Evidence map›Paper›PMID 25165143›Full record

ArticleMolecular biology of the cell2014

The novel component Kgd4 recruits the E3 subunit to the mitochondrial α-ketoglutarate dehydrogenase.

Manfred Heublein, Miguel A Burguillos, F Nora Vögtle, Pedro F Teixeira, Axel Imhof, Chris Meisinger, Martin Ott

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

29 citing papers in PubMed, 57 citations in OpenAlex.

  1. A Micropeptide Component of the OGDH Complex Modulates ATP Production in the TCA Cycle.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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  5. Case Report: Biallelic variants inFrontiers in pediatrics · 2025
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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 4 institutions in 2 countries.

Manfred HeubleinCenter for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.
Miguel A BurguillosCancer Centrum Karolinska, Karolinska Institutet, SE-171 76 Stockholm, Sweden.
F Nora VögtleInstitute for Biochemistry and Molecular Biology and BIOSS (Centre for Biological Signaling Studies), University of Freiburg, D-79104 Freiburg, Germany.
Pedro F TeixeiraCenter for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.
Axel ImhofZentrallabor für Proteinanalytik, Adolf-Butenandt Institut, LMU München, D-80336 München, Germany.
Chris MeisingerInstitute for Biochemistry and Molecular Biology and BIOSS (Centre for Biological Signaling Studies), University of Freiburg, D-79104 Freiburg, Germany.
Martin OttCenter for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden martin.ott@dbb.su.se.
Stockholm University · SEUniversity of Freiburg · DEKarolinska Institutet · SELudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mitochondrial citric acid cycle is a central hub of cellular metabolism, providing intermediates for biosynthetic pathways and channeling electrons to the respiratory chain complexes. In this study, we elucidated the composition and organization of the multienzyme complex α-ketoglutarate dehydrogenase (α-KGDH). In addition to the three classical E1-E3 subunits, we identified a novel component, Kgd4 (Ymr31/MRPS36), which was previously assigned to be a subunit of the mitochondrial ribosome. Biochemical analyses demonstrate that this protein plays an evolutionarily conserved role in the organization of mitochondrial α-KGDH complexes of fungi and animals. By binding to both the E1-E2 core and the E3 subunit, Kgd4 acts as a molecular adaptor that is necessary to a form a stable α-KGDH enzyme complex. Our work thus reveals a novel subunit of a key citric acid-cycle enzyme and shows how this large complex is organized.

Indexed as

Amino Acid SequenceAnimalsCell LineConserved SequenceEvolution, MolecularGene Knockdown TechniquesKetoglutarate Dehydrogenase ComplexMiceMicrogliaMitochondriaMitochondrial ProteinsMolecular Sequence DataProtein Structure, TertiaryProtein SubunitsRibosomal ProteinsSaccharomyces cerevisiaeKetoglutarate Dehydrogenase ComplexMitochondrial ProteinsProtein SubunitsRibosomal ProteinsSaccharomyces cerevisiae ProteinsYMR31 protein, S cerevisiae

Identifiers

PMID25165143
PMCPMC4214781
OpenAlexW1975919114

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.