Evidence map›Paper›PMID 20850366›Full record

ArticleMolecular cell2010

A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum.

Fei Wang, Emily C Brown, Gary Mak, Jimmy Zhuang, Vladimir Denic

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 130 papers.

0numbers the graph read from it
0cells of the map it votes in
130citing 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

130 citing papers in PubMed, 199 citations in OpenAlex.

  1. Review
  2. GET3 regulates apoptosis via tail-anchoring of MCL1.Cell death and differentiation · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. A unifying model for membrane protein biogenesis.Nature structural & molecular biology · 2024
    Review
  10. Article
  11. Modular Assembly of Mitochondrial β-Barrel Proteins.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  12. Multiomics ofInternational journal of molecular sciences · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. The Endoplasmic Reticulum and the Fidelity of Nascent Protein Localization.Cold Spring Harbor perspectives in biology · 2023
    Review
  17. Review
  18. Article
  19. Review
  20. Article

70 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

5 authors at 1 institution in 1 country.

Fei WangDepartment of Molecular and Cellular Biology, Harvard University, Northwest Labs, Cambridge, MA 02138, USA.
Emily C Brown
Gary Mak
Jimmy Zhuang
Vladimir Denic
Harvard University · US

Funding

Mechanistic analysis of post-translation membrane protein insertion into the ER.R01GM099943 · NIGMS · HARVARD UNIVERSITY · PI DENIC, VLADIMIR · 2012 to 2016
$1.6M
NIGMS NIH HHS R01 GM099943
6 · The paper itself

Abstract

Tail-anchored (TA) proteins are posttranslationally inserted into either the endoplasmic reticulum (ER) or the mitochondrial outer membrane. The C-terminal transmembrane domains (TMDs) of TA proteins enable their many essential cellular functions by specifying the membrane target, but how cells process these targeting signals is poorly understood. Here, we reveal the composition of a conserved multiprotein TMD recognition complex (TRC) and show that distinct TRC subunits recognize the two types of TMD signals. By engineering mutations in a mitochondrial TMD, we switch over its TRC subunit recognition, thus leading to its misinsertion into the ER. Biochemical reconstitution with purified components demonstrates that TRC tethers and enzymatically activates Get3 to selectively hand off ER-bound TA proteins to Get3. Thus, ER-bound TA proteins are sorted at the top of a TMD chaperone cascade that culminates with the formation of Get3-TA protein complexes, which are recruited to the ER membrane for insertion.

Indexed as

Protein Sorting SignalsAdenosine TriphosphatasesAmino Acid SequenceCarrier ProteinsEndoplasmic ReticulumGuanine Nucleotide Exchange FactorsMembrane ProteinsMitochondrial ProteinsMolecular ChaperonesMolecular Sequence DataMultiprotein ComplexesMutationProtein SubunitsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesCarrier ProteinsGet3 protein, S cerevisiaeGET4 protein, S cerevisiaeGuanine Nucleotide Exchange FactorsMdy2 protein, S cerevisiaeMembrane ProteinsMitochondrial ProteinsMolecular ChaperonesMultiprotein ComplexesProtein Sorting SignalsProtein SubunitsSaccharomyces cerevisiae ProteinsSgt2 protein, S cerevisiaeUbiquitin

Identifiers

PMID20850366
PMCPMC3652556
OpenAlexW2069538808

What OpenQuestion holds

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LicenceTDM
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.