Evidence map›Paper›PMID 18039934›Full record

ArticleThe Journal of cell biology2007

Alternative function for the mitochondrial SAM complex in biogenesis of alpha-helical TOM proteins.

Diana Stojanovski, Bernard Guiard, Vera Kozjak-Pavlovic, Nikolaus Pfanner, Chris Meisinger

Erratum issuedAbstract read
In one paragraph

Article in The Journal of cell biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
–field-weighted citation impact
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

52 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Review
  6. Sensing, signaling and surviving mitochondrial stress.Cellular and molecular life sciences : CMLS · 2021
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. The Role of Mitochondrial Stress in Muscle Wasting Following Severe Burn Trauma.Journal of burn care & research : official publication of the American Burn Association · 2018
    Review
  15. Transmembrane β-barrels: Evolution, folding and energetics.Biochimica et biophysica acta. Biomembranes · 2017
    Review
  16. Article
  17. Article
  18. Article
  19. How lipids modulate mitochondrial protein import.Journal of bioenergetics and biomembranes · 2016
    Review
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors.

Diana StojanovskiInstitut für Biochemie und Molekularbiologie, Zentrum für Biochemie und Molekulare Zellforschung, Universität Freiburg, D-79104 Freiburg, Germany.
Bernard Guiard
Vera Kozjak-Pavlovic
Nikolaus Pfanner
Chris Meisinger

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mitochondrial outer membrane contains two preprotein translocases: the general translocase of outer membrane (TOM) and the beta-barrel-specific sorting and assembly machinery (SAM). TOM functions as the central entry gate for nuclear-encoded proteins. The channel-forming Tom40 is a beta-barrel protein, whereas all Tom receptors and small Tom proteins are membrane anchored by a transmembrane alpha-helical segment in their N- or C-terminal portion. Synthesis of Tom precursors takes place in the cytosol, and their import occurs via preexisting TOM complexes. The precursor of Tom40 is then transferred to SAM for membrane insertion and assembly. Unexpectedly, we find that the biogenesis of alpha-helical Tom proteins with a membrane anchor in the C-terminal portion is SAM dependent. Each SAM protein is necessary for efficient membrane integration of the receptor Tom22, whereas assembly of the small Tom proteins depends on Sam37. Thus, the substrate specificity of SAM is not restricted to beta-barrel proteins but also includes the majority of alpha-helical Tom proteins.

Indexed as

Membrane Transport ProteinsMitochondriaMitochondrial MembranesMitochondrial Membrane Transport ProteinsMitochondrial ProteinsMitochondrial SwellingMultiprotein ComplexesMutationProtein PrecursorsProtein Structure, SecondaryProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMembrane Transport ProteinsMitochondrial Membrane Transport ProteinsMitochondrial ProteinsMultiprotein ComplexesProtein PrecursorsProtein SubunitsSaccharomyces cerevisiae ProteinsSam35 protein, S cerevisiaeTOM22 protein, S cerevisiae

Identifiers

PMID18039934
PMCPMC2099199

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Registered trials

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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.