Evidence map›Paper›PMID 41504667›Full record

ArticleThe Journal of cell biology2026

Mitochondrial presequences harbor variable strengths to maintain organellar function.

Youmian Yan, Baigalmaa Erdenepurev, Thiago N Menezes, Ian Collinson, Natalie M Niemi

Abstract read
In one paragraph

Article in The Journal of cell biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Mitochondrial depolarization stabilizes the vitamin BProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Quality control of protein import into mammalian mitochondria.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
  5. Article
  6. Review
  7. Article
  8. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Youmian YanDepartment of Biochemistry & Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, USA.ORCID 0000-0001-8733-6989
Baigalmaa ErdenepurevDepartment of Biochemistry & Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, USA.ORCID 0009-0004-6732-6408
Thiago N MenezesDepartment of Biochemistry & Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, USA.ORCID 0000-0003-3856-3397
Ian CollinsonSchool of Biochemistry, University of Bristol , Bristol, UK.ORCID 0000-0002-3931-0503
Natalie M NiemiDepartment of Biochemistry & Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, USA.ORCID 0000-0002-5174-4005

Funding

Delineating phosphorylation-mediated regulation of mitochondrial functionR35GM151130 · NIGMS · WASHINGTON UNIVERSITY · PI Natalie Niemi · 2023 to 2026
$1.6M
NIGMS NIH HHS R35 GM151130NIH HHS R35GM151130Washington University School of MedicineWellcome TrustWellcome Trust 104632/Z/14/Z
6 · The paper itself

Abstract

Hundreds of mitochondrial proteins rely on N-terminal presequences for organellar targeting and import. While generally described as positively charged amphiphilic helices, presequences lack a consensus motif and thus likely promote protein import into mitochondria with variable efficiencies. Indeed, the concept of presequence strength underlies biological models such as stress sensing, yet a quantitative analysis of what dictates strong versus weak presequences is lacking. Furthermore, the extent to which presequence strength affects mitochondrial function and cellular fitness remains unclear. Here, we capitalize on the MitoLuc protein import assay to define multiple aspects of presequence strength. We find that select presequences, including those that regulate the mitochondrial unfolded protein response (UPRmt), impart differential import efficiencies during mitochondrial uncoupling. Surprisingly, we find that presequences beyond those associated with stress signaling promote highly variable import efficiency in vitro, suggesting presequence strength may influence a broader array of processes than currently appreciated. We exploit this variability to demonstrate that only presequences that promote robust in vitro import can fully rescue defects in respiratory growth in complex IV-deficient yeast, suggesting that presequence strength dictates metabolic potential. Collectively, our findings demonstrate that presequence strength can describe numerous metrics, such as total imported protein, maximal import velocity, or sensitivity to uncoupling, suggesting that the annotation of presequences as weak or strong requires more nuanced characterization than typically performed. Importantly, we find that such variability in presequence strength meaningfully affects cellular fitness beyond stress signaling, suggesting that organisms may broadly exploit presequence strength to fine-tune mitochondrial import and thus organellar homeostasis.

Indexed as

MitochondriaMitochondrial ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsProtein TransportUnfolded Protein ResponseMitochondrial ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID41504667
PMCPMC12817251

What Socratic holds

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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 Socratic graph.