Evidence map›Paper›PMID 42066079›Full record

ArticleScience advances2026

A dynamic gateway: Uncovering the expanded human TOM complex interactome and its regulatory complexity.

Mayra A Borrero-Landazabal, Vanessa Linke, Tereza Kadavá, Zeshi Li, Piotr Draczkowski, Kacper Kaszuba, Lea Bertgen, Remigiusz A Serwa, Albert J R Heck, Agnieszka Chacinska

Abstract read
In one paragraph

Article in Science advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

10 authors.

Mayra A Borrero-LandazabalIMol Polish Academy of Sciences, Warsaw, Poland.ORCID 0000-0003-3464-4042
Vanessa LinkeIMol Polish Academy of Sciences, Warsaw, Poland.ORCID 0000-0002-1827-577X
Tereza KadaváBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Padualaan 8, Utrecht, 3584 CH, Netherlands.ORCID 0000-0003-3551-7563
Zeshi LiChemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Universiteitsweg 99, Utrecht, 3584 CG, Netherlands.ORCID 0000-0002-8358-3162
Piotr DraczkowskiDepartment of Biochemistry and Biophysics, National Bioinformatics Infrastructure Sweden, Science for Life Laboratory, Stockholm University, Solna, Sweden.ORCID 0000-0002-9408-2670
Kacper KaszubaIMol Polish Academy of Sciences, Warsaw, Poland.ORCID 0009-0009-5152-4481
Lea BertgenIMol Polish Academy of Sciences, Warsaw, Poland.ORCID 0000-0003-1278-3279
Remigiusz A SerwaIMol Polish Academy of Sciences, Warsaw, Poland.ORCID 0000-0002-4684-3754
Albert J R HeckBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Padualaan 8, Utrecht, 3584 CH, Netherlands.ORCID 0000-0002-2405-4404
Agnieszka ChacinskaIMol Polish Academy of Sciences, Warsaw, Poland.ORCID 0000-0002-2832-2568

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The translocase of the outer mitochondrial membrane (TOM) is the conserved entry gate for nuclear-encoded proteins. While structurally similar from yeast to humans, the human TOM complex operates in a cellular environment of vastly greater complexity. Here, we present a high-confidence map of the human TOM interactome using a membrane-permeable cross-linker to capture both stable and transient interactors. Alongside extensive overlap with known yeast partners, we uncover a set of human-specific interactors including regulatory factors and TOM-associated proteins. Mapping unique interprotein cross-links reveals conformational flexibility of the receptor TOM20 and enhanced recovery of peripheral components such as TOM70 and several associated quality control factors. Notably, we identify FKBP8 (FK506 binding protein 8) as a human-specific interactor that binds multiple TOM subunits and promotes organization of the complex. Our work redefines the human TOM complex as a dynamic, multifaceted hub coordinating biogenesis, quality control, and signaling. This expanded TOM landscape offers a rich resource for exploring mitochondrial regulation in health and disease.

Indexed as

Mitochondrial Membrane Transport ProteinsProtein Interaction MapsHumansMitochondriaMitochondrial MembranesMitochondrial Precursor Protein Import Complex ProteinsProtein BindingProtein Interaction MappingTacrolimus Binding ProteinsFKBP8 protein, humanMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsTacrolimus Binding ProteinsTOMM20 protein, human

Identifiers

PMID42066079
PMCPMC13134618

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Registered trials

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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.