Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer proliferation and chemoresistance
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 analyse...
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| Vydané v: | Nature communications Ročník 7; číslo 1; s. 11030 - 13 |
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| Hlavní autori: | , , , , , , , , , , , , , , , , , , , , |
| Médium: | Journal Article |
| Jazyk: | English |
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London
Nature Publishing Group UK
18.03.2016
Nature Publishing Group Nature Portfolio |
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| ISSN: | 2041-1723, 2041-1723 |
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| 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.
PGRMC1 binds to EGFR and cytochromes P450, and is known to be involved in cancer proliferation and in drug resistance. Here, the authors determine the structure of the cytosolic domain of PGRMC1, which forms a dimer via haem–haem stacking, and propose how this interaction could be involved in its function. |
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| AbstractList | 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.
PGRMC1 binds to EGFR and cytochromes P450, and is known to be involved in cancer proliferation and in drug resistance. Here, the authors determine the structure of the cytosolic domain of PGRMC1, which forms a dimer via haem–haem stacking, and propose how this interaction could be involved in its function. 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. PGRMC1 binds to EGFR and cytochromes P450, and is known to be involved in cancer proliferation and in drug resistance. Here, the authors determine the structure of the cytosolic domain of PGRMC1, which forms a dimer via haem–haem stacking, and propose how this interaction could be involved in its function. 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.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. |
| ArticleNumber | 11030 |
| Author | Harada, Erisa Koike, Ikko Yamamoto, Tatsuya Shimamura, Tatsuro Uchida, Takeshi Sugase, Kenji Nakane, Takanori Handa, Hiroshi Yamaguchi, Yuki Yamamoto, Ayumi Ishimori, Koichiro Ohmura, Mitsuyo Sugiura, Yuki Krayukhina, Elena Kobayashi, Takuya Kabe, Yasuaki Noda, Masanori Iwata, So Muraoka, Kazumi Uchiyama, Susumu Suematsu, Makoto |
| Author_xml | – sequence: 1 givenname: Yasuaki surname: Kabe fullname: Kabe, Yasuaki email: ykabe@z3.keio.jp organization: Department of Biochemistry, Keio University School of Medicine, and Japan Science and Technology Agency (JST), Core Research for Evolutional Science and Technology (CREST) – sequence: 2 givenname: Takanori surname: Nakane fullname: Nakane, Takanori organization: Department of Medical Chemistry and Cell Biology, Graduate School of Medicine, Kyoto University, Department of Statistical Genetics, Graduate School of Medicine, Kyoto University – sequence: 3 givenname: Ikko surname: Koike fullname: Koike, Ikko organization: Department of Biochemistry, Keio University School of Medicine, and Japan Science and Technology Agency (JST), Core Research for Evolutional Science and Technology (CREST) – sequence: 4 givenname: Tatsuya surname: Yamamoto fullname: Yamamoto, Tatsuya organization: Bioorganic Research Institute, Suntory Foundation for Life Sciences – sequence: 5 givenname: Yuki surname: Sugiura fullname: Sugiura, Yuki organization: Department of Biochemistry, Keio University School of Medicine, and Japan Science and Technology Agency (JST), Core Research for Evolutional Science and Technology (CREST) – sequence: 6 givenname: Erisa surname: Harada fullname: Harada, Erisa organization: Bioorganic Research Institute, Suntory Foundation for Life Sciences – sequence: 7 givenname: Kenji surname: Sugase fullname: Sugase, Kenji organization: Bioorganic Research Institute, Suntory Foundation for Life Sciences – sequence: 8 givenname: Tatsuro surname: Shimamura fullname: Shimamura, Tatsuro organization: Department of Medical Chemistry and Cell Biology, Graduate School of Medicine, Kyoto University – sequence: 9 givenname: Mitsuyo surname: Ohmura fullname: Ohmura, Mitsuyo organization: Department of Biochemistry, Keio University School of Medicine, and Japan Science and Technology Agency (JST), Core Research for Evolutional Science and Technology (CREST) – sequence: 10 givenname: Kazumi surname: Muraoka fullname: Muraoka, Kazumi organization: Department of Biochemistry, Keio University School of Medicine, and Japan Science and Technology Agency (JST), Core Research for Evolutional Science and Technology (CREST) – sequence: 11 givenname: Ayumi surname: Yamamoto fullname: Yamamoto, Ayumi organization: Department of Chemistry, Faculty of Science, Hokkaido University – sequence: 12 givenname: Takeshi surname: Uchida fullname: Uchida, Takeshi organization: Department of Chemistry, Faculty of Science, Hokkaido University – sequence: 13 givenname: So surname: Iwata fullname: Iwata, So organization: Department of Medical Chemistry and Cell Biology, Graduate School of Medicine, Kyoto University, JST, Research Acceleration Program, Membrane Protein Crystallography Project – sequence: 14 givenname: Yuki surname: Yamaguchi fullname: Yamaguchi, Yuki organization: Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology – sequence: 15 givenname: Elena surname: Krayukhina fullname: Krayukhina, Elena organization: Department of Biotechnology, Graduate School of Engineering, Osaka University – sequence: 16 givenname: Masanori surname: Noda fullname: Noda, Masanori organization: Department of Biotechnology, Graduate School of Engineering, Osaka University – sequence: 17 givenname: Hiroshi surname: Handa fullname: Handa, Hiroshi organization: Department of Nanoparticle Translational Research, Tokyo Medical University – sequence: 18 givenname: Koichiro orcidid: 0000-0002-5868-0462 surname: Ishimori fullname: Ishimori, Koichiro organization: Department of Chemistry, Faculty of Science, Hokkaido University – sequence: 19 givenname: Susumu surname: Uchiyama fullname: Uchiyama, Susumu organization: Department of Biotechnology, Graduate School of Engineering, Osaka University, Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences – sequence: 20 givenname: Takuya surname: Kobayashi fullname: Kobayashi, Takuya email: t-coba@mfour.med.kyoto-u.ac.jp organization: Department of Medical Chemistry and Cell Biology, Graduate School of Medicine, Kyoto University, JST, CREST, Platform for Drug Discovery, Informatics, and Structural Life Science, JST – sequence: 21 givenname: Makoto orcidid: 0000-0002-7165-6336 surname: Suematsu fullname: Suematsu, Makoto email: gasbiology@z6.keio.jp organization: Department of Biochemistry, Keio University School of Medicine, JST, Exploratory Research for Advanced Technology (ERATO), Suematsu Gas Biology Project |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/26988023$$D View this record in MEDLINE/PubMed |
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| ContentType | Journal Article |
| Copyright | The Author(s) 2016 Copyright Nature Publishing Group Mar 2016 Copyright © 2016, Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. 2016 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. |
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| Snippet | Progesterone-receptor membrane component 1 (PGRMC1/Sigma-2 receptor) is a haem-containing protein that interacts with epidermal growth factor receptor (EGFR)... PGRMC1 binds to EGFR and cytochromes P450, and is known to be involved in cancer proliferation and in drug resistance. Here, the authors determine the... |
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| SubjectTerms | 631/45/612/1237 631/67/1059/2326 631/80/86 96/95 Carbon monoxide Carbon Monoxide - metabolism Cell Proliferation Crystallography, X-Ray Cytochrome P-450 Enzyme System - metabolism Drug Resistance, Neoplasm Heme - metabolism Humanities and Social Sciences Humans Membrane Proteins - metabolism Models, Biological multidisciplinary Neoplasms - metabolism Neoplasms - pathology Protein Binding Protein Multimerization Receptor, Epidermal Growth Factor - metabolism Receptors, Progesterone - metabolism Receptors, sigma - metabolism Science Science (multidisciplinary) Signal Transduction - drug effects Solutions |
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| Title | Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer proliferation and chemoresistance |
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