Evidence map›Paper›PMID 24821790›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

The conserved AAA-ATPase Msp1 confers organelle specificity to tail-anchored proteins.

Voytek Okreglak, Peter Walter

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.

0numbers the graph read from it
0cells of the map it votes in
123citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

123 citing papers in PubMed, 226 citations in OpenAlex.

  1. Article
  2. Redox signals and oxidative stress in the control of mitochondrial protein import.Protein science : a publication of the Protein Society · 2026
    Review
  3. Article
  4. Function and regulation of the mitochondrial stress response.Nature structural & molecular biology · 2026
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Mitochondrial protein import stress.Nature cell biology · 2025
    Review
  15. Article
  16. Article
  17. Article
  18. Cryo-EM structure of AAA + ATPase thorase reveals novel helical filament formation.Computational and structural biotechnology journal · 2025
    Article
  19. Article
  20. Review

63 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Voytek OkreglakHoward Hughes Medical Institute and Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94158-2517.
Peter WalterHoward Hughes Medical Institute and Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94158-2517 peter@walterlab.ucsf.edu.
Howard 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
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM032384NIGMS NIH HHS R01GM32384
6 · The paper itself

Abstract

The accuracy of tail-anchored (TA) protein targeting to the endoplasmic reticulum (ER) depends on the Guided Entry of Tail-Anchored (Get) protein targeting machinery. The fate of TA proteins that become inappropriately inserted into other organelles, such as mitochondria, is unknown. Here, we identify Msp1, a conserved, membrane-anchored AAA-ATPase (ATPase associated with a variety of cellular activities) that localizes to mitochondria and peroxisomes, as a critical factor in a quality control pathway that senses and degrades TA proteins mistargeted to the outer mitochondrial membrane (OMM). Pex15 is normally targeted by the Get pathway to the ER, from where it travels to peroxisomes. Loss of Msp1 or loss of the Get pathway results in the redistribution of Pex15 to mitochondria. Cells lacking both a functional Get pathway and Msp1 accumulate increased amounts of Pex15 on the OMM and display severely dysfunctional mitochondrial morphology. In addition, Msp1 binds and promotes the turnover of a Pex15 mutant that is misdirected to the OMM. Our data suggest that Msp1 functions in local organelle surveillance by extracting mistargeted proteins, ensuring the fidelity of organelle specific-localization of TA proteins.

Indexed as

Adenosine TriphosphatasesConserved SequenceEndoplasmic ReticulumGreen Fluorescent ProteinsHydrophobic and Hydrophilic InteractionsMembrane ProteinsMitochondrial MembranesPeroxisomesPhosphoproteinsProtein Structure, TertiaryProtein TransportRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesGreen Fluorescent ProteinsMembrane ProteinsMSP1 protein, S cerevisiaePEX15 protein, S cerevisiaePhosphoproteinsRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID24821790
PMCPMC4050615
OpenAlexW2109283736

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.