ArticleThe Journal of cell biology2024
Synaptotagmin-1 undergoes phase separation to regulate its calcium-sensitive oligomerization.
Article in The Journal of cell biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- A primordial synaptotagmin-independent function of complexin in regulated exocytosis.Nature communications · 2026Article
- Impact of distinct neurotransmitter release modes on neuronal signaling.Molecular psychiatry · 2026Review
- Dynamic structural plasticity facilitates the developmental assembly of cochlear inner hair cell ribbon synapses.Frontiers in cell and developmental biology · 2026Article
- Mechanically induced dysregulation of calcium homeostasis: a molecular linchpin in asthmatic pathogenesis.European journal of medical research · 2025Review
- Dialogue Between the Clock Gene Bmal1 and Retinopathy: What Is the Exact Relationship?CNS neuroscience & therapeutics · 2025Review
- Article
- The liprin-α/RIM complex regulates the dynamic assembly of presynaptic active zones via liquid-liquid phase separation.PLoS biology · 2025Article
- Uncovering the Mechanisms of Intracellular Membrane Trafficking by Reconstituted Membrane Systems.Membranes · 2025Review
- Flexible iron: disorder in the ironome brings order to protein structure and function.Frontiers in molecular biosciences · 2025Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Synaptotagmin-1 (Syt1) is a calcium sensor that regulates synaptic vesicle fusion in synchronous neurotransmitter release. Syt1 interacts with negatively charged lipids and the SNARE complex to control the fusion event. However, it remains incompletely understood how Syt1 mediates Ca2+-trigged synaptic vesicle fusion. Here, we discovered that Syt1 undergoes liquid-liquid phase separation (LLPS) to form condensates both in vitro and in living cells. Syt1 condensates play a role in vesicle attachment to the PM and efficiently recruit SNAREs and complexin, which may facilitate the downstream synaptic vesicle fusion. We observed that Syt1 condensates undergo a liquid-to-gel-like phase transition, reflecting the formation of Syt1 oligomers. The phase transition can be blocked or reversed by Ca2+, confirming the essential role of Ca2+ in Syt1 oligomer disassembly. Finally, we showed that the Syt1 mutations causing Syt1-associated neurodevelopmental disorder impair the Ca2+-driven phase transition. These findings reveal that Syt1 undergoes LLPS and a Ca2+-sensitive phase transition, providing new insights into Syt1-mediated vesicle fusion.
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Registered trials
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