ArticleDevelopmental cell2019
A Steric Gating Mechanism Dictates the Substrate Specificity of a Rab-GEF.
Article in Developmental cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Avl9 defines a family of DENN domain GTPase-activating proteins.The Journal of cell biology · 2026Article
- A subcomplex comprising TRAPPC11, TRAPPC12, TRAPPC13 and the fungal TRAPPC2L homolog, Tca17, directs TRAPPIII to autophagy.Journal of cell science · 2026Article
- Avl9 defines a family of GTPase-activating proteins that regulate diverse cell biological functions.bioRxiv : the preprint server for biology · 2026Article
- Cisternal Maturation of the Golgi Apparatus in Budding Yeast.Sub-cellular biochemistry · 2026Review
- Mechanistic adaptation of the metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned.Science advances · 2025Article
- Structural insights into traffic through the Golgi complex.Current opinion in cell biology · 2025Review
- Structural basis for Rab6 activation by the Ric1-Rgp1 complex.Nature communications · 2024Article
- Structural basis for Rab6 activation by the Ric1-Rgp1 complex.bioRxiv : the preprint server for biology · 2024Article
- Regulatory sites in the Mon1-Ccz1 complex control Rab5 to Rab7 transition and endosome maturation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Nucleoporin foci are stress-sensitive condensates dispensable for C. elegans nuclear pore assembly.The EMBO journal · 2023Article
- Article
- 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
- High-resolution secretory timeline from vesicle formation at the Golgi to fusion at the plasma membrane ineLife · 2022Article
- Structure of a TRAPPII-Rab11 activation intermediate reveals GTPase substrate selection mechanisms.Science advances · 2022Article
- Structure of the Mon1-Ccz1 complex reveals molecular basis of membrane binding for Rab7 activation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural basis for assembly of TRAPPII complex and specific activation of GTPase Ypt31/32.Science advances · 2022Article
- Who's in control? Principles of Rab GTPase activation in endolysosomal membrane trafficking and beyond.The Journal of cell biology · 2021Review
- Structural basis of TRAPPIII-mediated Rab1 activation.The EMBO journal · 2021Article
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3 authors.
Funding
Abstract
Correct localization of Rab GTPases in cells is critical for proper function in membrane trafficking, yet the mechanisms that target Rabs to specific subcellular compartments remain controversial. Guanine nucleotide exchange factors (GEFs) activate and consequently stabilize Rab substrates on membranes, thus implicating GEFs as the primary determinants of Rab localization. A competing hypothesis is that the Rab C-terminal hypervariable domain (HVD) serves as a subcellular targeting signal. In this study, we present a unifying mechanism in which the HVD controls targeting of certain Rabs by mediating interaction with their GEFs. We demonstrate that the TRAPP complexes, two related GEFs that use the same catalytic site to activate distinct Rabs, distinguish between Ypt1 (Rab1) and Ypt31/32 (Rab11) via their divergent HVDs. Remarkably, we find that HVD length gates Rab access to the TRAPPII complex by constraining the distance between the nucleotide-binding domain and the membrane surface.
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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.