TNFRSF11B is a secreted protein; containing 2 death domains and 4 TNFR-Cys repeats. TNFRSF11B is a decoy receptor for the receptor activator of nuclear factor kappa B ligand (RANKL). By binding RANKL; TNFRSF11B inhibits nuclear kappa B (NF-κB) which is a central and rapid acting transcription factor for immune-related genes; and a key regulator of inflammation; innate immunity; and cell survival and differentiation. TNFRSF11B levels are influenced by voltage-dependent calcium channelsCav1.2. TNFRSF11B can reduce the production of osteoclasts by inhibiting the differentiation of osteoclast precursors into osteoclasts and also regulates the resorption of osteoclasts in vitroand in vivo. TNFRSF11B binding to RANKL on osteoblast/stromal cells; blocks the RANKL-RANK ligand interaction between osteoblast/stromal cells and osteoclast precursors. This has the effect of inhibiting the differentiation of the osteoclast precursor into a mature osteoclast.
TNFRSF11B is a secreted protein; containing 2 death domains and 4 TNFR-Cys repeats. TNFRSF11B is a decoy receptor for the receptor activator of nuclear factor kappa B ligand (RANKL). By binding RANKL; TNFRSF11B inhibits nuclear kappa B (NF-κB) which is a central and rapid acting transcription factor for immune-related genes; and a key regulator of inflammation; innate immunity; and cell survival and differentiation. TNFRSF11B levels are influenced by voltage-dependent calcium channelsCav1.2. TNFRSF11B can reduce the production of osteoclasts by inhibiting the differentiation of osteoclast precursors (osteoclasts are related to monocytes/macrophages and are derived from granulocyte/macrophage-forming colony units (CFU-GM)) into osteoclasts and also regulates the resorption of osteoclasts in vitroand in vivo. TNFRSF11B binding to RANKL on osteoblast/stromal cells; blocks the RANKL-RANK ligand interaction between osteoblast/stromal cells and osteoclast precursors. This has the effect of inhibiting the differentiation of the osteoclast precursor into a mature osteoclast.
Osteoprotegerin or TNFRSF11B is a member of the TNF-receptor superfamily. This protein is an osteoblast-secreted decoy receptor that functions as a negative regulator of bone resorption. This protein specifically binds to its ligand, osteoprotegerin ligand, both of which are key extracellular regulators of osteoclast development. Studies of the mouse counterpart also suggest that this protein and its ligand play a role in lymph-node organogenesis and vascular calcification. Alternatively spliced transcript variants of this gene have been reported, but their full length nature has not been determined. Osteoprotegerin/TNFRSF11B acts as decoy receptor for RANKL and thereby neutralizes its function in osteoclastogenesis. This protein may inhibit the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local RANKL/OPG ratio. Osteoprotegerin/TNFRSF11B also play a role in preventing arterial calcification, act as decoy receptor for TRAIL and protect against apoptosis. TRAIL binding blocks the inhibition of osteoclastogenesis.
Osteopetrosis-associated transmembrane protein 1 (OSTM1) is a Single-pass type I membrane protein. It is expressed in many hematopoietic cells of the myeloid and lymphoid B- and T-lineages. The analysis of OSTM1 association with CLCN7 demonstrated that OSTM1 requires CLCN7 to localize to lysosomes, whereas the formation of a CLCN7-OSTM1 complex is required to stabilize CLCN7. The researches found that OSTM1 plays a major role in myelopoiesis and lymphopoiesis and provided evidence of a crosstalk mechanism between hematopoietic cells for osteoclast activation. Thus, OSTM1 has a important role in osteoclast function and activation. The loss of function of OSTM1 results in deregulation of multiple hematopoietic lineages in addition to osteoclast lineage, OSTM1-defect patients display the most severe recessive osteopetrotic phenotype and die at early ages. Furthermore, it is suggested that OSTM1 has a primary role in neural development not related to lysosomal dysfunction. The canonical Wnt/beta-catenin signaling pathway may be a molecular basis for OSTM1 mutations and severe autosomal recessive osteopetrosis (ARO).
Otolin (OTOL1), also known as C1qTNF15, is an approximately 65 kDa protein found in the otoconial membrane lining the cochlea and vestibular labyrinth of the inner ear. Collagen-like protein specifically expressed in the inner ear, which provides an organic scaffold for otoconia, a calcium carbonate structure in the saccule and utricle of the ear. It associates into multimers and disulfide-linked oligomers and also associates with other otoconial proteins including and Otoconin-90 (also known as PLA2G2A, PLA2L, and phospholipase A2 homolog) and Cerebellin-1. It is extensively glycosylated and has multiple hydroxylated proline residues in the collagenous regions.
Ubiquitin thioesterase OTUB1, also known as Deubiquitinating enzyme OTUB1, OTU domain-containing ubiquitin aldehyde-binding protein 1, Otubain-1, Ubiquitin-specific-processing protease OTUB1, OTUB1 and OTB1, is a cytoplasm protein which belongs to thepeptidase C65 family. OTUB1 is a hydrolase that can remove conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation. OTUB1 is a regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen. OTUB1 acts via its interaction with RNF128 / GRAIL, a crucial inductor of CD4 T-cell anergy. Isoform1 of OTUB1 destabilizes RNF128, leading to prevent anergy. In contrast, isoform2of OTUB1 stabilizes RNF128 and promotes anergy. OTUB1 regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128. Deubiquitinates estrogen receptor alpha (ESR1). OTUB1 mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains. OTUB1 is also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to 'Lys-48'-linked ubiquitin.
Ubiquitin Thioesterase OTUB2 belongs to the peptidase C65 family, functions as a hydrolase that can remove conjugated ubiquitin from proteins in vitro, may plays an important regulatory role at the level of protein turnover by preventing degradation. OTUB2 is expressed at higher levels in the brain.
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