Evidence map›Paper›PMID 38664330›Full record

ReviewFEBS open bio2024

Protein insertion into the inner membrane of mitochondria: routes and mechanisms.

Büsra Kizmaz, Annika Nutz, Annika Egeler, Johannes M Herrmann

Open access · goldAbstract readReview
In one paragraph

Review in FEBS open bio, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

12 citing papers in PubMed, 12 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. Review
  4. Functions of J-domain proteins in mitochondrial protein biogenesis.Protein science : a publication of the Protein Society · 2026
    Review
  5. In and out of the mitochondrial intermembrane space.Protein science : a publication of the Protein Society · 2026
    Review
  6. Mitochondrial presequences are more than just address labels.Protein science : a publication of the Protein Society · 2026
    Review
  7. Article
  8. Mitochondria transfer in tissue homeostasis and diseases.International journal of biological sciences · 2026
    Review
  9. Review
  10. Review
  11. Article
  12. Article
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 1 country.

Büsra KizmazCell Biology, University of Kaiserslautern, RPTU, Germany.ORCID https://orcid.org/0000-0002-9179-973X
Annika NutzCell Biology, University of Kaiserslautern, RPTU, Germany.
Annika EgelerCell Biology, University of Kaiserslautern, RPTU, Germany.
Johannes M HerrmannCell Biology, University of Kaiserslautern, RPTU, Germany.ORCID https://orcid.org/0000-0003-2081-4506
University of Kaiserslautern · DE

Funding

Deutsche Forschungsgemeinschaft GRK2737-STRESSistanceLandesforschungsinitiative Rheinland-Pfalz
6 · The paper itself

Abstract

The inner membrane of mitochondria contains hundreds of different integral membrane proteins. These proteins transport molecules into and out of the matrix, they carry out multifold catalytic reactions and they promote the biogenesis or degradation of mitochondrial constituents. Most inner membrane proteins are encoded by nuclear genes and synthesized in the cytosol from where they are imported into mitochondria by translocases in the outer and inner membrane. Three different import routes direct proteins into the inner membrane and allow them to acquire their appropriate membrane topology. First, mitochondrial import intermediates can be arrested at the level of the TIM23 inner membrane translocase by a stop-transfer sequence to reach the inner membrane by lateral insertion. Second, proteins can be fully translocated through the TIM23 complex into the matrix from where they insert into the inner membrane in an export-like reaction. Carriers and other polytopic membrane proteins embark on a third insertion pathway: these hydrophobic proteins employ the specialized TIM22 translocase to insert from the intermembrane space (IMS) into the inner membrane. This review article describes these three targeting routes and provides an overview of the machinery that promotes the topogenesis of mitochondrial inner membrane proteins.

Indexed as

MitochondriaMitochondrial MembranesMitochondrial Membrane Transport ProteinsProtein TransportAnimalsHumansMembrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsSaccharomyces cerevisiae ProteinsMembrane Transport ProteinsMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsSaccharomyces cerevisiae Proteinscarrier proteinsmembrane proteinsmitochondriaprotein importTIM22 complexTIM23 complex

Identifiers

PMID38664330
PMCPMC11452304
OpenAlexW4395669869

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.