ArticleThe EMBO journal2012
Solution single-vesicle assay reveals PIP2-mediated sequential actions of synaptotagmin-1 on SNAREs.
Article in The EMBO journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 85 citations in OpenAlex.
- Synaptotagmin-1 undergoes phase separation to regulate its calcium-sensitive oligomerization.The Journal of cell biology · 2024Article
- Synergistic regulation of fusion pore opening and dilation by SNARE and synaptotagmin-1.Journal of molecular cell biology · 2024Article
- Article
- A supramolecular system mimicking the infection process of an enveloped virus through membrane fusion.Scientific reports · 2023Article
- A Suitable Membrane Distance Regulated by the RBD_ACE2 Interaction is Critical for SARS-CoV-2 Spike-Mediated Viral Invasion.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Non-Vesicular Release of Alarmin Prothymosin α Complex Associated with Annexin-2 Flop-Out.Cells · 2023Review
- DYRK1-mediated phosphorylation of endocytic components is required for extracellular lumen expansion in ascidian notochord.Biological research · 2023Article
- Role of calcium-sensor proteins in cell membrane repair.Bioscience reports · 2023Review
- α-Synuclein Disrupts Vesicle Fusion by Two Mutant-Specific Mechanisms.Molecules and cells · 2022Article
- On the difficulties of characterizing weak protein interactions that are critical for neurotransmitter release.FEBS open bio · 2022Review
- Vesicle trafficking and vesicle fusion: mechanisms, biological functions, and their implications for potential disease therapy.Molecular biomedicine · 2022Review
- Tricalbin proteins regulate plasma membrane phospholipid homeostasis.Life science alliance · 2022Article
- Cooperative inhibition of SNARE-mediated vesicle fusion by α-synuclein monomers and oligomers.Scientific reports · 2021Article
- Regulatory role of sorting nexin 5 in protein stability and vesicular targeting of vesicular acetylcholine transporter to synaptic vesicle-like vesicles in PC12 cells.Journal of biomedical research · 2020Article
- Proteomics-based screening of the target proteins associated with antidepressant-like effect and mechanism of Saikosaponin A.Journal of cellular and molecular medicine · 2020Article
- Highly Efficient Protein-free Membrane Fusion: A Giant Vesicle Study.Biophysical journal · 2019Article
- Mechanism of neurotransmitter release coming into focus.Protein science : a publication of the Protein Society · 2018Review
- The high-affinity calcium sensor synaptotagmin-7 serves multiple roles in regulated exocytosis.The Journal of general physiology · 2018Review
- Emerging Functional Differences between the Synaptotagmin and Ferlin Calcium Sensor Families.Biochemistry · 2017Article
- Botulinum Toxins A and E Inflict Dynamic Destabilization on t-SNARE to Impair SNARE Assembly and Membrane Fusion.Structure (London, England : 1993) · 2017Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Synaptotagmin-1 (Syt1) is a major Ca(2+) sensor for synchronous neurotransmitter release, which requires vesicle fusion mediated by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors). Syt1 utilizes its diverse interactions with target membrane (t-) SNARE, SNAREpin, and phospholipids, to regulate vesicle fusion. To dissect the functions of Syt1, we apply a single-molecule technique, alternating-laser excitation (ALEX), which is capable of sorting out subpopulations of fusion intermediates and measuring their kinetics in solution. The results show that Syt1 undergoes at least three distinct steps prior to lipid mixing. First, without Ca(2+), Syt1 mediates vesicle docking by directly binding to t-SNARE/phosphatidylinositol 4,5-biphosphate (PIP(2)) complex and increases the docking rate by 10(3) times. Second, synaptobrevin-2 binding to t-SNARE displaces Syt1 from SNAREpin. Third, with Ca(2+), Syt1 rebinds to SNAREpin, which again requires PIP(2). Thus without Ca(2+), Syt1 may bring vesicles to the plasma membrane in proximity via binding to t-SNARE/PIP(2) to help SNAREpin formation and then, upon Ca(2+) influx, it may rebind to SNAREpin, which may trigger synchronous fusion. The results show that ALEX is a powerful method to dissect multiple kinetic steps in the vesicle fusion pathway.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.