Interleukin 1 receptor; type II (IL1R2) also known as CD121b (Cluster of Differentiation 121b) is a cytokine receptor that belongs to the interleukin-1 receptor family. This protein binds interleukin alpha (IL1A); interleukin beta (IL1B); and interleukin 1 receptor; type I (IL1R1/IL1RA); and acts as a decoy receptor that inhibits the activity of its ligands. The pleiotropic cytokine IL1 is produced to regulate development and maintenance of the inflammatory responses; and binds to specific plasma membrane receptors on cells. Two distinct types of IL1 receptors which are able to bind IL1 specifically have been identified; designated as IL1RI (IL1RA) and IL1RII (IL1RB). IL1R1 contributes to IL-1 signaling; whereas the IL-1R2/CD121b has no signaling property and acts as a decoy for IL-1. IL-1R2/CD121b structurally consisting of a ligand binding portion comprised of three Ig-like domains; a single transmembrane region; and a short cytoplasmic domain; is expressed in a variety of cell types including B lymphocytes; neutrophils; monocytes; large granular leukocytes and endothelial cells. Interleukin 4 (IL4) is reported to antagonize the activity of interleukin 1 by inducing the expression and release of this cytokine.
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 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.
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