ArticleCell2008
The structural basis for activation of the Rab Ypt1p by the TRAPP membrane-tethering complexes.
Article in Cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.
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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
112 citing papers in PubMed.
- A subcomplex comprising TRAPPC11, TRAPPC12, TRAPPC13 and the fungal TRAPPC2L homolog, Tca17, directs TRAPPIII to autophagy.Journal of cell science · 2026Article
- Catalytic mechanism for β-carotene isomerisation and substrate selectivity by the strigolactone biosynthetic enzymes D27 and D27like1.Scientific reports · 2026Article
- Establishment of the phagophore-ERES membrane contact site initiates phagophore elongation.Nature structural & molecular biology · 2025Article
- Cryo-EM structure of the human MON1A-CCZ1-RAB7A complex provides insights into nucleotide exchange mechanism.Life metabolism · 2025Article
- Structural basis for Rab6 activation by the Ric1-Rgp1 complex.Nature communications · 2024Article
- Article
- Structural basis for Rab6 activation by the Ric1-Rgp1 complex.bioRxiv : the preprint server for biology · 2024Article
- The eukaryotic-like characteristics of small GTPase, roadblock and TRAPPC3 proteins from Asgard archaea.Communications biology · 2024Article
- SP-141 targets Trs85 to inhibit rice blast fungus infection and functions as a potential broad-spectrum antifungal agent.Plant communications · 2024Article
- Functional screening revealsmBio · 2023Article
- A C. albicans TRAPP Complex-Associated Gene Contributes to Cell Wall Integrity, Hyphal and Biofilm Formation, and Tissue Invasion.Microbiology spectrum · 2023Article
- Structure of the metazoan Rab7 GEF complex Mon1-Ccz1-Bulli.Proceedings of the National Academy of Sciences of the United States of America · 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
- 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
- Comparative genomic analysis and phylogeny of NAC25 gene from cultivated and wildFrontiers in plant science · 2022Article
- Impact of C-terminal truncations in the Arabidopsis Rab escort protein (REP) on REP-Rab interaction and plant fertility.The Plant journal : for cell and molecular biology · 2021Article
- Focus on the Small GTPase Rab1: A Key Player in the Pathogenesis of Parkinson's Disease.International journal of molecular sciences · 2021Review
- TRAPP structures reveal the big picture.The EMBO journal · 2021Article
52 more citing papers are in PubMed but not listed here.
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11 authors.
Funding
Abstract
The multimeric membrane-tethering complexes TRAPPI and TRAPPII share seven subunits, of which four (Bet3p, Bet5p, Trs23p, and Trs31p) are minimally needed to activate the Rab GTPase Ypt1p in an event preceding membrane fusion. Here, we present the structure of a heteropentameric TRAPPI assembly complexed with Ypt1p. We propose that TRAPPI facilitates nucleotide exchange primarily by stabilizing the nucleotide-binding pocket of Ypt1p in an open, solvent-accessible form. Bet3p, Bet5p, and Trs23p interact directly with Ypt1p to stabilize this form, while the C terminus of Bet3p invades the pocket to participate in its remodeling. The Trs31p subunit does not interact directly with the GTPase but allosterically regulates the TRAPPI interface with Ypt1p. Our findings imply that TRAPPII activates Ypt1p by an identical mechanism. This view of a multimeric membrane-tethering assembly complexed with a Rab provides a framework for understanding events preceding membrane fusion at the molecular level.
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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.