Evidence map›Paper›PMID 20516149›Full record

ArticleJournal of cell science2010

Bat3 promotes the membrane integration of tail-anchored proteins.

Pawel Leznicki, Anne Clancy, Blanche Schwappach, Stephen High

Abstract read
In one paragraph

Article in Journal of cell science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

77 citing papers in PubMed, 122 citations in OpenAlex.

  1. Review
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  9. A second chance for protein targeting/folding: Ubiquitination and deubiquitination of nascent proteins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022
    Review
  10. Article
  11. Article
  12. Review
  13. Structural insights into metazoan pretargeting GET complexes.Nature structural & molecular biology · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

17 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

4 authors at 1 institution in 1 country.

Pawel LeznickiFaculty of Life Sciences, University of Manchester, Oxford Road, Manchester, M13 9PT, UK.
Anne Clancy
Blanche Schwappach
Stephen High
University of Manchester · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

The membrane integration of tail-anchored proteins at the endoplasmic reticulum (ER) is post-translational, with different tail-anchored proteins exploiting distinct cytosolic factors. For example, mammalian TRC40 has a well-defined role during delivery of tail-anchored proteins to the ER. Although its Saccharomyces cerevisiae equivalent, Get3, is known to function in concert with at least four other components, Get1, Get2, Get4 and Get5 (Mdy2), the role of additional mammalian proteins during tail-anchored protein biogenesis is unclear. To this end, we analysed the cytosolic binding partners of Sec61beta, a well-defined substrate of TRC40, and identified Bat3 as a previously unknown interacting partner. Depletion of Bat3 inhibits the membrane integration of Sec61beta, but not of a second, TRC40-independent, tail-anchored protein, cytochrome b5. Thus, Bat3 influences the in vitro membrane integration of tail-anchored proteins using the TRC40 pathway. When expressed in Saccharomyces cerevisiae lacking a functional GET pathway for tail-anchored protein biogenesis, Bat3 associates with the resulting cytosolic pool of non-targeted chains and diverts it to the nucleus. This Bat3-mediated mislocalisation is not dependent upon Sgt2, a recently identified component of the yeast GET pathway, and we propose that Bat3 either modulates the TRC40 pathway in higher eukaryotes or provides an alternative fate for newly synthesised tail-anchored proteins.

Indexed as

Adenosine TriphosphateAnimalsCarrier ProteinsCell MembraneCytosolHumansMembrane ProteinsMembrane Transport ProteinsMolecular ChaperonesQa-SNARE ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSEC Translocation ChannelsSignal TransductionAdenosine TriphosphateBAG6 protein, humanCarrier ProteinsMembrane ProteinsMembrane Transport ProteinsMolecular ChaperonesQa-SNARE ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSEC61B protein, humanSEC61 protein, S cerevisiaeSEC Translocation ChannelsSed5 protein, S cerevisiaeSgt2 protein, S cerevisiae

Identifiers

PMID20516149
PMCPMC2886740
OpenAlexW2147420663

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.