{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Vardar G"],"funding":["Deutsche Forschungsgemeinschaft"],"pagination":["e78182"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9183232"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11"],"pubmed_abstract":["SNAREs are undoubtedly one of the core elements of synaptic transmission. Contrary to the well characterized function of their SNARE domains bringing the plasma and vesicular membranes together, the level of contribution of their juxtamembrane domain (JMD) and the transmembrane domain (TMD) to the vesicle fusion is still under debate. To elucidate this issue, we analyzed three groups of STX1A mutations in cultured mouse hippocampal neurons: (1) elongation of STX1A's JMD by three amino acid insertions in the junction of SNARE-JMD or JMD-TMD; (2) charge reversal mutations in STX1A's JMD; and (3) palmitoylation deficiency mutations in STX1A's TMD. We found that both JMD elongations and charge reversal mutations have position-dependent differential effects on Ca<sup>2+</sup>-evoked and spontan"],"journal":["eLife"],"pubmed_title":["Syntaxin-1A modulates vesicle fusion in mammalian neurons via juxtamembrane domain dependent palmitoylation of its transmembrane domain."],"pmcid":["PMC9183232"],"funding_grant_id":["388271549","399894546","436260754","27800197"],"pubmed_authors":["Trimbuch T","Zobel S","Vardar G","Salazar-Lazaro A","Rosenmund C"],"additional_accession":[]},"is_claimable":false,"name":"Syntaxin-1A modulates vesicle fusion in mammalian neurons via juxtamembrane domain dependent palmitoylation of its transmembrane domain.","description":"SNAREs are undoubtedly one of the core elements of synaptic transmission. Contrary to the well characterized function of their SNARE domains bringing the plasma and vesicular membranes together, the level of contribution of their juxtamembrane domain (JMD) and the transmembrane domain (TMD) to the vesicle fusion is still under debate. To elucidate this issue, we analyzed three groups of STX1A mutations in cultured mouse hippocampal neurons: (1) elongation of STX1A's JMD by three amino acid insertions in the junction of SNARE-JMD or JMD-TMD; (2) charge reversal mutations in STX1A's JMD; and (3) palmitoylation deficiency mutations in STX1A's TMD. We found that both JMD elongations and charge reversal mutations have position-dependent differential effects on Ca<sup>2+</sup>-evoked and spontan","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 May","modification":"2025-04-25T19:12:33.284Z","creation":"2025-02-19T03:51:59.842Z"},"accession":"S-EPMC9183232","cross_references":{"pubmed":["35638903"],"doi":["10.7554/eLife.78182"]}}