Interleukin-1 receptor type 2 (IL1R2) belongs to the interleukin-1 receptor family. Two distinct types of IL1 receptors which are able to bind IL1 specifically have been identified; designated as IL1RI (IL1RA) and IL1RII (IL1RB). IL1 receptor type II is a 68 kDa transmembrane protein found on B lymphocytes; neutrophils; monocytes; large granular leukocytes and endothelial cells. IL1R2 is non-signaling receptor forIL1A; IL1B and IL1RN; reduces IL1B activities. IL1R2 serves as a decoy receptor by competetive binding to IL1B and preventing its binding to IL1R1. IL1R2 modulates cellular response through non-signaling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors.
Interleukin-1 receptor accessory protein-like 1 (IL1RAPL1) is a member of interleukin-1 receptor family. The protein structurally comprises three extracellular immunoglobulin domains; which presumably mediate binding of an as yet unidentified ligand; a transmembrane region; and an intracellular domain; which is likely to enable signalling via the NFkB pathway. The means of signalling is almost certain to be identical to that used by the IL1R family and the more distally related Toll protein. L1RAPL1 protein physically interacts via its 150 aa C-terminal domain with neuronal calcium sensor-1 (NCS-1); a protein widely expressed in neurons and the related chromaffin and PC12 cells. IL1RAPL1 is an integral membrane protein responsible for a nonsyndromic form of mental retardation (MR). It is suggested to affect human cognitive ability to some extent; especially the memory and concentration capability.
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.
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