Evidence map›Paper›PMID 18768754›Full record

ArticleMolecular biology of the cell2008

Opposing activities of the Snx3-retromer complex and ESCRT proteins mediate regulated cargo sorting at a common endosome.

Todd I Strochlic, Briana C Schmiedekamp, Jacqueline Lee, David J Katzmann, Christopher G Burd

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

46 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
  6. Biological Basis of Cell Trafficking: A General Overview.Journal of inherited metabolic disease · 2025
    Review
  7. Article
  8. Article
  9. Receptor Recycling by Retromer.Molecular and cellular biology · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. 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

5 authors at 2 institutions in 1 country.

Todd I StrochlicDepartment of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6058, USA.
Briana C Schmiedekamp
Jacqueline Lee
David J Katzmann
Christopher G Burd
University of Pennsylvania · USMayo Clinic · US

Funding

TRAFFICKING BY FYVE DOMAIN EFFECTORS OF PI3 KINASER01GM061221 · NIGMS · YALE UNIVERSITY · PI BURD, CHRISTOPHER G · 2000 to 2016
$5.2M
Mechanisms of Endosomal SortingR01GM073024 · NIGMS · MAYO CLINIC ROCHESTER · PI KATZMANN, DAVID J · 2005 to 2013
$2.7M
Sorting and Trafficking in the Endosomal SystemR37GM061221 · NIGMS · YALE UNIVERSITY · PI BURD, CHRISTOPHER G · 2017 to 2021
$2.0M
NIGMS NIH HHS GM61221NIGMS NIH HHS R01 GM061221NIGMS NIH HHS R01 GM073024NIGMS NIH HHS R01 GM 73024NIGMS NIH HHS R37 GM061221
6 · The paper itself

Abstract

Endocytosed proteins are either delivered to the lysosome to be degraded or are exported from the endosomal system and delivered to other organelles. Sorting of the Saccharomyces cerevisiae reductive iron transporter, composed of the Fet3 and Ftr1 proteins, in the endosomal system is regulated by available iron; in iron-starved cells, Fet3-Ftr1 is sorted by Snx3/Grd19 and retromer into a recycling pathway that delivers it back to the plasma membrane, but when starved cells are exposed to iron, Fet3-Ftr1 is targeted to the lysosome-like vacuole and is degraded. We report that iron-induced endocytosis of Fet3-Ftr1 is independent of Fet3-Ftr1 ubiquitylation, and after endocytosis, degradation of Fet3-Ftr1 is mediated by the multivesicular body (MVB) sorting pathway. In mutant cells lacking any component of the ESCRT protein-dependent MVB sorting machinery, the Rsp5 ubiquitin ligase, or in wild-type cells expressing Fet3-Ftr1 lacking cytosolic lysyl ubiquitin acceptor sites, Fet3-Ftr1 is constitutively sorted into the recycling pathway independent of iron status. In the presence and absence of iron, Fet3-Ftr1 transits an endosomal compartment where a subunit of the MVB sorting receptor (Vps27), Snx3/Grd19, and retromer proteins colocalize. We propose that this endosome is where Rsp5 ubiquitylates Fet3-Ftr1 and where the recycling and degradative pathways diverge.

Indexed as

Carrier ProteinsCytosolEndocytosisEndosomesGreen Fluorescent ProteinsIronLysineModels, BiologicalMutationProtein TransportRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinationCarrier ProteinsGreen Fluorescent ProteinsIronLysineRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSNX3 protein, S cerevisiae

Identifiers

PMID18768754
PMCPMC2575174
OpenAlexW2150104537

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.