Evidence map›Paper›PMID 26463206›Full record

ArticleThe Journal of biological chemistry2015

Characterization of the Mammalian CORVET and HOPS Complexes and Their Modular Restructuring for Endosome Specificity.

Rik van der Kant, Caspar T H Jonker, Ruud H Wijdeven, Jeroen Bakker, Lennert Janssen, Judith Klumperman, Jacques Neefjes

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
5.0field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

63 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
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  8. The protein interactome of the Neuron Specific Gene family (NSG1-3).bioRxiv : the preprint server for biology · 2025
    Article
  9. Late endosome transport by RILP-RAB7A promotes dendrite arborization.bioRxiv : the preprint server for biology · 2025
    Article
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3 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Rik van der KantFrom the Division of Cell Biology, Netherlands Cancer Institute, Amsterdam, 1066 CX, The Netherlands and Rikkant@gmail.com j.neefjes@nki.nl.
Caspar T H JonkerDepartment of Cell Biology, Center of Molecular Medicine, Utrecht, 3584 CX, The Netherlands.
Ruud H WijdevenFrom the Division of Cell Biology, Netherlands Cancer Institute, Amsterdam, 1066 CX, The Netherlands and.
Jeroen BakkerFrom the Division of Cell Biology, Netherlands Cancer Institute, Amsterdam, 1066 CX, The Netherlands and.
Lennert JanssenFrom the Division of Cell Biology, Netherlands Cancer Institute, Amsterdam, 1066 CX, The Netherlands and.
Judith KlumpermanDepartment of Cell Biology, Center of Molecular Medicine, Utrecht, 3584 CX, The Netherlands.
Jacques NeefjesFrom the Division of Cell Biology, Netherlands Cancer Institute, Amsterdam, 1066 CX, The Netherlands and.
The Netherlands Cancer Institute · NLUtrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Trafficking of cargo through the endosomal system depends on endosomal fusion events mediated by SNARE proteins, Rab-GTPases, and multisubunit tethering complexes. The CORVET and HOPS tethering complexes, respectively, regulate early and late endosomal tethering and have been characterized in detail in yeast where their sequential membrane targeting and assembly is well understood. Mammalian CORVET and HOPS subunits significantly differ from their yeast homologues, and novel proteins with high homology to CORVET/HOPS subunits have evolved. However, an analysis of the molecular interactions between these subunits in mammals is lacking. Here, we provide a detailed analysis of interactions within the mammalian CORVET and HOPS as well as an additional endosomal-targeting complex (VIPAS39-VPS33B) that does not exist in yeast. We show that core interactions within CORVET and HOPS are largely conserved but that the membrane-targeting module in HOPS has significantly changed to accommodate binding to mammalian-specific RAB7 interacting lysosomal protein (RILP). Arthrogryposis-renal dysfunction-cholestasis (ARC) syndrome-associated mutations in VPS33B selectively disrupt recruitment to late endosomes by RILP or binding to its partner VIPAS39. Within the shared core of CORVET/HOPS, we find that VPS11 acts as a molecular switch that binds either CORVET-specific TGFBRAP1 or HOPS-specific VPS39/RILP thereby allowing selective targeting of these tethering complexes to early or late endosomes to time fusion events in the endo/lysosomal pathway.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SubstitutionArthrogryposisAutophagy-Related ProteinsCell LineCholestasisEndosomesHumansIntracellular Signaling Peptides and ProteinsMultiprotein ComplexesMutation, MissenseRenal InsufficiencyVesicular Transport ProteinsAdaptor Proteins, Signal TransducingAutophagy-Related ProteinsIntracellular Signaling Peptides and ProteinsMultiprotein ComplexesRILP protein, humanTGFBRAP1 protein, humanVesicular Transport ProteinsVIPAS39 protein, humanVPS11 protein, humanVPS33B protein, humanVPS39 protein, humanendosomeintracellular traffickingmembrane fusionRabtransport

Identifiers

PMID26463206
PMCPMC4683254
OpenAlexW2280662035

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.