Evidence map›Paper›PMID 25605331›Full record

ArticleMolecular and cellular biology2015

C11orf83, a mitochondrial cardiolipin-binding protein involved in bc1 complex assembly and supercomplex stabilization.

Marjorie Desmurs, Michelangelo Foti, Etienne Raemy, Frédéric Maxime Vaz, Jean-Claude Martinou, Amos Bairoch, Lydie Lane

Open access · bronzeAbstract read
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Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed, 66 citations in OpenAlex.

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  14. The cardiac-enriched microprotein mitolamban regulates mitochondrial respiratory complex assembly and function in mice.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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 2 countries.

Marjorie DesmursDepartment of Human Protein Sciences, University of Geneva, Geneva, Switzerland marjorie.desmurs@unige.ch lydie.lane@isb-sib.ch.
Michelangelo FotiDepartment of Cell Physiology and Metabolism, University of Geneva, Geneva, Switzerland.
Etienne RaemyDepartment of Cell Biology, University of Geneva, Geneva, Switzerland.
Frédéric Maxime VazLaboratory Genetic Metabolic Diseases, Department of Clinical Chemistry and Pediatrics, University of Amsterdam, Academic Medical Center, Amsterdam, The Netherlands.
Jean-Claude MartinouDepartment of Cell Biology, University of Geneva, Geneva, Switzerland.
Amos BairochDepartment of Human Protein Sciences, University of Geneva, Geneva, Switzerland CALIPHO Group, SIB Swiss Institute of Bioinformatics, Geneva, Switzerland.
Lydie LaneDepartment of Human Protein Sciences, University of Geneva, Geneva, Switzerland CALIPHO Group, SIB Swiss Institute of Bioinformatics, Geneva, Switzerland marjorie.desmurs@unige.ch lydie.lane@isb-sib.ch.
University of Geneva · CHAcademic Medical Center · NLSIB Swiss Institute of Bioinformatics · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mammalian mitochondria may contain up to 1,500 different proteins, and many of them have neither been confidently identified nor characterized. In this study, we demonstrated that C11orf83, which was lacking experimental characterization, is a mitochondrial inner membrane protein facing the intermembrane space. This protein is specifically associated with the bc1 complex of the electron transport chain and involved in the early stages of its assembly by stabilizing the bc1 core complex. C11orf83 displays some overlapping functions with Cbp4p, a yeast bc1 complex assembly factor. Therefore, we suggest that C11orf83, now called UQCC3, is the functional human equivalent of Cbp4p. In addition, C11orf83 depletion in HeLa cells caused abnormal crista morphology, higher sensitivity to apoptosis, a decreased ATP level due to impaired respiration and subtle, but significant, changes in cardiolipin composition. We showed that C11orf83 binds to cardiolipin by its α-helices 2 and 3 and is involved in the stabilization of bc1 complex-containing supercomplexes, especially the III2/IV supercomplex. We also demonstrated that the OMA1 metalloprotease cleaves C11orf83 in response to mitochondrial depolarization, suggesting a role in the selection of cells with damaged mitochondria for their subsequent elimination by apoptosis, as previously described for OPA1.

Indexed as

Amino Acid SequenceAnimalsApoptosisCardiolipinsCarrier ProteinsDown-RegulationElectron Transport Complex IIIGene DeletionHeLa CellsHumansMetalloendopeptidasesMitochondriaMitochondrial ProteinsMolecular Sequence DataXenopusCardiolipinsCarrier ProteinsElectron Transport Complex IIIMetalloendopeptidasesMitochondrial Proteinsmolecule metalloprotease-related protein-1, humanUQCC3 protein, human

Identifiers

PMID25605331
PMCPMC4355537
OpenAlexW1999407072

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.