Evidence map›Paper›PMID 32142709›Full record

ArticleCurrent biology : CB2020

Defining the Substrate Spectrum of the TIM22 Complex Identifies Pyruvate Carrier Subunits as Unconventional Cargos.

Ridhima Gomkale, Luis Daniel Cruz-Zaragoza, Ida Suppanz, Bernard Guiard, Julio Montoya, Sylvie Callegari, David Pacheu-Grau, Bettina Warscheid, Peter Rehling

Open access · hybridAbstract read
In one paragraph

Article in Current biology : CB, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

22 citing papers in PubMed, 45 citations in OpenAlex.

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  17. Targeting and Insertion of Membrane Proteins in Mitochondria.Frontiers in cell and developmental biology · 2021
    Review
  18. Subcellular proteomics.Nature reviews. Methods primers · 2021
    Article
  19. Article
  20. 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

9 authors at 5 institutions in 3 countries.

Ridhima GomkaleDepartment of Cellular Biochemistry, University Medical Center Göttingen, 37073 Göttingen, Germany.
Luis Daniel Cruz-ZaragozaDepartment of Cellular Biochemistry, University Medical Center Göttingen, 37073 Göttingen, Germany.
Ida SuppanzBiochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology, University of Freiburg, 79104 Freiburg, Germany; Signalling Research Centres BIOSS and CIBSS, University of Freiburg, 79104 Freiburg, Germany.
Bernard GuiardCentre de Génétique Moléculaire, CNRS, 91190 Gif-sur-Yvette, France.
Julio MontoyaDepartamento de Bioquímica y Biología Molecular y Celular, Universidad de Zaragoza-CIBER de Enfermedades Raras (CIBERER)-Instituto de investigación Sanitaria de Aragón (IIS Aragón), 50013 Zaragoza, Spain.
Sylvie CallegariDepartment of Cellular Biochemistry, University Medical Center Göttingen, 37073 Göttingen, Germany.
David Pacheu-GrauDepartment of Cellular Biochemistry, University Medical Center Göttingen, 37073 Göttingen, Germany.
Bettina WarscheidBiochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology, University of Freiburg, 79104 Freiburg, Germany; Signalling Research Centres BIOSS and CIBSS, University of Freiburg, 79104 Freiburg, Germany.
Peter RehlingDepartment of Cellular Biochemistry, University Medical Center Göttingen, 37073 Göttingen, Germany. Electronic address: peter.rehling@medizin.uni-goettingen.de.
University of Göttingen · DEUniversitätsmedizin Göttingen · DEUniversity of Freiburg · DECentre de Génétique Moléculaire · FRCentre for Biomedical Network Research on Rare Diseases · ES

Funding

European Research Council 648235
6 · The paper itself

Abstract

In mitochondria, the carrier translocase (TIM22 complex) facilitates membrane insertion of multi-spanning proteins with internal targeting signals into the inner membrane [1-3]. Tom70, a subunit of TOM complex, represents the major receptor for these precursors [2, 4-6]. After transport across the outer membrane, the hydrophobic carriers engage with the small TIM protein complex composed of Tim9 and Tim10 for transport across the intermembrane space (IMS) toward the TIM22 complex [7-12]. Tim22 represents the pore-forming core unit of the complex [13, 14]. Only a small subset of TIM22 cargo molecules, containing four or six transmembrane spans, have been experimentally defined. Here, we used a tim22 temperature-conditional mutant to define the TIM22 substrate spectrum. Along with carrier-like cargo proteins, we identified subunits of the mitochondrial pyruvate carrier (MPC) as unconventional TIM22 cargos. MPC proteins represent substrates with atypical topology for this transport pathway. In agreement with this, a patient affected in TIM22 function displays reduced MPC levels. Our findings broaden the repertoire of carrier pathway substrates and challenge current concepts of TIM22-mediated transport processes.

Indexed as

Biological TransportHEK293 CellsHumansMembrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsMonocarboxylic Acid TransportersPyruvic AcidSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMembrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsMonocarboxylic Acid TransportersPyruvic AcidSaccharomyces cerevisiae ProteinsTIM22 protein, humanmetabolite carriermitochondriaprotein importpyruvate carrierTIM22

Identifiers

PMID32142709
PMCPMC7090383
OpenAlexW3009827201

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.