Interleukin-1 receptor accessory protein-like 1; also known as IL1RAPL1; can be detected at low levels in heart; skeletal muscle; ovary; skin; amygdala; caudate nucleus; corpus callosum; hippocampus; substantia nigra and thalamus. IL1RAPL1 functions as a homodimer; it interacts with NCS1; PTPRD. This interaction is PTPRD-splicing-dependent and induces pre- and post-synaptic differentiation of neurons and is required for IL1RAPL1-mediated synapse formation. During dendritic spine formation; it can bidirectionally induce pre- and post-synaptic differentiation of neurons by trans-synaptically binding to PTPRD.
X-linked interleukin-1 receptor accessory protein-like 2 (IL1RAPL2) or Interleukin-1 receptor 9 (IL-1R9) is a member of the interleukin 1 receptor family. This protein is similar to the interleukin 1 accessory proteins. IL-1R9/IL1RAPL2 shows restricted expression in fetal brain and is highly homologous to IL1RAPL; which is reportedly involved in nonsyndromic X-linked mental retardation. IL-1R9/IL1RAPL2 is highly homologous to IL-1R8. Both forms have no known ligands and receptor are found in the fetal brain. IL-1R9/IL1RAPL2 may function as a negative receptor. Both IL1RAPL1 and IL1RAPL2 have novel C-terminal sequences not present in other related proteins. IL-1R9/IL1RAPL2 may be strong candidates for X-linked non-syndromic mental retardation loci; and that molecules resembling IL-1 and IL-18 play a role in the development or function of the central nervous system.
Interleukin-1 Receptor Accessory Protein (IL-1RAcP) is a member of the interleukin-1 receptor family. It contains three Ig-like C2-type domains in the extracellular region and a long cytoplasmic domain implicated in signal transduction. IL-1RAcP acts as a non-ligand binding accessory component of the receptors for IL1α; IL1βand IL33. IL-1RAcP mediates interleukin-1-dependent activation of NF-kappa-B. It is part of the membrane-bound form of the IL-1 receptor. IL-1 RAcP takes part in the Signaling ways by the formation of a ternary complex containing IL1R1; TOLLIP; MYD88; and IRAK1 or IRAK2. In addition; IL-1RAcP modulates the response to interleukins by associating with soluble IL1R1 and enhancing interleukin-binding to the decoy receptor.
Interleukin-1 receptor accessory protein (IL-1RAcP) also known as Interleukin-1 receptor member 3 (IL-1R3) is a a cytokine receptor which binds interleukin 1. The IL-1 receptor accessory protein (IL1RAP) is a transmembrane protein that interacts with IL-1R and is required for IL-1 signal transduction. Interleukin 1 induces synthesis of acute phase and proinflammatory proteins during infection, tissue damage, or stress, by forming a complex at the cell membrane with an interleukin 1 receptor and an accessory protein. IL-1RAcP/IL-1R3 is a necessary part of the interleukin 1 receptor complex which initiates signalling events that result in the activation of interleukin 1-responsive genes. Alternative splicing of this gene results in two transcript variants encoding two different isoforms, one membrane-bound and one soluble. The ratio of soluble to membrane-bound forms increases during acute-phase induction or stress. IL-1RAcP/IL-1R3 mediates interleukin-1-dependent activation of NF-kappa-B. Isoform 1 is part of the membrane-bound form of the IL-1 receptor. Signaling involves formation of a ternary complex containing IL1R1, TOLLIP, MYD88, and IRAK1 or IRAK2. Isoform 2 modulates the response to interleukins by associating with soluble IL1R1 and enhancing interleukin-binding to the decoy receptor.
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