Evidence map›Paper›PMID 41676891›Full record

ReviewProtein science : a publication of the Protein Society2026

Mitochondrial presequences are more than just address labels.

Erik Marcel Heller, Svenja Lenhard, Doron Rapaport, Johannes Herrmann

Abstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Adaptation of OXPHOS biogenesis to cellular requirements.Protein science : a publication of the Protein Society · 2026
    Review
  2. Review
  3. Dynamic disorder is crucial for mitochondrial protein import.Protein science : a publication of the Protein Society · 2026
    Review
  4. Mitochondrial presequences are more than just address labels.Protein science : a publication of the Protein Society · 2026
    Review
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.

Erik Marcel HellerCell Biology, University of Kaiserslautern, RPTU, Kaiserslautern, Germany.ORCID https://orcid.org/0000-0001-6716-8180
Svenja LenhardCell Biology, University of Kaiserslautern, RPTU, Kaiserslautern, Germany.
Doron RapaportInterfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.
Johannes HerrmannCell Biology, University of Kaiserslautern, RPTU, Kaiserslautern, Germany.ORCID https://orcid.org/0000-0003-2081-4506

Funding

Deutsche Forschungsgemeinschaft 541210481Deutsche Forschungsgemeinschaft 541647314Deutsche Forschungsgemeinschaft HE2803/11-1Deutsche Forschungsgemeinschaft RA1028/11-1European Research Council (MitoCyto) 101052639Research Initiative of Rheinland-Pfalz (BioComp)
6 · The paper itself

Abstract

Most mitochondrial proteins are synthesized in the cytosol as precursor proteins with N-terminal presequences. These presequences serve as targeting signals that facilitate the binding to mitochondrial surface receptors and translocation across the mitochondrial membranes. However, recent studies showed that presequences can be more than address tags. They can contain degradation signals recognized by components of the ubiquitin-proteasome system, and therefore, serve as timers that determine the lifespan of newly synthesized precursor proteins. Moreover, presequences can interact with components of the cytosolic chaperone system to prevent or delay precursor folding. Finally, presequences of some dually localized proteins contain targeting information not only for mitochondria but also for other cellular destinations such as the nuclear lumen or chloroplasts in plant cells. Thus, presequences contain multifaceted information to endow mitochondrial precursor proteins with specific properties that are critical for the early steps of mitochondrial protein biogenesis.

Indexed as

MitochondriaMitochondrial ProteinsProtein PrecursorsAnimalsHumansMolecular ChaperonesProteasome Endopeptidase ComplexProtein TransportMitochondrial ProteinsMolecular ChaperonesProteasome Endopeptidase ComplexProtein PrecursorschaperonesmitochondriaPresequenceproteasomeprotein importubiquitin ligases

Identifiers

PMID41676891
PMCPMC12895284

What OpenQuestion holds

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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.