Evidence map›Paper›PMID 27097106›Full record

ArticleeLife2016

Selective sorting and destruction of mitochondrial membrane proteins in aged yeast.

Adam L Hughes, Casey E Hughes, Kiersten A Henderson, Nina Yazvenko, Daniel E Gottschling

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
7.0field-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

83 citing papers in PubMed, 152 citations in OpenAlex.

  1. Article
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  3. Article
  4. Article
  5. Review
  6. Review
  7. Vacuolar-type HNature communications · 2025
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Mechanisms of heme transport in the mitochondria.Biochemical Society transactions · 2025
    Review
  14. Review
  15. Article
  16. Molecular mechanisms of mitochondrial dynamics.Nature reviews. Molecular cell biology · 2025
    Review
  17. Review
  18. Article
  19. Article
  20. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Adam L HughesDivision of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, United States.ORCID 0000-0002-7095-3793
Casey E HughesDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.
Kiersten A HendersonDivision of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, United States.
Nina YazvenkoDivision of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, United States.
Daniel E GottschlingDivision of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, United States.ORCID 0000-0002-7303-6552
Fred Hutch Cancer Center · USUniversity of Utah · US

Funding

Mechanism of increase genomic instability in aging yeastR01AG023779 · NIA · FRED HUTCHINSON CANCER RESEARCH CENTER · PI PARKHURST, SUSAN M · 2004 to 2019
$4.2M
Dissecting the mechanism of increased genomic instability in aging yeastR37AG023779 · NIA · FRED HUTCHINSON CANCER RESEARCH CENTER · PI GOTTSCHLING, DANIEL E. · 2010 to 2015
$2.9M
Mechanisms of organelle deteriorationR01AG037512 · NIA · FRED HUTCHINSON CANCER RESEARCH CENTER · PI GOTTSCHLING, DANIEL E. · 2011 to 2015
$2.2M
Role of Mitophagy in Mitochondrial Protein Quality ControlR00AG043095 · NIA · UNIVERSITY OF UTAH · PI HUGHES, ADAM · 2014 to 2016
$740k
Role of Mitophagy in Mitochondrial Protein Quality ControlK99AG043095 · NIA · FRED HUTCHINSON CANCER RESEARCH CENTER · PI HUGHES, ADAM · 2013 to 2013
$90k
NIA NIH HHS K99 AG043095NIA NIH HHS R00 AG043095NIA NIH HHS R01 AG023779NIA NIH HHS R01 AG037512NIA NIH HHS R37 AG023779
6 · The paper itself

Abstract

Mitochondrial dysfunction is a hallmark of aging, and underlies the development of many diseases. Cells maintain mitochondrial homeostasis through a number of pathways that remodel the mitochondrial proteome or alter mitochondrial content during times of stress or metabolic adaptation. Here, using yeast as a model system, we identify a new mitochondrial degradation system that remodels the mitochondrial proteome of aged cells. Unlike many common mitochondrial degradation pathways, this system selectively removes a subset of membrane proteins from the mitochondrial inner and outer membranes, while leaving the remainder of the organelle intact. Selective removal of preexisting proteins is achieved by sorting into a mitochondrial-derived compartment, or MDC, followed by release through mitochondrial fission and elimination by autophagy. Formation of MDCs requires the import receptors Tom70/71, and failure to form these structures exacerbates preexisting mitochondrial dysfunction, suggesting that the MDC pathway provides protection to mitochondria in times of stress.

Indexed as

AgedHumansMitochondrial MembranesMitochondrial ProteinsProtein TransportProteolysisSaccharomyces cerevisiaeMitochondrial Proteinsagingautophagycell biologylysosomeMDCmitochondriaprotein degradationS. cerevisiaevacuoleyeast

Identifiers

PMID27097106
PMCPMC4889329
OpenAlexW2341273528

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.