SUMOylation of Syntaxin1A regulates presynaptic endocytosis

Tim Craig, Dina Anderson, Ashley Evans, Fatima Girach, Jeremy Henley

Research output: Contribution to journalArticle (Academic Journal)peer-review

42 Citations (Scopus)
364 Downloads (Pure)


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.
Original languageEnglish
Article number17669
Number of pages11
JournalScientific Reports
Publication statusPublished - 4 Dec 2015


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