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SUMOylation of Syntaxin1A regulates presynaptic endocytosis

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

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Jeremy M. Henley

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Dr Tim Craig
Associate Professor of Neuroscience

Dina Anderson

Ashley J. Evans

Fatima Girach


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.


Henley, J. M., Craig, T. J., Anderson, D., Evans, A. J., & Girach, F. (2015). SUMOylation of Syntaxin1A regulates presynaptic endocytosis. Scientific Reports, 5, 17669.

Journal Article Type Article
Acceptance Date Nov 3, 2015
Publication Date Dec 4, 2015
Deposit Date Dec 8, 2015
Publicly Available Date Feb 9, 2016
Journal Scientific Reports
Electronic ISSN 2045-2322
Publisher Nature Research (part of Springer Nature)
Peer Reviewed Peer Reviewed
Volume 5
Pages 17669
Keywords SUMOylation, exocytosis, endocytosis, Syntaxin1A, presynaptic
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