ArticleNature structural & molecular biology2010
The SM protein Vps33 and the t-SNARE H(abc) domain promote fusion pore opening.
Article in Nature structural & molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- SM protein Sly1 and a SNARE Habc domain promote membrane fusion through multiple mechanisms.The Journal of cell biology · 2024Article
- Domain 3a mutation of VPS33A suppresses larval arrest phenotype in the loss of VPS45 inmicroPublication biology · 2024Article
- Vesicle trafficking and vesicle fusion: mechanisms, biological functions, and their implications for potential disease therapy.Molecular biomedicine · 2022Review
- The road to lysosome-related organelles: Insights from Hermansky-Pudlak syndrome and other rare diseases.Traffic (Copenhagen, Denmark) · 2019Review
- A VPS33A-binding motif on syntaxin 17 controls autophagy completion in mammalian cells.The Journal of biological chemistry · 2019Article
- SNARE-mediated membrane fusion arrests at pore expansion to regulate the volume of an organelle.The EMBO journal · 2018Article
- Article
- How and why intralumenal membrane fragments form during vacuolar lysosome fusion.Molecular biology of the cell · 2017Article
- Steric hindrance of SNARE transmembrane domain organization impairs the hemifusion-to-fusion transition.EMBO reports · 2016Article
- Vtc5, a Novel Subunit of the Vacuolar Transporter Chaperone Complex, Regulates Polyphosphate Synthesis and Phosphate Homeostasis in Yeast.The Journal of biological chemistry · 2016Article
- Reconstituting Intracellular Vesicle Fusion Reactions: The Essential Role of Macromolecular Crowding.Journal of the American Chemical Society · 2015Article
- Recruitment of VPS33A to HOPS by VPS16 Is Required for Lysosome Fusion with Endosomes and Autophagosomes.Traffic (Copenhagen, Denmark) · 2015Article
- Vacuolar SNARE protein transmembrane domains serve as nonspecific membrane anchors with unequal roles in lipid mixing.The Journal of biological chemistry · 2015Article
- A modular tethering complex for endosomal recycling.Nature cell biology · 2015Article
- The Habc domain of the SNARE Vam3 interacts with the HOPS tethering complex to facilitate vacuole fusion.The Journal of biological chemistry · 2015Article
- Loss of the Sec1/Munc18-family proteins VPS-33.2 and VPS-33.1 bypasses a block in endosome maturation in Caenorhabditis elegans.Molecular biology of the cell · 2014Article
- A dynamin homolog promotes the transition from hemifusion to content mixing in intracellular membrane fusion.Traffic (Copenhagen, Denmark) · 2014Article
- Membrane tethering.F1000prime reports · 2014Review
- Comparative studies of Munc18c and Munc18-1 reveal conserved and divergent mechanisms of Sec1/Munc18 proteins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Structural basis of Vps33A recruitment to the human HOPS complex by Vps16.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intracellular membrane fusion proceeds via distinct stages of membrane docking, hemifusion and fusion pore opening and depends on interacting families of Rab, SNARE and SM proteins. Trans-SNARE complexes dock the membranes in close apposition. Efficient fusion requires further SNARE-associated proteins. They might increase the number of trans-SNARE complexes or the fusogenic potential of a single SNARE complex. We investigated the contributions of the SM protein Vps33 to hemifusion and pore opening between yeast vacuoles. Mutations in Vps33 that weaken its interactions with the SNARE complex allowed normal trans-SNARE pairing and lipid mixing but retarded content mixing. Deleting the H(abc) domain of the vacuolar t-SNARE Vam3, which interacts with Vps33, had the same effect. This suggests that SM proteins promote fusion pore opening by enhancing the fusogenic activity of a SNARE complex. They should thus be considered integral parts of the fusion machinery.
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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.