Cole, David J. Wyllie ORCID, Calum Sutherland, Phillip James Robinson ORCID, Michael Alan Cousin ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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.