Evidence map›Paper›PMID 20696390›Full record

ReviewStructure (London, England : 1993)2010

Structures of Get3, Get4, and Get5 provide new models for TA membrane protein targeting.

Peter J Simpson, Blanche Schwappach, Henrik G Dohlman, Rivka L Isaacson

Abstract readComparative StudyReview
In one paragraph

Review in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
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

29 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. The roles of cytosolic quality control proteins, SGTA and the BAG6 complex, in disease.Advances in protein chemistry and structural biology · 2019
    Review
  11. Article
  12. Loss of GET pathway orthologs inProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  13. Article
  14. pHLIP Peptide Interaction with a Membrane Monitored by SAXS.The journal of physical chemistry. B · 2016
    Article
  15. Article
  16. Review
  17. Review
  18. Structure of the Sgt2/Get5 complex provides insights into GET-mediated targeting of tail-anchored membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  19. Review
  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

4 authors.

Peter J SimpsonDivision of Molecular Biosciences, Imperial College London, Exhibition Road, South Kensington, London SW7 2AZ, UK.
Blanche Schwappach
Henrik G Dohlman
Rivka L Isaacson

Funding

G Protein Signaling at the endosomeR01GM080739 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DOHLMAN, HENRIK G. · 2007 to 2014
$2.6M
Medical Research Council G0900936NIGMS NIH HHS GM080739NIGMS NIH HHS R01 GM080739Wellcome Trust
6 · The paper itself

Abstract

The GET pathway, using several proteins (Gets 1-5 and probably Sgt2), posttranslationally conducts tail-anchored (TA) proteins to the endoplasmic reticulum (ER). At the ER, TA proteins are inserted into the lipid bilayer and then sorted and directed to their respective destinations in the secretory pathway. Until last year, there was no structural information on any of the GET components but now there are ten crystal structures of Get3 in a variety of nucleotide-bound states and conformations. The structures of Get4 and a portion of Get5 also emerged in 2010. This minireview provides a detailed comparison of the GET structures and discusses their mechanistic relevance to TA protein insertion. It also addresses the outstanding gaps in detailed molecular information on this system, including the structures of Get5, Sgt2, and the transmembrane complex comprising Get1 and Get2.

Indexed as

Models, MolecularAdenosine TriphosphatasesCarrier ProteinsEndoplasmic ReticulumGuanine Nucleotide Exchange FactorsMembrane ProteinsModels, BiologicalProtein TransportSaccharomyces cerevisiae ProteinsSignal TransductionUbiquitinAdenosine TriphosphatasesCarrier ProteinsGet3 protein, S cerevisiaeGET4 protein, S cerevisiaeGuanine Nucleotide Exchange FactorsMdy2 protein, S cerevisiaeMembrane ProteinsSaccharomyces cerevisiae ProteinsUbiquitin

Identifiers

PMID20696390
PMCPMC3557799

What OpenQuestion holds

Textmetadata
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.