Evidence map›Paper›PMID 29464284›Full record

ArticleCellular and molecular life sciences : CMLS2018

Degradation of the mitochondrial complex I assembly factor TMEM126B under chronic hypoxia.

Dominik C Fuhrmann, Ilka Wittig, Stefan Dröse, Tobias Schmid, Nathalie Dehne, Bernhard Brüne

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

28 citing papers in PubMed, 45 citations in OpenAlex.

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  10. Using cryo-EM to understand the assembly pathway of respiratory complex I.Acta crystallographica. Section D, Structural biology · 2024
    Article
  11. Article
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  13. Review
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  15. Complexome Profiling: Assembly and Remodeling of Protein Complexes.International journal of molecular sciences · 2021
    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

6 authors at 1 institution in 1 country.

Dominik C FuhrmannFaculty of Medicine, Institute of Biochemistry I, Goethe-University Frankfurt, Theodor-Stern-Kai 7, 60590, Frankfurt, Germany.
Ilka WittigFunctional Proteomics, SFB 815 Core Unit, Goethe-University Frankfurt, Frankfurt, Germany.
Stefan DröseDepartment of Anesthesiology, Intensive-Care Medicine and Pain Therapy, Faculty of Medicine, Goethe-University Frankfurt, Frankfurt, Germany.
Tobias SchmidFaculty of Medicine, Institute of Biochemistry I, Goethe-University Frankfurt, Theodor-Stern-Kai 7, 60590, Frankfurt, Germany.
Nathalie DehneFaculty of Medicine, Institute of Biochemistry I, Goethe-University Frankfurt, Theodor-Stern-Kai 7, 60590, Frankfurt, Germany.
Bernhard BrüneFaculty of Medicine, Institute of Biochemistry I, Goethe-University Frankfurt, Theodor-Stern-Kai 7, 60590, Frankfurt, Germany. b.bruene@biochem.uni-frankfurt.de.ORCID http://orcid.org/0000-0001-8237-2841
Goethe University Frankfurt · DE

Funding

Deutsche Forschungsgemeinschaft SFB 815 (TPA08Deutsche Forschungsgemeinschaft Z01)
6 · The paper itself

Abstract

Cell stress such as hypoxia elicits adaptive responses, also on the level of mitochondria, and in part is mediated by the hypoxia-inducible factor (HIF) 1α. Adaptation of mitochondria towards acute hypoxic conditions is reasonably well understood, while regulatory mechanisms, especially of respiratory chain assembly factors, under chronic hypoxia remains elusive. One of these assembly factors is transmembrane protein 126B (TMEM126B). This protein is part of the mitochondrial complex I assembly machinery. We identified changes in complex I abundance under chronic hypoxia, in association with impaired substrate-specific mitochondrial respiration. Complexome profiling of isolated mitochondria of the human leukemia monocytic cell line THP-1 revealed HIF-1α-dependent deficits in complex I assembly and mitochondrial complex I assembly complex (MCIA) abundance. Of all mitochondrial MCIA members, we proved a selective HIF-1-dependent decrease of TMEM126B under chronic hypoxia. Mechanistically, HIF-1α induces the E3-ubiquitin ligase F-box/WD repeat-containing protein 1A (β-TrCP1), which in turn facilitates the proteolytic degradation of TMEM126B. Attenuating a functional complex I assembly appears critical for cellular adaptation towards chronic hypoxia and is linked to destruction of the mitochondrial assembly factor TMEM126B.

Indexed as

Oxygen ConsumptionAmino Acid SequenceCell HypoxiaCell Line, TumorElectron Transport Complex IHumansHypoxia-Inducible Factor 1, alpha SubunitMembrane ProteinsMitochondriaProteolysisRNA InterferenceTHP-1 CellsElectron Transport Complex IHypoxia-Inducible Factor 1, alpha SubunitMembrane ProteinsTMEM126B protein, humanAKTComplexome profilingHypoxia-inducible factor (HIF)MCIAMitochondrial respirationβ-TrCP

Identifiers

PMID29464284
PMCPMC11105659
OpenAlexW2792931785

What OpenQuestion holds

Textmetadata
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.