ArticleFEBS letters2013
Juxtamembrane tryptophans of synaptobrevin 2 control the process of membrane fusion.
Article in FEBS letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
- Molecular mechanism underlying SNARE-mediated membrane fusion enlightened by all-atom molecular dynamics simulations.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Membrane transformations of fusion and budding.Nature communications · 2024Review
- The function of VAMP2 in mediating membrane fusion: An overview.Frontiers in molecular neuroscience · 2022Review
- Intracellular Vesicle Fusion Requires a Membrane-Destabilizing Peptide Located at the Juxtamembrane Region of the v-SNARE.Cell reports · 2019Article
- Drug testing complementary metal-oxide-semiconductor chip reveals drug modulation of transmitter release for potential therapeutic applications.Journal of neurochemistry · 2019Article
- Synaptobrevin-2 C-Terminal Flexible Region Regulates the Discharge of Catecholamine Molecules.Biophysical journal · 2019Article
- Review
- Amperometry methods for monitoring vesicular quantal size and regulation of exocytosis release.Pflugers Archiv : European journal of physiology · 2018Review
- How does the stimulus define exocytosis in adrenal chromaffin cells?Pflugers Archiv : European journal of physiology · 2018Review
- v-SNARE function in chromaffin cells.Pflugers Archiv : European journal of physiology · 2018Review
- The Multifaceted Role of SNARE Proteins in Membrane Fusion.Frontiers in physiology · 2017Review
- The first non Clostridial botulinum-like toxin cleaves VAMP within the juxtamembrane domain.Scientific reports · 2016Article
- Molecular underpinnings of synaptic vesicle pool heterogeneity.Traffic (Copenhagen, Denmark) · 2015Review
- Catecholamine exocytosis during low frequency stimulation in mouse adrenal chromaffin cells is primarily asynchronous and controlled by the novel mechanism of Ca2+ syntilla suppression.The Journal of physiology · 2014Article
- How could SNARE proteins open a fusion pore?Physiology (Bethesda, Md.) · 2014Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Synaptobrevin 2 (Syb2), syntaxin (Sx1A), and SNAP-25, generate a force to induce fusion pore formation. The v-SNARE, Syb2, is anchored to the vesicle membrane by a single transmembrane domain. Here we show that 2 tryptophans (W89/W90) located in the juxtamembrane domain of Syb2, which stabilize the transmembrane (TM) domain position, control the ratio of spontaneous vs. stimulated membrane fusion events in chromaffin cells. Changing the 2 hydrophobic tryptophans to neutral alanines promotes spontaneous membrane fusion, faster transmitter release kinetics and complete release from individual vesicles. The results indicate that the two tryptophans act as a fusion clamp making fusion stimulus-dependent.
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Registered trials
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.