| First Author | Ryoden Y | Year | 2020 |
| Journal | J Immunol | Volume | 204 |
| Issue | 3 | Pages | 559-568 |
| PubMed ID | 31862710 | Mgi Jnum | J:284036 |
| Mgi Id | MGI:6388990 | Doi | 10.4049/jimmunol.1900448 |
| Citation | Ryoden Y, et al. (2020) Functional Expression of the P2X7 ATP Receptor Requires Eros. J Immunol 204(3):559-568 |
| abstractText | In response to extracellular ATP, the purinergic receptor P2X7 mediates various biological processes, including phosphatidylserine (PtdSer) exposure, phospholipid scrambling, dye uptake, ion transport, and IL-1beta production. A genome-wide CRISPR screen for molecules responsible for ATP-induced PtdSer exposure identified a transmembrane protein, essential for reactive oxygen species (Eros), as a necessary component for P2X7 expression. An Eros-null mouse T cell line lost the ability to expose PtdSer, to scramble phospholipids, and to internalize a dye YO-PRO-1 and Ca(2+) ions. Eros-null mutation abolished the ability of an LPS-primed human THP-1 macrophage cell line and mouse bone marrow-derived macrophages to secrete IL-1beta in response to ATP. Eros is localized to the endoplasmic reticulum and functions as a chaperone for NADPH oxidase components. Similarly, Eros at the endoplasmic reticulum transiently associated with P2X7 to promote the formation of a stable homotrimeric complex of P2X7. These results indicated that Eros acts as a chaperone not only for NADPH oxidase, but also for P2X7, and contributes to the innate immune reaction. |
