Evidence map›Paper›PMID 32403431›Full record

ArticleInternational journal of molecular sciences2020

Characteristic Analysis of Homo- and Heterodimeric Complexes of Human Mitochondrial Pyruvate Carrier Related to Metabolic Diseases.

Jinyi Lee, Zeyu Jin, Donghan Lee, Ji-Hye Yun, Weontae Lee

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

12 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
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  3. Article
  4. Article
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  6. Article
  7. Review
  8. The mitochondrial pyruvate carrier at the crossroads of intermediary metabolism.American journal of physiology. Endocrinology and metabolism · 2022
    Review
  9. Structural Insights into the Human Mitochondrial Pyruvate Carrier Complexes.Journal of chemical information and modeling · 2021
    Article
  10. Review
  11. Review
  12. 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

5 authors at 2 institutions in 2 countries.

Jinyi LeeDepartment of Biochemistry, College of Life Science & Biotechnology, Yonsei University, Seoul 03722, Korea.ORCID 0000-0002-8070-1784
Zeyu JinDepartment of Biochemistry, College of Life Science & Biotechnology, Yonsei University, Seoul 03722, Korea.ORCID 0000-0002-6478-2967
Donghan LeeDepartment of Medicine, James Graham Brown Cancer Center, University of Louisville, Louisville, KY 40292, USA.
Ji-Hye YunDepartment of Biochemistry, College of Life Science & Biotechnology, Yonsei University, Seoul 03722, Korea.ORCID 0000-0001-7570-369X
Weontae LeeDepartment of Biochemistry, College of Life Science & Biotechnology, Yonsei University, Seoul 03722, Korea.
Yonsei University · KRUniversity of Louisville · US

Funding

National Research Foundation of Korea 2016R1A6A3A04010213National Research Foundation of Korea 2017M3A9F6029753National Research Foundation of Korea 2018K2A9A2A06024227National Research Foundation of Korea 2019M3E5D6063903
6 · The paper itself

Abstract

Human mitochondrial pyruvate carriers (hMPCs), which are required for the uptake of pyruvate into mitochondria, are associated with several metabolic diseases, including type 2 diabetes and various cancers. Yeast MPC was recently demonstrated to form a functional unit of heterodimers. However, human MPC-1 (hMPC-1) and MPC-2 (hMPC-2) have not yet been individually isolated for their detailed characterization, in particular in terms of their structural and functional properties, namely, whether they exist as homo- or heterodimers. In this study, hMPC-1 and hMPC-2 were successfully isolated in micelles and they formed stable homodimers. However, the heterodimer state was found to be dominant when both hMPC-1 and hMPC-2 were present. In addition, as heterodimers, the molecules exhibited a higher binding capacity to both substrates and inhibitors, together with a larger structural stability than when they existed as homodimers. Taken together, our results demonstrated that the hetero-dimerization of hMPCs is the main functional unit of the pyruvate metabolism, providing a structural insight into the transport mechanisms of hMPCs.

Indexed as

Protein MultimerizationAmino Acid SequenceAnimalsCircular DichroismHumansMetabolic DiseasesMitochondrial Membrane Transport ProteinsModels, MolecularMonocarboxylic Acid TransportersProtein BindingProtein ConformationProtein StabilityPyruvic AcidSequence Homology, Amino AcidSf9 CellsSpodopteraMitochondrial Membrane Transport ProteinsMonocarboxylic Acid TransportersMPC1 protein, humanMPC2 protein, humanPyruvic Acidcellular homeostasishetero-complexhuman mitochondrial pyruvate carrieroligomerization

Identifiers

PMID32403431
PMCPMC7246999
OpenAlexW3023012694

What OpenQuestion holds

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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.