Evidence map›Paper›PMID 37073556›Full record

ArticleJournal of cell science2023

The UbiB family member Cqd1 forms a novel membrane contact site in mitochondria.

Siavash Khosravi, Xenia Chelius, Ann-Katrin Unger, Daniela Rieger, Johanna Frickel, Timo Sachsenheimer, Christian Lüchtenborg, Rico Schieweck, Britta Brügger, Benedikt Westermann and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

1 citing paper in PubMed, 5 citations in OpenAlex.

  1. New Insights on the Uptake and Trafficking of Coenzyme Q.Antioxidants (Basel, Switzerland) · 2023
    Review
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

13 authors at 3 institutions in 1 country.

Siavash KhosraviDepartment of Cell Biology, Biomedical Center, Medical Faculty, Ludwig-Maximilians University Munich, 82152 Planegg/Martinsried, Germany.ORCID 0000-0001-9658-8248
Xenia CheliusInstitute of Cell Biology, University of Bayreuth, 95440 Bayreuth, Germany.
Ann-Katrin UngerInstitute of Cell Biology, University of Bayreuth, 95440 Bayreuth, Germany.
Daniela RiegerDepartment of Cell Biology, Biomedical Center, Medical Faculty, Ludwig-Maximilians University Munich, 82152 Planegg/Martinsried, Germany.
Johanna FrickelDepartment of Cell Biology, Biomedical Center, Medical Faculty, Ludwig-Maximilians University Munich, 82152 Planegg/Martinsried, Germany.
Timo SachsenheimerHeidelberg University Biochemistry Center (BZH), 69120 Heidelberg, Germany.
Christian LüchtenborgHeidelberg University Biochemistry Center (BZH), 69120 Heidelberg, Germany.
Rico SchieweckDepartment of Cell Biology, Biomedical Center, Medical Faculty, Ludwig-Maximilians University Munich, 82152 Planegg/Martinsried, Germany.ORCID 0000-0002-0251-0288
Britta BrüggerHeidelberg University Biochemistry Center (BZH), 69120 Heidelberg, Germany.ORCID 0000-0002-3477-8270
Benedikt WestermannInstitute of Cell Biology, University of Bayreuth, 95440 Bayreuth, Germany.ORCID 0000-0002-2991-1604
Till KleckerInstitute of Cell Biology, University of Bayreuth, 95440 Bayreuth, Germany.ORCID 0000-0003-0149-042X
Walter NeupertDepartment of Cell Biology, Biomedical Center, Medical Faculty, Ludwig-Maximilians University Munich, 82152 Planegg/Martinsried, Germany.
Max E HarnerDepartment of Cell Biology, Biomedical Center, Medical Faculty, Ludwig-Maximilians University Munich, 82152 Planegg/Martinsried, Germany.ORCID 0000-0002-5513-1046
Ludwig-Maximilians-Universität München · DEUniversity of Bayreuth · DEHeidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondria are essential organelles of eukaryotic cells and are characterized by their unique and complex membrane system. They are confined from the cytosol by an envelope consisting of two membranes. Signals, metabolites, proteins and lipids have to be transferred across these membranes via proteinaceous contact sites to keep mitochondria functional. In the present study, we identified a novel mitochondrial contact site in Saccharomyces cerevisiae that is formed by the inner membrane protein Cqd1 and the outer membrane proteins Por1 and Om14. Similar to what is found for the mitochondrial porin Por1, Cqd1 is highly conserved, suggesting that this complex is conserved in form and function from yeast to human. Cqd1 is a member of the UbiB protein kinase-like family (also called aarF domain-containing kinases). It was recently shown that Cqd1, in cooperation with Cqd2, controls the cellular distribution of coenzyme Q by a yet unknown mechanism. Our data suggest that Cqd1 is additionally involved in phospholipid homeostasis. Moreover, overexpression of CQD1 and CQD2 causes tethering of mitochondria to the endoplasmic reticulum, which might explain the ability of Cqd2 to rescue ERMES deletion phenotypes.

Indexed as

MitochondriaSaccharomyces cerevisiae ProteinsEndoplasmic ReticulumHumansMembrane ProteinsMitochondrial MembranesSaccharomyces cerevisiaeMembrane ProteinsSaccharomyces cerevisiae ProteinsContact sitesMitochondriaMitochondrial biogenesisMitochondrial morphologyPhospholipidsUbiB protein family

Identifiers

PMID37073556
PMCPMC10214851
OpenAlexW4366352949

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.