Protein SUMOylation modulates calcium influx and glutamate release from presynaptic terminals

M Feligioni, A Nishimune, JM Henley

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

51 Citations (Scopus)

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.
Translated title of the contributionProtein SUMOylation modulates calcium influx and glutamate release from presynaptic terminals
Original languageEnglish
Pages (from-to)1348 - 1356
Number of pages9
JournalEuropean Journal of Neuroscience
Volume9(7)
DOIs
Publication statusPublished - Mar 2009

Bibliographical note

Publisher: Wiley

Fingerprint

Dive into the research topics of 'Protein SUMOylation modulates calcium influx and glutamate release from presynaptic terminals'. Together they form a unique fingerprint.

Cite this