Evidence map›Paper›PMID 26451041›Full record

ArticleThe Journal of biological chemistry2015

Mechanism of Assembly of a Substrate Transfer Complex during Tail-anchored Protein Targeting.

Harry B Gristick, Michael E Rome, Justin W Chartron, Meera Rao, Sonja Hess, Shu-ou Shan, William M Clemons

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

14 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. A protean clamp guides membrane targeting of tail-anchored proteins.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Mechanisms of Tail-Anchored Membrane Protein Targeting and Insertion.Annual review of cell and developmental biology · 2017
    Review
  13. Article
  14. 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

7 authors at 1 institution in 1 country.

Harry B GristickFrom the Division of Chemistry and Chemical Engineering and.
Michael E RomeFrom the Division of Chemistry and Chemical Engineering and.
Justin W ChartronFrom the Division of Chemistry and Chemical Engineering and.
Meera RaoFrom the Division of Chemistry and Chemical Engineering and.
Sonja HessThe Proteome Exploration Laboratory, Beckman Institute, California Institute of Technology, Pasadena, California 91125.
Shu-ou ShanFrom the Division of Chemistry and Chemical Engineering and sshan@caltech.edu.
William M ClemonsFrom the Division of Chemistry and Chemical Engineering and clemons@caltech.edu.
California Institute of Technology · US

Funding

PREDOCTORAL TRAINING IN BIOLOGY AND CHEMISTRYT32GM007616 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI STERNBERG, PAUL WARREN · 1985 to 2019
$22.9M
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
Targeting of tail-anchored membrane proteins by the Get pathway.R01GM097572 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI CLEMONS, WILLIAM M. · 2011 to 2015
$1.5M
NIGMS NIH HHS 5T32GM007616-33NIGMS NIH HHS R01 GM097572NIGMS NIH HHS R01GM097572NIGMS NIH HHS R01 GM107368NIGMS NIH HHS R01GM107368NIGMS NIH HHS T32 GM007616
6 · The paper itself

Abstract

Tail-anchored (TA) proteins, defined as having a single transmembrane helix at their C terminus, are post-translationally targeted to the endoplasmic reticulum membrane by the guided entry of TA proteins (GET) pathway. In yeast, the handover of TA substrates is mediated by the heterotetrameric Get4/Get5 complex (Get4/5), which tethers the co-chaperone Sgt2 to the targeting factor, the Get3 ATPase. Binding of Get4/5 to Get3 is critical for efficient TA targeting; however, questions remain about the formation of the Get3·Get4/5 complex. Here we report crystal structures of a Get3·Get4/5 complex from Saccharomyces cerevisiae at 2.8 and 6.0 Å that reveal a novel interface between Get3 and Get4 dominated by electrostatic interactions. Kinetic and mutational analyses strongly suggest that these structures represent an on-pathway intermediate that rapidly assembles and then rearranges to the final Get3·Get4/5 complex. Furthermore, we provide evidence that the Get3·Get4/5 complex is dominated by a single Get4/5 heterotetramer bound to one monomer of a Get3 dimer, uncovering an intriguing asymmetry in the Get4/5 heterotetramer upon Get3 binding. Ultrafast diffusion-limited electrostatically driven Get3·Get4/5 association enables Get4/5 to rapidly sample and capture Get3 at different stages of the GET pathway.

Indexed as

Amino Acid SequenceKineticsModels, MolecularMolecular Sequence DataProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidStatic ElectricitySubstrate SpecificitySaccharomyces cerevisiae Proteinskineticsmembrane proteinprotein targetingSaccharomyces cerevisiaestructural biology

Identifiers

PMID26451041
PMCPMC4705998
OpenAlexW1771817800

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.