Evidence map›Paper›PMID 31999255›Full record

ArticleeLife2020

Structure of the AAA protein Msp1 reveals mechanism of mislocalized membrane protein extraction.

Lan Wang, Alexander Myasnikov, Xingjie Pan, Peter Walter

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
7.3field-weighted citation impact, top 3% 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

33 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
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  8. The AAA+ protein Msp1 recognizes substrates by a hydrophobic mismatch.bioRxiv : the preprint server for biology · 2024
    Article
  9. Article
  10. Molecular basis of FIGNL1 in dissociating RAD51 from DNA and chromatin.bioRxiv : the preprint server for biology · 2024
    Article
  11. Article
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  14. Article
  15. Article
  16. Article
  17. Visualization of the Cdc48 AAA+ ATPase protein unfolding pathway.bioRxiv : the preprint server for biology · 2023
    Article
  18. Article
  19. The Endoplasmic Reticulum and the Fidelity of Nascent Protein Localization.Cold Spring Harbor perspectives in biology · 2023
    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 at 3 institutions in 2 countries.

Lan WangHoward Hughes Medical Institute, Chevy Chase, Maryland, United States.ORCID 0000-0002-8931-7201
Alexander MyasnikovDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, United States.
Xingjie PanUCSF/UCB Graduate Program in Bioengineering, University of California, San Francisco, San Francisco, United States.
Peter WalterHoward Hughes Medical Institute, Chevy Chase, Maryland, United States.ORCID 0000-0002-6849-708X
Howard Hughes Medical Institute · USCentre National de la Recherche Scientifique · FRUniversity of California, San Francisco · US

Funding

MECHANISM OF PROTEIN TRANSLOCATION ACROSS MEMBRANESR01GM032384 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 1985 to 2023
$7.6M
Acquisition of an electron microscope for high-resolution single particle cryo-EMS10OD021741 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2016 to 2016
$2.0M
Linux cluster for near atomic resolution single particle cryo-EMS10OD020054 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2015 to 2015
$456k
Damon Runyon Cancer Research Foundation DRG-2312-17Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM032384NIH HHS S10 OD020054NIH HHS S10 OD021741
6 · The paper itself

Abstract

The AAA protein Msp1 extracts mislocalized tail-anchored membrane proteins and targets them for degradation, thus maintaining proper cell organization. How Msp1 selects its substrates and firmly engages them during the energetically unfavorable extraction process remains a mystery. To address this question, we solved cryo-EM structures of Msp1-substrate complexes at near-atomic resolution. Akin to other AAA proteins, Msp1 forms hexameric spirals that translocate substrates through a central pore. A singular hydrophobic substrate recruitment site is exposed at the spiral's seam, which we propose positions the substrate for entry into the pore. There, a tight web of aromatic amino acids grips the substrate in a sequence-promiscuous, hydrophobic milieu. Elements at the intersubunit interfaces coordinate ATP hydrolysis with the subunits' positions in the spiral. We present a comprehensive model of Msp1's mechanism, which follows general architectural principles established for other AAA proteins yet specializes Msp1 for its unique role in membrane protein extraction.

Indexed as

AAA ProteinsCryoelectron MicroscopyFungal ProteinsMembrane ProteinsProtein ConformationProtein TransportYeastsAAA ProteinsFungal ProteinsMembrane ProteinsAAA proteincryo-EME. colimitochondrial protein quality controlmolecular biophysicsprotein quality controlprotein structurestructural biologytail-anchored protein

Identifiers

PMID31999255
PMCPMC7018516
OpenAlexW3003695775

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.