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SUMOylation of Syntaxin1A regulates presynaptic endocytosis

Henley, Jeremy M.; Craig, Tim J.; Anderson, Dina; Evans, Ashley J.; Girach, Fatima

Authors

Jeremy M. Henley

Tim Craig Tim.Craig@uwe.ac.uk
Senior Lecturer in Physiology

Dina Anderson

Ashley J. Evans

Fatima Girach



Abstract

Neurotransmitter release from the presynaptic terminal is under very precise spatial and temporal control. Following neurotransmitter release, synaptic vesicles are recycled by endocytosis and refilled with neurotransmitter. During the exocytosis event leading to release, SNARE proteins provide most of the mechanical force for membrane fusion. Here, we show one of these proteins, Syntaxin1A, is SUMOylated near its C-terminal transmembrane domain in an activity-dependent manner. Preventing SUMOylation of Syntaxin1A reduces its interaction with other SNARE proteins and disrupts the balance of synaptic vesicle endo/exocytosis, resulting in an increase in endocytosis. These results indicate that SUMOylation regulates the emerging role of Syntaxin1A in vesicle endocytosis, which in turn, modulates neurotransmitter release and synaptic function.

Journal Article Type Article
Publication Date Dec 4, 2015
Journal Scientific Reports
Electronic ISSN 2045-2322
Publisher Nature Research (part of Springer Nature)
Peer Reviewed Peer Reviewed
Volume 5
Pages 17669
Institution Citation Henley, J. M., Craig, T. J., Anderson, D., Evans, A. J., Girach, F., & Henley, J. (2015). SUMOylation of Syntaxin1A regulates presynaptic endocytosis. Scientific Reports, 5, 17669. https://doi.org/10.1038/srep17669
DOI https://doi.org/10.1038/srep17669
Keywords SUMOylation, exocytosis, endocytosis, Syntaxin1A, presynaptic
Publisher URL http://dx.doi.org/10.1038/srep17669

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