Evidence map›Paper›PMID 28906250›Full record

ArticleeLife2017

The AAA protein Msp1 mediates clearance of excess tail-anchored proteins from the peroxisomal membrane.

Nicholas R Weir, Roarke A Kamber, James S Martenson, Vladimir Denic

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.1field-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

51 citing papers in PubMed, 84 citations in OpenAlex.

  1. Review
  2. Article
  3. Function and regulation of the mitochondrial stress response.Nature structural & molecular biology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. The AAA+ protein Msp1 recognizes substrates by a hydrophobic mismatch.bioRxiv : the preprint server for biology · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. The Endoplasmic Reticulum and the Fidelity of Nascent Protein Localization.Cold Spring Harbor perspectives in biology · 2023
    Review
  16. Article
  17. Article
  18. Article
  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

4 authors at 1 institution in 2 countries.

Nicholas R WeirDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, United States.ORCID http://orcid.org/0000-0002-1797-849X
Roarke A KamberDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, United States.
James S MartensonDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, United States.
Vladimir DenicDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, United States.ORCID http://orcid.org/0000-0002-1982-7281
Harvard University · US

Funding

Training in Molecular, Cellular, and Chemical BiologyT32GM007598 · NIGMS · HARVARD UNIVERSITY · PI DULAC, CATHERINE · 1985 to 2019
$16.2M
Mechanistic dissection of eukaryotic protein biogenesis and degradation pathwaysR35GM127136 · NIGMS · HARVARD UNIVERSITY · PI Vladimir Denic · 2018 to 2026
$5.0M
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 GM099943NIGMS NIH HHS R35 GM127136NIGMS NIH HHS T32 GM007598
6 · The paper itself

Abstract

Msp1 is a conserved AAA ATPase in budding yeast localized to mitochondria where it prevents accumulation of mistargeted tail-anchored (TA) proteins, including the peroxisomal TA protein Pex15. Msp1 also resides on peroxisomes but it remains unknown how native TA proteins on mitochondria and peroxisomes evade Msp1 surveillance. We used live-cell quantitative cell microscopy tools and drug-inducible gene expression to dissect Msp1 function. We found that a small fraction of peroxisomal Pex15, exaggerated by overexpression, is turned over by Msp1. Kinetic measurements guided by theoretical modeling revealed that Pex15 molecules at mitochondria display age-independent Msp1 sensitivity. By contrast, Pex15 molecules at peroxisomes are rapidly converted from an initial Msp1-sensitive to an Msp1-resistant state. Lastly, we show that Pex15 interacts with the peroxisomal membrane protein Pex3, which shields Pex15 from Msp1-dependent turnover. In sum, our work argues that Msp1 selects its substrates on the basis of their solitary membrane existence.

Indexed as

Adenosine TriphosphatasesIntracellular MembranesIntravital MicroscopyMembrane ProteinsPeroxisomesPhosphoproteinsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesMembrane ProteinsMSP1 protein, S cerevisiaePEX15 protein, S cerevisiaePhosphoproteinsSaccharomyces cerevisiae ProteinsAAA ATPasecell biologymitochondriaperoxisomequality controlS. cerevisiaetail-anchored protein

Identifiers

PMID28906250
PMCPMC5633344
OpenAlexW2763915801

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.