ArticleThe Journal of biological chemistry2010
The longin SNARE VAMP7/TI-VAMP adopts a closed conformation.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 37 citations in OpenAlex.
- VAMP7-dependent late endosomal secretion of ER and mitochondrial proteins impacts the tumor microenvironment and macrophage engagement.Nature communications · 2026Article
- Formation, Organization, and Maintenance of Synaptic Vesicle Pools: From Molecules to Structure and Dynamics.Advances in neurobiology · 2026Review
- The STX17-SNAP47-VAMP7/VAMP8 complex is the default SNARE complex mediating autophagosome-lysosome fusion.Cell research · 2024Article
- VAMP7j: A Splice Variant of Human VAMP7 That Modulates Neurite Outgrowth by Regulating L1CAM Transport to the Plasma Membrane.International journal of molecular sciences · 2023Article
- Nuclear and Cytoplasmatic Players in Mitochondria-Related CNS Disorders: Chromatin Modifications and Subcellular Trafficking.Biomolecules · 2022Review
- Role of SNAREs in Unconventional Secretion-Focus on the VAMP7-Dependent Secretion.Frontiers in cell and developmental biology · 2022Review
- Review
- A BLOC-1-AP-3 super-complex sorts a cis-SNARE complex into endosome-derived tubular transport carriers.The Journal of cell biology · 2021Article
- The ins and outs of the Arf4-based ciliary membrane-targeting complex.Small GTPases · 2021Review
- DIPK2A promotes STX17- and VAMP7-mediated autophagosome-lysosome fusion by binding to VAMP7B.Autophagy · 2020Article
- Cytotoxic Granule Exocytosis From Human Cytotoxic T Lymphocytes Is Mediated by VAMP7.Frontiers in immunology · 2019Article
- An interaction network between the SNARE VAMP7 and Rab GTPases within a ciliary membrane-targeting complex.Journal of cell science · 2018Article
- Presynaptic origins of distinct modes of neurotransmitter release.Current opinion in neurobiology · 2018Review
- VAMP721 Conformations Unmask an Extended Motif for K+ Channel Binding and Gating Control.Plant physiology · 2017Article
- Subcellular localization and trafficking of phytolongins (non-SNARE longins) in the plant secretory pathway.Journal of experimental botany · 2016Article
- VAMP7 regulates constitutive membrane incorporation of the cold-activated channel TRPM8.Nature communications · 2016Article
- The Arabidopsis R-SNARE VAMP721 Interacts with KAT1 and KC1 K+ Channels to Moderate K+ Current at the Plasma Membrane.The Plant cell · 2015Article
- Increased activity of the vesicular soluble N-ethylmaleimide-sensitive factor attachment protein receptor TI-VAMP/VAMP7 by tyrosine phosphorylation in the Longin domain.The Journal of biological chemistry · 2013Article
- Article
- The binding of Varp to VAMP7 traps VAMP7 in a closed, fusogenically inactive conformation.Nature structural & molecular biology · 2012Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
SNARE protein complexes are key mediators of exocytosis by juxtaposing opposing membranes, leading to membrane fusion. SNAREs generally consist of one or two core domains that can form a four-helix bundle with other SNARE core domains. Some SNAREs, such as syntaxin target-SNAREs and longin vesicular-SNAREs, have independent, folded N-terminal domains that can interact with their respective SNARE core domains and thereby affect the kinetics of SNARE complex formation. This autoinhibition mechanism is believed to regulate the role of the longin VAMP7/TI-VAMP in neuronal morphogenesis. Here we use nuclear magnetic resonance spectroscopy to study the longin-SNARE core domain interaction for VAMP7. Using complete backbone resonance assignments, chemical shift perturbations analysis, and hydrogen/deuterium exchange experiments, we conclusively show that VAMP7 adopts a preferentially closed conformation in solution. Taken together, the closed conformation of longins is conserved, in contrast to the syntaxin family of SNAREs for which mixtures of open and closed states have been observed. This may indicate different regulatory mechanisms for SNARE complexes containing syntaxins and longins, respectively.
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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.