SUMOylation of Syntaxin1A regulates presynaptic endocytosis.

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_name

Sci Rep

journal_title

Scientific reports

authors

Craig TJ,Anderson D,Evans AJ,Girach F,Henley JM

doi

10.1038/srep17669

subject

Has Abstract

pub_date

2015-12-04 00:00:00

pages

17669

issn

2045-2322

pii

srep17669

journal_volume

5

pub_type

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