Evidence map›Paper›PMID 42839116›Full record

ArticleEMBO reports2026

The AMIGa complex is at the crossroads of cytochrome c oxidase and ATP synthase biogenesis.

Ulrik Pedroza-Dávila, Yolanda Camacho-Villasana, Miriam Vázquez-Acevedo, Madhurya Lutikurti, Diego González-Halphen, Alfredo Cabrera-Orefice, Xochitl Perez-Martinez

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

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0cells of the map it votes in
0citing papers in PubMed
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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

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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

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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.

Ulrik Pedroza-DávilaDepartamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, México City, México. upedroza@ifc.unam.mx.ORCID http://orcid.org/0009-0007-1667-6127
Yolanda Camacho-VillasanaDepartamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, México City, México.ORCID http://orcid.org/0000-0002-2652-537X
Miriam Vázquez-AcevedoDepartamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, México City, México.
Madhurya LutikurtiResearch Institute for Medical Innovation, Radboud University Medical Center, Nijmegen, the Netherlands.
Diego González-HalphenDepartamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, México City, México.ORCID http://orcid.org/0000-0003-0654-655X
Alfredo Cabrera-OreficeResearch Institute for Medical Innovation, Radboud University Medical Center, Nijmegen, the Netherlands.
Xochitl Perez-MartinezDepartamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, México City, México. xperez@ifc.unam.mx.ORCID http://orcid.org/0000-0002-3651-8413

Funding

Deutsche Forschungsgemeinschaft (DFG) Project S01#456687919Secretaría de Ciencia, Humanidades, Tecnología e Innovación (Conahcyt) CVU 883299UNAM | Dirección General de Asuntos del Personal Académico, Universidad Nacional Autónoma de México (DGAPA) IF262026UNAM | Dirección General de Asuntos del Personal Académico, Universidad Nacional Autónoma de México (DGAPA) IN207023UNAM | Dirección General de Asuntos del Personal Académico, Universidad Nacional Autónoma de México (DGAPA) IN220026UNAM | Dirección General de Asuntos del Personal Académico, Universidad Nacional Autónoma de México (DGAPA) IN223623ZonMw (Netherlands Organisation for Health Research and Development) ZonMW TOP-Grant 91217009
6 · The paper itself

Abstract

Cytochrome c oxidase (CIV) and ATP synthase are part of the oxidative phosphorylation machinery. Their modular, highly regulated assembly requires specific factors and is coordinated through a common intermediate, the Atco complex, composed of the Atp9 ring and Cox6. By high-throughput analysis, it was previously detected that Aim11 interacts with some CIV and ATP synthase subunits, but its relevance was unknown. In this work, we characterize the role of Aim11 in CIV and ATP synthase biogenesis. We find that the null mutant exhibits reduced respiratory growth and diminished CIV activity. Mitochondrial complexome profiling of the Δaim11 mutant shows an accumulation of intermediates of the CIV and ATP synthase assembly modules. Aim11 forms a complex with three other proteins: Mtc3, Gep7, and Iai11, which we coin as AMIGa (Aim11-Mtc3-Iai11-Gep7 assembly complex). Aim11 interacts with the newly synthesized Atp9 ring, possibly mediated by the Atco complex. In addition, we identify the human protein TMEM242 as an Aim11 orthologue.

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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 Socratic graph.