Evidence map›Paper›PMID 27925580›Full record

ArticleeLife2016

Multiple selection filters ensure accurate tail-anchored membrane protein targeting.

Meera Rao, Voytek Okreglak, Un Seng Chio, Hyunju Cho, Peter Walter, Shu-Ou Shan

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

57 citing papers in PubMed, 93 citations in OpenAlex.

  1. Review
  2. Article
  3. YeastbioRxiv : the preprint server for biology · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. The AAA+ protein Msp1 recognizes substrates by a hydrophobic mismatch.bioRxiv : the preprint server for biology · 2024
    Article
  9. A unifying model for membrane protein biogenesis.Nature structural & molecular biology · 2024
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. The Endoplasmic Reticulum and the Fidelity of Nascent Protein Localization.Cold Spring Harbor perspectives in biology · 2023
    Review
  19. Article
  20. Review
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

6 authors at 2 institutions in 1 country.

Meera RaoDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, United States.
Voytek OkreglakHoward Hughes Medical Institute, University of California, San Francisco, United States.
Un Seng ChioDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, United States.
Hyunju ChoDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, United States.
Peter WalterHoward Hughes Medical Institute, University of California, San Francisco, United States.ORCID 0000-0002-6849-708X
Shu-Ou ShanDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, United States.ORCID 0000-0002-6526-1733
California Institute of Technology · USHoward Hughes Medical Institute · US

Funding

MECHANISM OF PROTEIN TRANSLOCATION ACROSS MEMBRANESR01GM032384 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 1985 to 2023
$7.6M
Structural Basis of Protein HomeostasisU01GM098254 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI AGARD, DAVID A., FRYDMAN, JUDITH · 2012 to 2014
$3.2M
Molecular mechanisms of post-translational targeting of tail-anchored proteins.R01GM107368 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI SHAN, SHU-OU · 2014 to 2019
$2.1M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM032384NIGMS NIH HHS R01 GM107368NIGMS NIH HHS U01 GM098254
6 · The paper itself

Abstract

Accurate protein localization is crucial to generate and maintain organization in all cells. Achieving accuracy is challenging, as the molecular signals that dictate a protein's cellular destination are often promiscuous. A salient example is the targeting of an essential class of tail-anchored (TA) proteins, whose sole defining feature is a transmembrane domain near their C-terminus. Here we show that the Guided Entry of Tail-anchored protein (GET) pathway selects TA proteins destined to the endoplasmic reticulum (ER) utilizing distinct molecular steps, including differential binding by the co-chaperone Sgt2 and kinetic proofreading after ATP hydrolysis by the targeting factor Get3. Further, the different steps select for distinct physicochemical features of the TA substrate. The use of multiple selection filters may be general to protein biogenesis pathways that must distinguish correct and incorrect substrates based on minor differences.

Indexed as

Protein TransportAdenosine TriphosphatasesAdenosine TriphosphateCarrier ProteinsEndoplasmic ReticulumGuanine Nucleotide Exchange FactorsHydrolysisMembrane ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesAdenosine TriphosphateCarrier ProteinsGet3 protein, S cerevisiaeGuanine Nucleotide Exchange FactorsMembrane ProteinsSaccharomyces cerevisiae ProteinsSgt2 protein, S cerevisiaeATPasebiochemistrybiological fidelitycell biologyfluorescence spectroscopyguided entry of tail anchored proteinsprotein targeting and translocationS. cerevisiae

Identifiers

PMID27925580
PMCPMC5214336
OpenAlexW2560350971

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.