| First Author | Born TL | Year | 1998 |
| Journal | J Biol Chem | Volume | 273 |
| Issue | 45 | Pages | 29445-50 |
| PubMed ID | 9792649 | Mgi Jnum | J:50863 |
| Mgi Id | MGI:1312979 | Doi | 10.1074/jbc.273.45.29445 |
| Citation | Born TL, et al. (1998) Cloning of a novel receptor subunit, AcPL, required for interleukin-18 signaling. J Biol Chem 273(45):29445-50 |
| abstractText | We have identified a novel member of the interleukin-1 (IL-1) receptor family, which we have termed AcPL. In transient transfection assays, we were unable to demonstrate a role for AcPL in IL-1-induced activation of NFkappaB. Interleukin-18 (interferon-gamma-inducing factor) is another member of the IL-1 family of cytokines, and it has recently been shown that IL-18 has a weak affinity for IL-1R-rp1. We examined whether AcPL might function alone or in concert with IL-1R-rp1 to mediate IL-18 signaling. We found that both IL-1R-rp1 and AcPL expression were required for induction of NFkappaB activity and for activation of c-Jun N-terminal kinase in response to IL-18. Furthermore, a dominant negative version of AcPL specifically inhibited IL-18 signaling. In vitro immunoprecipitation assays demonstrated that AcPL alone was unable to bind IL-18 with any appreciable affinity. We propose that although IL-1R-rp1 binds the cytokine, IL-1R-rp1 and AcPL proteins are both required for IL-18 signaling, analogous to the requirement for both IL-1R and IL-1RAcP in IL-1-mediated responses. |
