Evidence map›Paper›PMID 26988023›Full record

ArticleNature communications2016

Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer proliferation and chemoresistance.

Yasuaki Kabe, Takanori Nakane, Ikko Koike, Tatsuya Yamamoto, Yuki Sugiura, Erisa Harada, Kenji Sugase, Tatsuro Shimamura, Mitsuyo Ohmura, Kazumi Muraoka and 11 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
12.2field-weighted citation impact, top 1% 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

101 citing papers in PubMed, 194 citations in OpenAlex.

  1. Article
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  6. Mechanisms of heme transport in the mitochondria.Biochemical Society transactions · 2025
    Review
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  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Sigma Receptors: Novel Regulators of Iron/Heme Homeostasis and Ferroptosis.International journal of molecular sciences · 2023
    Review
  20. Article

41 more citing papers are in PubMed but not listed here.

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

21 authors at 8 institutions in 4 countries.

Yasuaki KabeDepartment of Biochemistry, Keio University School of Medicine, and Japan Science and Technology Agency (JST), Core Research for Evolutional Science and Technology (CREST), Tokyo 160-8582, Japan.
Takanori NakaneDepartment of Medical Chemistry and Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto 606-8501, Japan.
Ikko KoikeDepartment of Biochemistry, Keio University School of Medicine, and Japan Science and Technology Agency (JST), Core Research for Evolutional Science and Technology (CREST), Tokyo 160-8582, Japan.
Tatsuya YamamotoBioorganic Research Institute, Suntory Foundation for Life Sciences, Kyoto 619-0284, Japan.
Yuki SugiuraDepartment of Biochemistry, Keio University School of Medicine, and Japan Science and Technology Agency (JST), Core Research for Evolutional Science and Technology (CREST), Tokyo 160-8582, Japan.
Erisa HaradaBioorganic Research Institute, Suntory Foundation for Life Sciences, Kyoto 619-0284, Japan.
Kenji SugaseBioorganic Research Institute, Suntory Foundation for Life Sciences, Kyoto 619-0284, Japan.
Tatsuro ShimamuraDepartment of Medical Chemistry and Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto 606-8501, Japan.
Mitsuyo OhmuraDepartment of Biochemistry, Keio University School of Medicine, and Japan Science and Technology Agency (JST), Core Research for Evolutional Science and Technology (CREST), Tokyo 160-8582, Japan.
Kazumi MuraokaDepartment of Biochemistry, Keio University School of Medicine, and Japan Science and Technology Agency (JST), Core Research for Evolutional Science and Technology (CREST), Tokyo 160-8582, Japan.
Ayumi YamamotoDepartment of Chemistry, Faculty of Science, Hokkaido University, Sapporo 060-0810, Japan.
Takeshi UchidaDepartment of Chemistry, Faculty of Science, Hokkaido University, Sapporo 060-0810, Japan.
So IwataDepartment of Medical Chemistry and Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto 606-8501, Japan.
Yuki YamaguchiDepartment of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
Elena KrayukhinaDepartment of Biotechnology, Graduate School of Engineering, Osaka University, Osaka 565-0871, Japan.
Masanori NodaDepartment of Biotechnology, Graduate School of Engineering, Osaka University, Osaka 565-0871, Japan.
Hiroshi HandaDepartment of Nanoparticle Translational Research, Tokyo Medical University, Tokyo 160-8402, Japan.
Koichiro IshimoriDepartment of Chemistry, Faculty of Science, Hokkaido University, Sapporo 060-0810, Japan.ORCID http://orcid.org/0000-0002-5868-0462
Susumu UchiyamaDepartment of Biotechnology, Graduate School of Engineering, Osaka University, Osaka 565-0871, Japan.
Takuya KobayashiDepartment of Medical Chemistry and Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto 606-8501, Japan.
Makoto SuematsuDepartment of Biochemistry, Keio University School of Medicine, JST, Exploratory Research for Advanced Technology (ERATO), Suematsu Gas Biology Project, Tokyo 160-8582, Japan.ORCID http://orcid.org/0000-0002-7165-6336
Keio University · JPKyoto University · JPHokkaido University · JPSuntory Foundation for Life Sciences · JPThe University of Osaka · JPNational Institutes of Natural Sciences · JPTokyo Institute of Technology · JPTokyo Medical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Progesterone-receptor membrane component 1 (PGRMC1/Sigma-2 receptor) is a haem-containing protein that interacts with epidermal growth factor receptor (EGFR) and cytochromes P450 to regulate cancer proliferation and chemoresistance; its structural basis remains unknown. Here crystallographic analyses of the PGRMC1 cytosolic domain at 1.95 Å resolution reveal that it forms a stable dimer through stacking interactions of two protruding haem molecules. The haem iron is five-coordinated by Tyr113, and the open surface of the haem mediates dimerization. Carbon monoxide (CO) interferes with PGRMC1 dimerization by binding to the sixth coordination site of the haem. Haem-mediated PGRMC1 dimerization is required for interactions with EGFR and cytochromes P450, cancer proliferation and chemoresistance against anti-cancer drugs; these events are attenuated by either CO or haem deprivation in cancer cells. This study demonstrates protein dimerization via haem-haem stacking, which has not been seen in eukaryotes, and provides insights into its functional significance in cancer.

Indexed as

Drug Resistance, NeoplasmProtein MultimerizationCarbon MonoxideCell ProliferationCrystallography, X-RayCytochrome P-450 Enzyme SystemErbB ReceptorsHemeHumansMembrane ProteinsModels, BiologicalNeoplasmsProtein BindingReceptors, ProgesteroneReceptors, sigmaSignal TransductionCarbon MonoxideCytochrome P-450 Enzyme SystemErbB ReceptorsHemeMembrane ProteinsPGRMC1 protein, humanReceptors, ProgesteroneReceptors, sigmasigma-2 receptorSolutions

Identifiers

PMID26988023
PMCPMC4802085
OpenAlexW2296998275

What OpenQuestion holds

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LicenceCC BY
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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.