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- W2296998275 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." @default.
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- W2296998275 date "2016-03-18" @default.
- W2296998275 modified "2023-10-15" @default.
- W2296998275 title "Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer proliferation and chemoresistance" @default.
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- W2296998275 doi "https://doi.org/10.1038/ncomms11030" @default.
- W2296998275 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4802085" @default.
- W2296998275 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26988023" @default.
- W2296998275 hasPublicationYear "2016" @default.
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