ArticlePloS one2013
Crystal Structures of the Sec1/Munc18 (SM) Protein Vps33, Alone and Bound to the Homotypic Fusion and Vacuolar Protein Sorting (HOPS) Subunit Vps16*.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
41 citing papers in PubMed, 60 citations in OpenAlex.
- VPS33B regulates MHC class II antigen presentation in dendritic cells to drive CD4 T cell immunity.iScience · 2026Article
- Molecular Mechanisms of Extracellular Vesicle Biogenesis and Their Impact on the Design of Custom EVs.Advanced healthcare materials · 2025Review
- UtilizingJournal of developmental biology · 2025Review
- Mucopolysaccharidosis-Plus Syndrome: Is This a Type of Mucopolysaccharidosis or a Separate Kind of Metabolic Disease?International journal of molecular sciences · 2024Review
- Molecular structures and function of the autophagosome-lysosome fusion machinery.Autophagy reports · 2024Article
- Domain 3a mutation of VPS33A suppresses larval arrest phenotype in the loss of VPS45 inmicroPublication biology · 2024Article
- Association mapping in multiple yam species (Dioscorea spp.) of quantitative trait loci for yield-related traits.BMC plant biology · 2023Article
- A humanizedmicroPublication biology · 2023Article
- SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023Article
- Modeling of Protein Complexes.Methods in molecular biology (Clifton, N.J.) · 2023Article
- High-resolution secretory timeline from vesicle formation at the Golgi to fusion at the plasma membrane ineLife · 2022Article
- Chaperoning SNARE Folding and Assembly.Annual review of biochemistry · 2021Review
- Bi-allelic VPS16 variants limit HOPS/CORVET levels and cause a mucopolysaccharidosis-like disease.EMBO molecular medicine · 2021Article
- Munc13 activates the Munc18-1/syntaxin-1 complex and enables Munc18-1 to prime SNARE assembly.The EMBO journal · 2020Article
- Article
- Mucopolysaccharidosis-Plus Syndrome.International journal of molecular sciences · 2020Article
- 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
- Munc18 and Munc13 serve as a functional template to orchestrate neuronal SNARE complex assembly.Nature communications · 2019Article
- Phosphoinositides control the localization of HOPS subunit VPS41, which together with VPS33 mediates vacuole fusion in plants.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Intracellular membrane fusion requires the regulated assembly of SNARE (soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptor) proteins anchored in the apposed membranes. To exert the force required to drive fusion between lipid bilayers, juxtamembrane SNARE motifs zipper into four-helix bundles. Importantly, SNARE function is regulated by additional factors, none more extensively studied than the SM (Sec1/Munc18-like) proteins. SM proteins interact with both individual SNAREs and SNARE complexes, likely chaperoning SNARE complex formation and protecting assembly intermediates from premature disassembly by NSF. Four families of SM proteins have been identified, and representative members of two of these families (Sec1/Munc18 and Sly1) have been structurally characterized. We report here the 2.6 Å resolution crystal structure of an SM protein from the third family, Vps33. Although Vps33 shares with the first two families the same basic three-domain architecture, domain 1 is displaced by 15 Å, accompanied by a 40° rotation. A unique feature of the Vps33 family of SM proteins is that its members function as stable subunits within a multi-subunit tethering complex called HOPS (homotypic fusion and vacuolar protein sorting). Integration into the HOPS complex depends on the interaction between Vps33 and a second HOPS subunit, Vps16. The crystal structure of Vps33 bound to a C-terminal portion of Vps16, also at 2.6 Å resolution, reveals the structural basis for this interaction. Despite the extensive interface between the two HOPS subunits, the conformation of Vps33 is only subtly affected by binding to Vps16.
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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.