Evidence map›Paper›PMID 35938928›Full record

ArticleeLife2022

The VINE complex is an endosomal VPS9-domain GEF and SNX-BAR coat.

Shawn P Shortill, Mia S Frier, Ponthakorn Wongsangaroonsri, Michael Davey, Elizabeth Conibear

Open access · goldAbstract read
In one paragraph

Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.9field-weighted citation impact, top 30% 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

6 citing papers in PubMed, 9 citations in OpenAlex.

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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 1 institution in 1 country.

Shawn P ShortillDepartment of Medical Genetics, University of British Columbia, Vancouver, Canada.ORCID 0000-0001-8742-7442
Mia S FrierDepartment of Medical Genetics, University of British Columbia, Vancouver, Canada.ORCID 0000-0002-5634-3235
Ponthakorn WongsangaroonsriCentre for Molecular Medicine and Therapeutics, British Columbia Children's Hospital Research Institute, University of British Columbia, Vancouver, Canada.
Michael DaveyCentre for Molecular Medicine and Therapeutics, British Columbia Children's Hospital Research Institute, University of British Columbia, Vancouver, Canada.ORCID 0000-0002-1172-5934
Elizabeth ConibearDepartment of Medical Genetics, University of British Columbia, Vancouver, Canada.ORCID 0000-0001-5129-0499
University of British Columbia · CA

Funding

CIHR 247169CIHR 365914
6 · The paper itself

Abstract

Membrane trafficking pathways perform important roles in establishing and maintaining the endosomal network. Retrograde protein sorting from the endosome is promoted by conserved SNX-BAR-containing coat complexes including retromer which enrich cargo at tubular microdomains and generate transport carriers. In metazoans, retromer cooperates with VARP, a conserved VPS9-domain GEF, to direct an endosomal recycling pathway. The function of the yeast VARP homolog Vrl1 has been overlooked due to an inactivating mutation found in commonly studied strains. Here, we demonstrate that Vrl1 has features of a SNX-BAR coat protein and forms an obligate complex with Vin1, the paralog of the retromer SNX-BAR protein Vps5. Unique features in the Vin1 N-terminus allow Vrl1 to distinguish it from Vps5, thereby forming a complex that we have named VINE. The VINE complex occupies endosomal tubules and redistributes a conserved mannose 6-phosphate receptor-like protein from endosomes. We also find that membrane recruitment by Vin1 is essential for Vrl1 GEF activity, suggesting that VINE is a multifunctional coat complex that regulates trafficking and signaling events at the endosome.

Indexed as

Saccharomyces cerevisiae ProteinsSorting NexinsEndosomesGuanine Nucleotide Exchange FactorsMannosePhosphatesProtein TransportSaccharomyces cerevisiaeVesicular Transport ProteinsGuanine Nucleotide Exchange FactorsMannosePhosphatesSaccharomyces cerevisiae ProteinsSorting NexinsVesicular Transport ProteinsVPS9 protein, S cerevisiaecell biologygeneticsgenomicsretromerS. cerevisiaeVINEVps5Vps501Vrl1Ykr078w

Identifiers

PMID35938928
PMCPMC9507130
OpenAlexW4290648813

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.