Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer proliferation and chemoresistance
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 fu...
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Nature Publishing Group
2016-03-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/ncomms11030 |
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doaj-01684b9a896d47d19e6de2ba77a9a1cb2021-05-11T10:36:41ZengNature Publishing GroupNature Communications2041-17232016-03-017111310.1038/ncomms11030Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer proliferation and chemoresistanceYasuaki Kabe0Takanori Nakane1Ikko Koike2Tatsuya Yamamoto3Yuki Sugiura4Erisa Harada5Kenji Sugase6Tatsuro Shimamura7Mitsuyo Ohmura8Kazumi Muraoka9Ayumi Yamamoto10Takeshi Uchida11So Iwata12Yuki Yamaguchi13Elena Krayukhina14Masanori Noda15Hiroshi Handa16Koichiro Ishimori17Susumu Uchiyama18Takuya Kobayashi19Makoto Suematsu20Department of Biochemistry, Keio University School of Medicine, and Japan Science and Technology Agency (JST), Core Research for Evolutional Science and Technology (CREST)Department of Medical Chemistry and Cell Biology, Graduate School of Medicine, Kyoto UniversityDepartment of Biochemistry, Keio University School of Medicine, and Japan Science and Technology Agency (JST), Core Research for Evolutional Science and Technology (CREST)Bioorganic Research Institute, Suntory Foundation for Life SciencesDepartment of Biochemistry, Keio University School of Medicine, and Japan Science and Technology Agency (JST), Core Research for Evolutional Science and Technology (CREST)Bioorganic Research Institute, Suntory Foundation for Life SciencesBioorganic Research Institute, Suntory Foundation for Life SciencesDepartment of Medical Chemistry and Cell Biology, Graduate School of Medicine, Kyoto UniversityDepartment of Biochemistry, Keio University School of Medicine, and Japan Science and Technology Agency (JST), Core Research for Evolutional Science and Technology (CREST)Department of Biochemistry, Keio University School of Medicine, and Japan Science and Technology Agency (JST), Core Research for Evolutional Science and Technology (CREST)Department of Chemistry, Faculty of Science, Hokkaido UniversityDepartment of Chemistry, Faculty of Science, Hokkaido UniversityDepartment of Medical Chemistry and Cell Biology, Graduate School of Medicine, Kyoto UniversityDepartment of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of TechnologyDepartment of Biotechnology, Graduate School of Engineering, Osaka UniversityDepartment of Biotechnology, Graduate School of Engineering, Osaka UniversityDepartment of Nanoparticle Translational Research, Tokyo Medical UniversityDepartment of Chemistry, Faculty of Science, Hokkaido UniversityDepartment of Biotechnology, Graduate School of Engineering, Osaka UniversityDepartment of Medical Chemistry and Cell Biology, Graduate School of Medicine, Kyoto UniversityDepartment of Biochemistry, Keio University School of Medicine, JST, Exploratory Research for Advanced Technology (ERATO), Suematsu Gas Biology ProjectPGRMC1 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.https://doi.org/10.1038/ncomms11030 |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Yasuaki Kabe Takanori Nakane Ikko Koike Tatsuya Yamamoto Yuki Sugiura Erisa Harada Kenji Sugase Tatsuro Shimamura Mitsuyo Ohmura Kazumi Muraoka Ayumi Yamamoto Takeshi Uchida So Iwata Yuki Yamaguchi Elena Krayukhina Masanori Noda Hiroshi Handa Koichiro Ishimori Susumu Uchiyama Takuya Kobayashi Makoto Suematsu |
| spellingShingle |
Yasuaki Kabe Takanori Nakane Ikko Koike Tatsuya Yamamoto Yuki Sugiura Erisa Harada Kenji Sugase Tatsuro Shimamura Mitsuyo Ohmura Kazumi Muraoka Ayumi Yamamoto Takeshi Uchida So Iwata Yuki Yamaguchi Elena Krayukhina Masanori Noda Hiroshi Handa Koichiro Ishimori Susumu Uchiyama Takuya Kobayashi Makoto Suematsu Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer proliferation and chemoresistance Nature Communications |
| author_facet |
Yasuaki Kabe Takanori Nakane Ikko Koike Tatsuya Yamamoto Yuki Sugiura Erisa Harada Kenji Sugase Tatsuro Shimamura Mitsuyo Ohmura Kazumi Muraoka Ayumi Yamamoto Takeshi Uchida So Iwata Yuki Yamaguchi Elena Krayukhina Masanori Noda Hiroshi Handa Koichiro Ishimori Susumu Uchiyama Takuya Kobayashi Makoto Suematsu |
| author_sort |
Yasuaki Kabe |
| title |
Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer proliferation and chemoresistance |
| title_short |
Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer proliferation and chemoresistance |
| title_full |
Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer proliferation and chemoresistance |
| title_fullStr |
Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer proliferation and chemoresistance |
| title_full_unstemmed |
Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer proliferation and chemoresistance |
| title_sort |
haem-dependent dimerization of pgrmc1/sigma-2 receptor facilitates cancer proliferation and chemoresistance |
| publisher |
Nature Publishing Group |
| series |
Nature Communications |
| issn |
2041-1723 |
| publishDate |
2016-03-01 |
| description |
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. |
| url |
https://doi.org/10.1038/ncomms11030 |
| work_keys_str_mv |
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