Evidence map›Paper›PMID 26510789›Full record

ArticleGenetics2015

Evidence for a Nonendosomal Function of the Saccharomyces cerevisiae ESCRT-III-Like Protein Chm7.

Iva Bauer, Thomas Brune, Richard Preiss, Ralf Kölling

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed, 57 citations in OpenAlex.

  1. ESCRT-III function in membrane fission and repair.Nature reviews. Molecular cell biology · 2026
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  14. The many functions of ESCRTs.Nature reviews. Molecular cell biology · 2020
    Review
  15. Article
  16. Article
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  18. ESCRT-dependent control of membrane remodelling during cell division.Seminars in cell & developmental biology · 2018
    Review
  19. Review
  20. LEM2 recruits CHMP7 for ESCRT-mediated nuclear envelope closure in fission yeast and human cells.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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

4 authors at 2 institutions in 2 countries.

Iva BauerInstitut für Lebensmittelwissenschaft und Biotechnologie, Fg. Hefegenetik und Gärungstechnologie, Universität Hohenheim, 70599 Stuttgart, Germany.
Thomas BruneInstitut für Lebensmittelwissenschaft und Biotechnologie, Fg. Hefegenetik und Gärungstechnologie, Universität Hohenheim, 70599 Stuttgart, Germany.
Richard PreissDepartment of Molecular and Cellular Biology, University of Guelph, Ontario, Canada N1G 2W1.
Ralf KöllingInstitut für Lebensmittelwissenschaft und Biotechnologie, Fg. Hefegenetik und Gärungstechnologie, Universität Hohenheim, 70599 Stuttgart, Germany ralf.koelling@uni-hohenheim.de.
University of Hohenheim · DEUniversity of Guelph · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endosomal sorting complex required for transport (ESCRT) proteins are involved in a number of cellular processes, such as endosomal protein sorting, HIV budding, cytokinesis, plasma membrane repair, and resealing of the nuclear envelope during mitosis. Here we explored the function of a noncanonical member of the ESCRT-III protein family, the Saccharomyces cerevisiae ortholog of human CHMP7. Very little is known about this protein. In silico analysis predicted that Chm7 (yeast ORF YJL049w) is a fusion of an ESCRT-II and ESCRT-III-like domain, which would suggest a role in endosomal protein sorting. However, our data argue against a role of Chm7 in endosomal protein sorting. The turnover of the endocytic cargo protein Ste6 and the vacuolar protein sorting of carboxypeptidase S (CPS) were not affected by CHM7 deletion, and Chm7 also responded very differently to a loss in Vps4 function compared to a canonical ESCRT-III protein. Our data indicate that the Chm7 function could be connected to the endoplasmic reticulum (ER). In line with a function at the ER, we observed a strong negative genetic interaction between the deletion of a gene function (APQ12) implicated in nuclear pore complex assembly and messenger RNA (mRNA) export and the CHM7 deletion. The patterns of genetic interactions between the APQ12 deletion and deletions of ESCRT-III genes, two-hybrid interactions, and the specific localization of mCherry fusion proteins are consistent with the notion that Chm7 performs a novel function at the ER as part of an alternative ESCRT-III complex.

Indexed as

Adaptor Proteins, Signal TransducingATP-Binding Cassette TransportersEndocytosisEndoplasmic ReticulumEndosomal Sorting Complexes Required for TransportProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingATP-Binding Cassette TransportersChm7 protein, S cerevisiaeEndosomal Sorting Complexes Required for TransportSaccharomyces cerevisiae ProteinsSTE6 protein, S cerevisiaeendoplasmic reticulumendosomeESCRT-IIImultivesicular bodyprotein degradation

Identifiers

PMID26510789
PMCPMC4676514
OpenAlexW2175359650

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.