Evidence map›Paper›PMID 11179429›Full record

ArticleMolecular biology of the cell2001

Vps10p transport from the trans-Golgi network to the endosome is mediated by clathrin-coated vesicles.

O Deloche, B G Yeung, G S Payne, R Schekman

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

27 citing papers in PubMed, 56 citations in OpenAlex.

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  2. Review
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  7. Tetrahymena thermophila: a divergent perspective on membrane traffic.Journal of experimental zoology. Part B, Molecular and developmental evolution · 2014
    Review
  8. Article
  9. Article
  10. Review
  11. The Vps10p-domain receptor family.Cellular and molecular life sciences : CMLS · 2009
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
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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

4 authors at 3 institutions in 2 countries.

O DelocheHoward Hughes Medical Institute and Department of Molecular and Cell Biology, University of California, 229 Stanley Hall, Berkeley, California 94720-3206, USA.
B G Yeung
G S Payne
R Schekman
University of California, Los Angeles · USHoward Hughes Medical Institute · USUniversity of Geneva · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A native immunoisolation procedure has been used to investigate the role of clathrin-coated vesicles (CCVs) in the transport of vacuolar proteins between the trans-Golgi network (TGN) and the prevacuolar/endosome compartments in the yeast Saccharomyces cerevisiae. We find that Apl2p, one large subunit of the adaptor protein-1 complex, and Vps10p, the carboxypeptidase Y vacuolar protein receptor, are associated with clathrin molecules. Vps10p packaging in CCVs is reduced in pep12 Delta and vps34 Delta, two mutants that block Vps10p transport from the TGN to the endosome. However, Vps10p sorting is independent of Apl2p. Interestingly, a Vps10C(t) Delta p mutant lacking its C-terminal cytoplasmic domain, the portion of the receptor responsible for carboxypeptidase Y sorting, is also coimmunoprecipitated with clathrin. Our results suggest that CCVs mediate Vps10p transport from the TGN to the endosome independent of direct interactions between Vps10p and clathrin coats. The Vps10p C-terminal domain appears to play a principal role in retrieval of Vps10p from the prevacuolar compartment rather than in sorting from the TGN.

Indexed as

Proprotein ConvertasesSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsAdaptor Protein Complex beta SubunitsAspartic Acid EndopeptidasesCell MembraneClathrinClathrin-Coated VesiclesEndosomesFungal ProteinsMembrane ProteinsMutationPrecipitin TestsProtein TransportQa-SNARE ProteinsReceptors, Cell SurfaceAdaptor Protein Complex beta SubunitsAPL2 protein, S cerevisiaeAspartic Acid Endopeptidasesaspartic proteinase AClathrinFungal ProteinsKEX2 protein, S cerevisiaeMembrane ProteinsPEP12 protein, S cerevisiaePEP1 protein, S cerevisiaeProprotein ConvertasesQa-SNARE ProteinsReceptors, Cell SurfaceSaccharomyces cerevisiae ProteinsSubtilisinsVesicular Transport Proteins

Identifiers

PMID11179429
PMCPMC30957
OpenAlexW2136743991

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.