ArticleNature communications2015
Direct quantitative detection of Doc2b-induced hemifusion in optically trapped membranes.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 40 citations in OpenAlex.
- Mechanistic Insights into Synaptotagmin-1 Mediated Membrane Fusion and Interactions.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Membrane-induced 2D phase separation of the focal adhesion protein talin.Nature communications · 2024Article
- Pancreatic β-cells package double C2-like domain beta protein into extracellular vesicles via tandem C2 domains.Frontiers in endocrinology · 2024Article
- Article
- Toxoplasma gondii phosphatidylserine flippase complex ATP2B-CDC50.4 critically participates in microneme exocytosis.PLoS pathogens · 2022Article
- Membrane fusion studied by colloidal probes.European biophysics journal : EBJ · 2021Review
- Doc2 Proteins Are Not Required for the Increased Spontaneous Release Rate in Synaptotagmin-1-Deficient Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020Article
- Synaptotagmin-1 and Doc2b Exhibit Distinct Membrane-Remodeling Mechanisms.Biophysical journal · 2020Article
- Phosphatidylserine is critical for vesicle fission during clathrin-mediated endocytosis.Journal of neurochemistry · 2020Article
- Doc2b CaScientific reports · 2019Article
- Artificial Cell Membranes Interfaced with Optical Tweezers: A Versatile Microfluidics Platform for Nanomanipulation and Mechanical Characterization.ACS applied materials & interfaces · 2019Article
- Colloid supported lipid bilayers for self-assembly.Soft matter · 2019Article
- Protecting functional β cells with a therapeutic peptide.Annals of translational medicine · 2018Article
- Article
- Doc2B acts as a calcium sensor for vesicle priming requiring synaptotagmin-1, Munc13-2 and SNAREs.eLife · 2017Article
- Article
- How and why intralumenal membrane fragments form during vacuolar lysosome fusion.Molecular biology of the cell · 2017Article
- SNARE-mediated membrane fusion trajectories derived from force-clamp experiments.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ca(2+)-sensor proteins control the secretion of many neuroendocrine substances. Calcium-secretion coupling may involve several mechanisms. First, Ca(2+)-dependent association of their tandem C2 domains with phosphatidylserine may induce membrane curvature and thereby enhance fusion. Second, their association with SNARE complexes may inhibit membrane fusion in the absence of a Ca(2+) trigger. Here we present a method using two optically trapped beads coated with SNARE-free synthetic membranes to elucidate the direct role of the C2AB domain of the soluble Ca(2+)-sensor Doc2b. Contacting membranes are often coupled by a Doc2b-coated membrane stalk that resists forces up to 600 pN upon bead separation. Stalk formation depends strictly on Ca(2+) and phosphatidylserine. Real-time fluorescence imaging shows phospholipid but not content mixing, indicating membrane hemifusion. Thus, Doc2b acts directly on membranes and stabilizes the hemifusion intermediate in this cell-free system. In living cells, this mechanism may co-occur with progressive SNARE complex assembly, together defining Ca(2+)-secretion coupling.
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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.