RIM1α SUMOylation is required for fast synaptic vesicle exocytosis

Fatima Girach, Tim J Craig, Jeremy M Henley, Jeremy M Henley

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

42 Citations (Scopus)


The rapid, activity-dependent quantal presynaptic release of neurotransmitter is vital for
brain function. The complex process of vesicle priming, fusion and retrieval is very
precisely controlled and requires the spatio-temperal coordination of multiple proteinprotein
interactions. Here we show that posttranslational modification of the active zone
protein, Rab3 Interacting Molecule 1α (RIM1α) by the Small Ubiquitin-like Modifier-1
(SUMO-1) functions as a molecular switch to direct these interactions and is essential
for fast synaptic vesicle exocytosis. RIM1α SUMOylation at lysine residue K502
facilitates clustering of CaV2.1 and enhances the Ca2+ influx necessary for vesicular
release whereas non-SUMOylated RIM1α participates in the docking/priming of
synaptic vesicles and maintenance of active zone structure. These results demonstrate
that SUMOylation of RIM1α is a key determinant of rapid, synchronous
neurotransmitter release and the SUMO-mediated 'switching' of RIM1α between
binding proteins provides new insight into the mechanisms underpinning synaptic
function and dysfunction.
Original languageEnglish
JournalCell Reports
Publication statusPublished - Nov 2013


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