Evidence map›Paper›PMID 14560025›Full record

ArticleMolecular and cellular biology2003

Mitochondria use different mechanisms for transport of multispanning membrane proteins through the intermembrane space.

Ann E Frazier, Agnieszka Chacinska, Kaye N Truscott, Bernard Guiard, Nikolaus Pfanner, Peter Rehling

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

29 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Article
  3. Cox15 interacts with the cytochromeThe Journal of biological chemistry · 2018
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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

6 authors at 2 institutions in 2 countries.

Ann E FrazierInstitut für Biochemie und Molekularbiologie. Fakultät für Biologie, Universität Freiburg, D-79104 Freiburg, Germany.
Agnieszka Chacinska
Kaye N Truscott
Bernard Guiard
Nikolaus Pfanner
Peter Rehling
Centre de Génétique Moléculaire · FRUniversity of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mitochondrial inner membrane contains numerous multispanning integral proteins. The precursors of these hydrophobic proteins are synthesized in the cytosol and therefore have to cross the mitochondrial outer membrane and intermembrane space to reach the inner membrane. While the import pathways of noncleavable multispanning proteins, such as the metabolite carriers, have been characterized in detail by the generation of translocation intermediates, little is known about the mechanism by which cleavable preproteins of multispanning proteins, such as Oxa1, are transferred from the outer membrane to the inner membrane. We have identified a translocation intermediate of the Oxa1 preprotein in the translocase of the outer membrane (TOM) and found that there are differences from the import mechanisms of carrier proteins. The intermembrane space domain of the receptor Tom22 supports the stabilization of the Oxa1 intermediate. Transfer of the Oxa1 preprotein to the inner membrane is not affected by inactivation of the soluble TIM complexes. Both the inner membrane potential and matrix heat shock protein 70 are essential to release the preprotein from the TOM complex, suggesting a close functional cooperation of the TOM complex and the presequence translocase of the inner membrane. We conclude that mitochondria employ different mechanisms for translocation of multispanning proteins across the aqueous intermembrane space.

Indexed as

Membrane Transport ProteinsReceptors, Cell SurfaceElectron Transport Complex IVFungal ProteinsHSP70 Heat-Shock ProteinsMacromolecular SubstancesMembrane PotentialsMembrane ProteinsMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial ProteinsNuclear ProteinsProtein PrecursorsProtein TransportSaccharomyces cerevisiae ProteinsCOX18 protein, S cerevisiaeElectron Transport Complex IVFungal ProteinsHSP70 Heat-Shock ProteinsMacromolecular SubstancesMembrane ProteinsMembrane Transport ProteinsMitochondrial Membrane Transport ProteinsMitochondrial ProteinsNuclear ProteinsOXA1 proteinProtein PrecursorsReceptors, Cell SurfaceSaccharomyces cerevisiae ProteinsTOM22 protein, S cerevisiae

Identifiers

PMID14560025
PMCPMC207575
OpenAlexW2107009106

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.