{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Cingolani LA"],"funding":["Telethon"],"pagination":["931-937"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10695435"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["404(10)"],"pubmed_abstract":["The distance between Ca<sub>V</sub>2.1 voltage-gated Ca<sup>2+</sup> channels and the Ca<sup>2+</sup> sensor responsible for vesicle release at presynaptic terminals is critical for determining synaptic strength. Yet, the molecular mechanisms responsible for a loose coupling configuration of Ca<sub>V</sub>2.1 in certain synapses or developmental periods and a tight one in others remain unknown. Here, we examine the nanoscale organization of two Ca<sub>V</sub>2.1 splice isoforms (Ca<sub>V</sub>2.1[EFa] and Ca<sub>V</sub>2.1[EFb]) at presynaptic terminals by superresolution structured illumination microscopy. We find that Ca<sub>V</sub>2.1[EFa] is more tightly co-localized with presynaptic markers than Ca<sub>V</sub>2.1[EFb], suggesting that alternative splicing plays a crucial role in the synaptic organization of Ca<sub>V</sub>2.1 channels."],"journal":["Biological chemistry"],"pubmed_title":["Nanoscale organization of Ca<sub>V</sub>2.1 splice isoforms at presynaptic terminals: implications for synaptic vesicle release and synaptic facilitation."],"pmcid":["PMC10695435"],"funding_grant_id":["GGP19181"],"pubmed_authors":["Jaudon F","Thalhammer A","Muia J","Baj G","Cingolani LA"],"additional_accession":[]},"is_claimable":false,"name":"Nanoscale organization of Ca<sub>V</sub>2.1 splice isoforms at presynaptic terminals: implications for synaptic vesicle release and synaptic facilitation.","description":"The distance between Ca<sub>V</sub>2.1 voltage-gated Ca<sup>2+</sup> channels and the Ca<sup>2+</sup> sensor responsible for vesicle release at presynaptic terminals is critical for determining synaptic strength. Yet, the molecular mechanisms responsible for a loose coupling configuration of Ca<sub>V</sub>2.1 in certain synapses or developmental periods and a tight one in others remain unknown. Here, we examine the nanoscale organization of two Ca<sub>V</sub>2.1 splice isoforms (Ca<sub>V</sub>2.1[EFa] and Ca<sub>V</sub>2.1[EFb]) at presynaptic terminals by superresolution structured illumination microscopy. We find that Ca<sub>V</sub>2.1[EFa] is more tightly co-localized with presynaptic markers than Ca<sub>V</sub>2.1[EFb], suggesting that alternative splicing plays a crucial role in the synaptic organization of Ca<sub>V</sub>2.1 channels.","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Sep","modification":"2026-05-29T00:41:07.396Z","creation":"2025-04-06T05:35:41.566Z"},"accession":"S-EPMC10695435","cross_references":{"pubmed":["37658578"],"doi":["10.1515/hsz-2023-0235"]}}