Evidence map›Paper›PMID 11038177›Full record

ArticleThe Journal of cell biology2000

Sorting of yeast membrane proteins into an endosome-to-Golgi pathway involves direct interaction of their cytosolic domains with Vps35p.

S F Nothwehr, S A Ha, P Bruinsma

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

88 citing papers in PubMed, 194 citations in OpenAlex.

  1. Article
  2. Endocytosis and trans-Golgi Network in Yeast.Sub-cellular biochemistry · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Navigating the Controversies of Retromer-Mediated Endosomal Protein Sorting.Frontiers in cell and developmental biology · 2021
    Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. Article

28 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

3 authors at 1 institution in 1 country.

S F NothwehrDivision of Biological Sciences, University of Missouri, Columbia, Missouri 65211, USA. nothwehrs@missouri.edu
S A Ha
P Bruinsma
University of Missouri · US

Funding

ANALYSIS OF GOLGI MEMBRANE PROTEIN LOCALIZATION IN YEASTR01GM053449 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI NOTHWEHR, STEVEN F · 2000 to 2003
$749k
YEAST LATE GOLGI MEMBRANE PROTEIN RETENTIONR29GM053449 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI NOTHWEHR, STEVEN F · 1995 to 1999
–
NIGMS NIH HHS GM53449NIGMS NIH HHS R01 GM053449NIGMS NIH HHS R29 GM053449
6 · The paper itself

Abstract

Resident late-Golgi membrane proteins in Saccharomyces cerevisiae are selectively retrieved from a prevacuolar-endosomal compartment, a process dependent on aromatic amino acid-based sorting determinants on their cytosolic domains. The formation of retrograde vesicles from the prevacuolar compartment and the selective recruitment of vesicular cargo are thought to be mediated by a peripheral membrane retromer protein complex. We previously described mutations in one of the retromer subunit proteins, Vps35p, which caused cargo-specific defects in retrieval. By genetic and biochemical means we now show that Vps35p directly associates with the cytosolic domains of cargo proteins. Chemical cross-linking, followed by coimmunoprecipitation, demonstrated that Vps35p interacts with the cytosolic domain of A-ALP, a model late-Golgi membrane protein, in a retrieval signal-dependent manner. Furthermore, mutations in the cytosolic domains of A-ALP and another cargo protein, Vps10p, were identified that suppressed cargo-specific mutations in Vps35p but did not suppress the retrieval defects of a vps35 null mutation. Suppression was shown to be due to an improvement in protein sorting at the prevacuolar compartment. These data strongly support a model in which Vps35p acts as a "receptor" protein for recognition of the retrieval signal domains of cargo proteins during their recruitment into retrograde vesicles.

Indexed as

Carrier ProteinsProtein TransportSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsAlkaline PhosphataseCell PolarityDipeptidyl-Peptidases and Tripeptidyl-PeptidasesEndosomesFungal ProteinsGolgi ApparatusMembrane ProteinsModels, BiologicalMutationProtein Sorting SignalsProtein Structure, TertiaryReceptors, Cell SurfaceAlkaline PhosphataseCarrier ProteinsDipeptidyl-Peptidases and Tripeptidyl-PeptidasesFungal ProteinsMembrane ProteinsPEP1 protein, S cerevisiaeProtein Sorting SignalsReceptors, Cell SurfaceRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSignal Recognition ParticleSTE13 protein, S cerevisiaeVesicular Transport ProteinsVPS35 protein, S cerevisiae

Identifiers

PMID11038177
PMCPMC2192648
OpenAlexW2121939655

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.