Evidence map›Paper›PMID 37984987›Full record

ArticleLife science alliance2024

Mitochondrial phosphoproteomes are functionally specialized across tissues.

Fynn M Hansen, Laura S Kremer, Ozge Karayel, Isabell Bludau, Nils-Göran Larsson, Inge Kühl, Matthias Mann

Open access · goldAbstract read
In one paragraph

Article in Life science alliance, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

  1. Mass spectrometry proteomics for studying mitostasis.Protein science : a publication of the Protein Society · 2026
    Review
  2. Proteoforms as the true units of physiological function.European journal of applied physiology · 2026
    Review
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  14. Mitochondrial proteome research: the road ahead.Nature reviews. Molecular cell biology · 2024
    Review
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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

7 authors at 3 institutions in 3 countries.

Fynn M HansenDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.
Laura S KremerDepartment of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Ozge KarayelDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.
Isabell BludauDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.
Nils-Göran LarssonDepartment of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.ORCID https://orcid.org/0000-0001-5100-996X
Inge KühlDepartment of Cell Biology, Institute of Integrative Biology of the Cell, UMR9198, CEA, CNRS, Université Paris-Saclay, Gif-sur-Yvette, France.ORCID https://orcid.org/0000-0003-4797-0859
Matthias MannDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany mmann@biochem.mpg.de.ORCID https://orcid.org/0000-0003-1292-4799
Max Planck Institute of Biochemistry · DEKarolinska Institutet · SECentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondria are essential organelles whose dysfunction causes human pathologies that often manifest in a tissue-specific manner. Accordingly, mitochondrial fitness depends on versatile proteomes specialized to meet diverse tissue-specific requirements. Increasing evidence suggests that phosphorylation may play an important role in regulating tissue-specific mitochondrial functions and pathophysiology. Building on recent advances in mass spectrometry (MS)-based proteomics, we here quantitatively profile mitochondrial tissue proteomes along with their matching phosphoproteomes. We isolated mitochondria from mouse heart, skeletal muscle, brown adipose tissue, kidney, liver, brain, and spleen by differential centrifugation followed by separation on Percoll gradients and performed high-resolution MS analysis of the proteomes and phosphoproteomes. This in-depth map substantially quantifies known and predicted mitochondrial proteins and provides a resource of core and tissue-specific mitochondrial proteins (mitophos.de). Predicting kinase substrate associations for different mitochondrial compartments indicates tissue-specific regulation at the phosphoproteome level. Illustrating the functional value of our resource, we reproduce mitochondrial phosphorylation events on dynamin-related protein 1 responsible for its mitochondrial recruitment and fission initiation and describe phosphorylation clusters on MIGA2 linked to mitochondrial fusion.

Indexed as

MitochondriaProteomeAnimalsHumansMass SpectrometryMiceMitochondrial ProteinsPhosphorylationMitochondrial ProteinsProteome

Identifiers

PMID37984987
PMCPMC10662294
OpenAlexW4388832985

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.