Human PVRIG (poliovirus receptor related immunoglobulin domain-containing protein), also known as CD112 receptor (CD112R), is an approximately 34 kDa single transmembrane protein in the poliovirus receptor-like protein (PVR) family. The extracellular domain sequence of human and mouse PVRIG have approximately 65% similarity. PVRIG functions as a cell surface receptor for Nectin-2/CD112, a cell surface protein that is widely expressed on antigen-presenting cells and tumor cells. Disrupting the PVRIG/Nectin-2 interaction enhances human T cell response, suggesting PVRIG is a novel checkpoint for human T cells. PVRIG may act as a coinhibitory receptor that suppresses T-cell receptor-mediated signals.
Nectin-1 is a type I transmembrane glycoprotein belonging to the Ig superfamily. Nectin-1 promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between Nectin-1 and Nectin-3 and between Nectin-1 and Nectin-4. Nectin ECDs contain three Ig like domains: an N terminal V type that mediates ligand binding, and two C2 type. Nectin-1 binds viral Glycoprotein D to mediate Herpesvirus (but not Poxvirus) entry into vaginal mucosa, sensory neurons and fibroblasts. In forming adherens junctions and synapses, Nectin-1 and Nectin-3 initiate cell-cell interactions, recruiting αvβ3 integrin extracellularly and cadherins intracellularly through afadin and other junctional proteins. These interactions organize the cytoskeleton, strengthen attachment to basement membrane and promote further cell-cell connections. Nectin-1 and Nectin-3 have been found to localize assymetrically along the chemical synapse, with Nectin-1 primarily on the axonal side and Nectin-3 on the dendritic side. Deficiency of Nectin-1 can result in cleft lip/palate ectodermal dysplasia. Nectin-1 downregulation in epithelial cancers is mediated in part by ectodomain shedding, but it may contribute to invasiveness.
CD112 is a type I transmembrane glycoprotein belonging to the Immunoglobulin superfamily. It comprises one Ig-like V-type domain and two Ig-like C2-type domains in the extracellular region. The V domain is believed to mediate nectin binding to its ligands. Nectin2 is known to bind the pseudorabies virus, and herpes simplex virus2 (HSV2), involving in cell to cell spreading of these viruses. It does not bind poliovirus. As a homophilic adhesion molecule, CD112 is found concentrated in adherens junctions, and exists on neurons, endothelial cells,epithelial cells and fibroblasts. CD112 has been identified as the ligand for DNAM-1 (CD226), and the interaction of CD226/CD112 mediates cytotoxicity and cytokine secretion by T and NK cells. The costimulatory responses may be a critical component in allergic reactions and may therefore become targets for anti-allergic therapy.
Partner of Y14 and Mago (WIBG) is a key regulator of the Exon Junction Complex (EJC). EJC is a multiprotein complex that associates immediately upstream of the exon-exon junction on mRNAs, is a positional landmarker for the intron exon structure of genes, and directs post-transcriptional processes in the cytoplasm, for instance mRNA export, nonsense-mediated mRNA decay or translation. WIBG is a cytoplasmic RNA-binding protein, it can be excluded from nucleus by Crm1. WIBG as a cooperateing partner of Mago-14, relates with Mago-14 by its N-terminal domain.
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