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• W2139061567 endingPage "1356" @default.
• W2139061567 startingPage "1348" @default.
• W2139061567 abstract "Abstract Posttranslational modification by small ubiquitin‐like modifier (SUMO) proteins is emerging as an important regulatory mechanism for neuronal function and dysfunction. Although multiple potential presynaptic SUMOylation substrate proteins have been proposed from sequence analysis the functional consequences of presynaptic SUMOylation have not been determined. Here we show that SUMOylation of presynaptic proteins modulates neurotransmitter release. Increasing protein SUMOylation by entrapping recombinant SUMO‐1 in synaptosomes decreased glutamate release evoked by KCl whereas decreasing SUMOylation with the SUMO‐specific protease SENP‐1 enhanced KCl‐evoked release. In contrast, SUMO increased and SENP‐1 decreased synaptosomal glutamate release evoked by kainate stimulation. Consistent with these results, SENP‐1 increased Ca 2+ influx into synaptosomes evoked by KCl whereas it decreased kainate‐induced Ca 2+ influx. These results demonstrate that, in addition to postsynaptic effects, protein SUMOylation acts to modulate neurotransmitter release and thereby regulate synaptic function." @default.
• W2139061567 created "2016-06-24" @default.
• W2139061567 creator A5029889770 @default.
• W2139061567 creator A5082068871 @default.
• W2139061567 creator A5083648774 @default.
• W2139061567 date "2009-03-30" @default.
• W2139061567 modified "2023-10-16" @default.
• W2139061567 title "Protein SUMOylation modulates calcium influx and glutamate release from presynaptic terminals" @default.
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• W2139061567 doi "https://doi.org/10.1111/j.1460-9568.2009.06692.x" @default.
• W2139061567 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3309032" @default.
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