Evidence map›Paper›PMID 31483742›Full record

ArticleMolecular biology of the cell2019

The mitochondrial intermembrane space-facing proteins Mcp2 and Tgl2 are involved in yeast lipid metabolism.

Fenja Odendall, Sandra Backes, Takashi Tatsuta, Uri Weill, Maya Schuldiner, Thomas Langer, Johannes M Herrmann, Doron Rapaport, Kai Stefan Dimmer

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. Coenzyme Q biochemistry and biosynthesis.Trends in biochemical sciences · 2023
    Review
  4. Article
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

9 authors at 4 institutions in 2 countries.

Fenja OdendallInterfaculty Institute of Biochemistry, University of Tübingen, 72076 Tübingen, Germany.
Sandra BackesCell Biology, University of Kaiserslautern, 67663 Kaiserslautern, Germany.
Takashi TatsutaMax Planck Institute for Biology of Ageing, 50931 Köln, Germany.
Uri WeillDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Maya SchuldinerDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Thomas LangerMax Planck Institute for Biology of Ageing, 50931 Köln, Germany.
Johannes M HerrmannCell Biology, University of Kaiserslautern, 67663 Kaiserslautern, Germany.
Doron RapaportInterfaculty Institute of Biochemistry, University of Tübingen, 72076 Tübingen, Germany.
Kai Stefan DimmerInterfaculty Institute of Biochemistry, University of Tübingen, 72076 Tübingen, Germany.
University of Tübingen · DEMax Planck Institute for Biology of Ageing · DEUniversity of Kaiserslautern · DEWeizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondria are unique organelles harboring two distinct membranes, the mitochondrial inner and outer membrane (MIM and MOM, respectively). Mitochondria comprise only a subset of metabolic pathways for the synthesis of membrane lipids; therefore most lipid species and their precursors have to be imported from other cellular compartments. One such import process is mediated by the ER mitochondria encounter structure (ERMES) complex. Both mitochondrial membranes surround the hydrophilic intermembrane space (IMS). Therefore, additional systems are required that shuttle lipids between the MIM and MOM. Recently, we identified the IMS protein Mcp2 as a high-copy suppressor for cells that lack a functional ERMES complex. To understand better how mitochondria facilitate transport and biogenesis of lipids, we searched for genetic interactions of this suppressor. We found that

Indexed as

Lipid MetabolismEndoplasmic ReticulumEpistasis, GeneticLipaseMitochondrial MembranesMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsPhosphatidylethanolaminesProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsLipaseMCP2 protein, S cerevisiaeMIA40 protein, S cerevisiaeMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsphosphatidylethanolaminePhosphatidylethanolaminesSaccharomyces cerevisiae ProteinsTGL3 protein, S cerevisiae

Identifiers

PMID31483742
PMCPMC6761770
OpenAlexW2971923455

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.