ArticleNature structural & molecular biology2010
Molecular architecture of the TRAPPII complex and implications for vesicle tethering.
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 50 papers.
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Who cites it
50 citing papers in PubMed.
- PCIPG: A comprehensive framework for protein complex identification based on a probabilistic graphical model.PLoS computational biology · 2026Article
- Canine Neuronal Ceroid Lipofuscinosis-like Disorder Associated with Sequence Variants inGenes · 2025Article
- TRAPPopathies: Severe Multisystem Disorders Caused by Variants in Genes of the Transport Protein Particle (TRAPP) Complexes.International journal of molecular sciences · 2024Review
- A role for β-1,6- and β-1,3-glucans in kinetochore function in Saccharomyces cerevisiae.Genetics · 2024Article
- Large scale microfluidic CRISPR screening for increased amylase secretion in yeast.Lab on a chip · 2023Article
- The P4-ATPase Drs2 interacts with and stabilizes the multisubunit tethering complex TRAPPIII in yeast.EMBO reports · 2023Article
- The TRAPP complexes: discriminating GTPases in context.FEBS letters · 2023Review
- The TRAPP complexes: oligomeric exchange factors that activate the small GTPases Rab1 and Rab11.FEBS letters · 2023Review
- Neuronal SNARE complex assembly guided by Munc18-1 and Munc13-1.FEBS open bio · 2022Review
- A bipartite, low-affinity roadblock domain-containing GAP complex regulates bacterial front-rear polarity.PLoS genetics · 2022Article
- Structure of a TRAPPII-Rab11 activation intermediate reveals GTPase substrate selection mechanisms.Science advances · 2022Article
- Structural basis for assembly of TRAPPII complex and specific activation of GTPase Ypt31/32.Science advances · 2022Article
- Cryo-EM structure of metazoan TRAPPIII, the multi-subunit complex that activates the GTPase Rab1.The EMBO journal · 2021Article
- Insights on autophagosome-lysosome tethering from structural and biochemical characterization of human autophagy factor EPG5.Communications biology · 2021Article
- The substrate specificity of the human TRAPPII complex's Rab-guanine nucleotide exchange factor activity.Communications biology · 2020Article
- Recent Advances in Single-Particle Electron Microscopic Analysis of Autophagy Degradation Machinery.International journal of molecular sciences · 2020Review
- Characterization of Aspergillus nidulans TRAPPs uncovers unprecedented similarities between fungi and metazoans and reveals the modular assembly of TRAPPII.PLoS genetics · 2019Article
- The C7orf43/TRAPPC14 component links the TRAPPII complex to Rabin8 for preciliary vesicle tethering at the mother centriole during ciliogenesis.The Journal of biological chemistry · 2019Article
- Ypt/Rab GTPases and their TRAPP GEFs at the Golgi.FEBS letters · 2019Review
- Adaptor protein complex-1 (AP-1) is recruited by the HEATR5 protein Laa1 and its co-factor Laa2 in yeast.The Journal of biological chemistry · 2019Article
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3 authors.
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Abstract
Multisubunit tethering complexes participate in the process of vesicle tethering--the initial interaction between transport vesicles and their acceptor compartments. TRAPPII (named for transport protein particle II) is a highly conserved tethering complex that functions in the late Golgi apparatus and consists of all of the subunits of TRAPPI and three additional, specific subunits. We have purified native yeast TRAPPII and characterized its structure and subunit organization by single-particle EM. Our data show that the nine TRAPPII components form a core complex that dimerizes into a three-layered, diamond-shaped structure. The TRAPPI subunits assemble into TRAPPI complexes that form the outer layers. The three TRAPPII-specific subunits cap the ends of TRAPPI and form the middle layer, which is responsible for dimerization. TRAPPII binds the Ypt1 GTPase and probably uses the TRAPPI catalytic core to promote guanine nucleotide exchange. We discuss the implications of the structure of TRAPPII for coat interaction and TRAPPII-associated human pathologies.
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