Vesicle docking and fusion pore modulation by the neuronal calcium sensor Synaptotagmin-1.
Journal
bioRxiv : the preprint server for biology
ISSN: 2692-8205
Titre abrégé: bioRxiv
Pays: United States
ID NLM: 101680187
Informations de publication
Date de publication:
12 Sep 2024
12 Sep 2024
Historique:
medline:
24
9
2024
pubmed:
24
9
2024
entrez:
24
9
2024
Statut:
epublish
Résumé
Synaptotagmin-1 (Syt1) is a major calcium sensor for rapid neurotransmitter release in neurons and hormone release in many neuroendocrine cells. It possesses two tandem cytosolic C2 domains that bind calcium, negatively charged phospholipids, and the neuronal SNARE complex. Calcium binding to Syt1 triggers exocytosis, but how this occurs is not well understood. Syt1 has additional roles in docking dense core vesicles (DCV) and synaptic vesicles (SV) to the plasma membrane (PM) and in regulating fusion pore dynamics. Thus, Syt1 perturbations could affect release through vesicle docking, fusion triggering, fusion pore regulation, or a combination of these. Here, using a human neuroendocrine cell line, we show that neutralization of highly conserved polybasic patches in either C2 domain of Syt1 impairs both DCV docking and efficient release of serotonin from DCVs. Interestingly, the same mutations resulted in larger fusion pores and faster release of serotonin during individual fusion events. Thus, Syt1's roles in vesicle docking, fusion triggering, and fusion pore control may be functionally related.
Identifiants
pubmed: 39314345
doi: 10.1101/2024.09.12.612660
pmc: PMC11419119
pii:
doi:
Types de publication
Journal Article
Preprint
Langues
eng