Evidence map›Paper›PMID 19812245›Full record

ArticleMolecular biology of the cell2009

The exomer coat complex transports Fus1p to the plasma membrane via a novel plasma membrane sorting signal in yeast.

Robyn M Barfield, J Christopher Fromme, Randy Schekman

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

39 citing papers in PubMed, 62 citations in OpenAlex.

  1. Rethinking the Yeast Endomembrane System.Sub-cellular biochemistry · 2026
    Review
  2. Article
  3. Conventional and Unconventional Protein Secretion in Yeast and Animal Cells.Methods in molecular biology (Clifton, N.J.) · 2024
    Review
  4. Chitin Synthesis in Yeast: A Matter of Trafficking.International journal of molecular sciences · 2022
    Review
  5. Article
  6. Article
  7. Exomer complex regulates protein traffic at the TGN through differential interactions with cargos and clathrin adaptor complexes.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Endosomal trafficking of yeast membrane proteins.Biochemical Society transactions · 2018
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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.

Robyn M BarfieldDepartment of Molecular and Cell Biology and Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, CA, 94720, USA.
J Christopher Fromme
Randy Schekman
Howard Hughes Medical Institute · US

Funding

MOLECULAR STUDIES OF EUKARYOTIC CELL SURFACE GROWTHR01GM026755 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI SCHEKMAN, RANDY W. · 1985 to 2005
$1.1M
Control of polarized cell surface assemblyF32GM071164 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BARFIELD, ROBYN · 2004 to 2006
$134k
Howard Hughes Medical InstituteNIGMS NIH HHS F32 GM071164NIGMS NIH HHS F32-GM-071164-03NIGMS NIH HHS GM-26755NIGMS NIH HHS R01 GM026755
6 · The paper itself

Abstract

Sorting of transmembrane cargo proteins to different cellular compartments is mediated by sorting signals that are recognized by coat proteins involved in vesicle biogenesis. We have identified a sorting signal in the yeast cell fusion protein Fus1p that is required for its transport from the trans-Golgi compartment to the plasma membrane. Transport of Fus1p from the trans-Golgi to the cell surface is dependent on Chs5p, a component of the multisubunit exomer complex. We show that Fus1p transport is also dependent on the exomer components Bch1p and Bud7p. Disruption of the clathrin adaptor protein complex 1 (AP-1) restores Fus1p localization to the cell surface in the absence of exomer, possibly by promoting an alternate, exomer-independent route of transport. Mutation of an IXTPK sequence in the cytosolic tail of Fus1p abolishes its physical interaction with Chs5p, results in mislocalization of Fus1p, and therefore causes a cell fusion defect. These defects are suppressed by disruption of AP-1. We suggest that IXTPK comprises a novel sorting signal that is recognized and bound by exomer leading to the capture of Fus1p into coated vesicles en route to the cell surface.

Indexed as

Protein Sorting SignalsAmino Acid SequenceCell MembraneChitin SynthaseCoated VesiclesExocytosisMembrane FusionMembrane ProteinsMolecular Sequence DataMutationProtein TransportRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentTranscription Factor AP-1Chitin SynthaseCHS5 protein, S cerevisiaeFUS1 protein, S cerevisiaeMembrane ProteinsProtein Sorting SignalsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsTranscription Factor AP-1

Identifiers

PMID19812245
PMCPMC2785741
OpenAlexW2136176984

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.