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 Portfolio
2016
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oai:doaj.org-article:01684b9a896d47d19e6de2ba77a9a1cb2021-12-02T16:49:40ZHaem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer proliferation and chemoresistance10.1038/ncomms110302041-1723https://doaj.org/article/01684b9a896d47d19e6de2ba77a9a1cb2016-03-01T00:00:00Zhttps://doi.org/10.1038/ncomms11030https://doaj.org/toc/2041-1723PGRMC1 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.Yasuaki KabeTakanori NakaneIkko KoikeTatsuya YamamotoYuki SugiuraErisa HaradaKenji SugaseTatsuro ShimamuraMitsuyo OhmuraKazumi MuraokaAyumi YamamotoTakeshi UchidaSo IwataYuki YamaguchiElena KrayukhinaMasanori NodaHiroshi HandaKoichiro IshimoriSusumu UchiyamaTakuya KobayashiMakoto SuematsuNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-13 (2016) |
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| topic |
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Science Q 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 |
| 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. |
| format |
article |
| 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 |
| 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 Portfolio |
| publishDate |
2016 |
| url |
https://doaj.org/article/01684b9a896d47d19e6de2ba77a9a1cb |
| work_keys_str_mv |
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1718383255787405312 |