Evidence map›Paper›PMID 28100638›Full record

ArticleMolecular biology of the cell2017

Retromer-driven membrane tubulation separates endosomal recycling from Rab7/Ypt7-dependent fusion.

Latha Kallur Purushothaman, Henning Arlt, Anne Kuhlee, Stefan Raunser, Christian Ungermann

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

32 citing papers in PubMed, 53 citations in OpenAlex.

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  10. γ-secretase facilitates retromer-mediated retrograde transport.bioRxiv : the preprint server for biology · 2024
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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

5 authors at 2 institutions in 1 country.

Latha Kallur PurushothamanDepartment of Biology/Chemistry, Biochemistry Section, University of Osnabrück, 49076 Osnabrück, Germany.
Henning ArltDepartment of Biology/Chemistry, Biochemistry Section, University of Osnabrück, 49076 Osnabrück, Germany hearlt@hsph.harvard.edu cu@uos.de.
Anne KuhleeDepartment of Structural Biochemistry, Max-Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.
Stefan RaunserDepartment of Structural Biochemistry, Max-Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.
Christian UngermannDepartment of Biology/Chemistry, Biochemistry Section, University of Osnabrück, 49076 Osnabrück, Germany hearlt@hsph.harvard.edu cu@uos.de.
Osnabrück University · DEMax Planck Institute of Molecular Physiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endosomes are the major protein-sorting hubs of the endocytic pathway. They sort proteins destined for degradation into internal vesicles while in parallel recycling receptors via tubular carriers back to the Golgi. Tubule formation depends on the Rab7/Ypt7-interacting retromer complex, consisting of the sorting nexin dimer (SNX-BAR) and the trimeric cargo selection complex (CSC). Fusion of mature endosomes with the lysosome-like vacuole also requires Rab7/Ypt7. Here we solve a major problem in understanding this dual function of endosomal Rab7/Ypt7, using a fully reconstituted system, including purified, full-length yeast SNX-BAR and CSC, whose overall structure we present. We reveal that the membrane-active SNX-BAR complex displaces Ypt7 from cargo-bound CSC during formation of recycling tubules. This explains how a single Rab can coordinate recycling and fusion on endosomes.

Indexed as

Biological TransportEndosomesGolgi ApparatusLysosomesProtein Transportrab7 GTP-Binding Proteinsrab GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSorting NexinsVacuolesVesicular Transport Proteinsrab7 GTP-Binding Proteinsrab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsSorting NexinsVesicular Transport ProteinsYPT7 protein, S cerevisiae

Identifiers

PMID28100638
PMCPMC5349785
OpenAlexW2575593256

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.