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.
CD200 is a transmembrane immunoregulatory protein that belongs to the immunoglobulin superfamily. It contains one Ig like V type domain and one Ig like C2 type domain in its extracelluar domain. CD200 is widely but not ubiquitously expressed. Its receptor (CD200R) is restricted primarily to mast cells; basophils; macrophages; and dendritic cells; which suggests myeloid cell regulation as the major function of CD200. CD200 and CD200R associate via their respective N-terminal Ig-like domains. In myeloid cells; CD200R initiates inhibitory signals following receptor-ligand contact. In T cells; CD200 functions as a co-stimulatory molecule independent of the CD28 pathway. In addition; CD200 also plays an important role in prevention of graft rejection; autoimmune diseases and spontaneous abortion.
OX40; also termed CD134 and TNFRSF4; is a T cell co-stimulatory molecule of the TNF receptor superfamily which plays a key role in the survival and homeostasis of effector and memory T cells. OX40 is expressed on CD4+ and CD8+ T cells upon engagement of the TCR by antigen presenting cells along with co-stimulation by CD40-CD40 Ligand and CD28-B7. The interaction between OX40 and OX40 ligand (OX40L) will occur when activated T cells bind to professional antigen-presenting cells (APCs). The T-cell functions; including cytokine production; expansion; and survival; are then enhanced by the OX40 costimulatory signals. OX40 signals are critical for controlling the function and differentiation of Foxp3+ regulatory T cells. OX40-OX40L interaction regulates T-cell tolerance; peripheral T-cell homeostasis; and T-cell-mediated inflammatory diseases.
OX40;also termed CD134 and TNFRSF4; is a T cell co-stimulatory molecule of the TNF receptor superfamily which plays a key role in the survival and homeostasis of effector and memory T cells. OX40 is expressed on CD4+ and CD8+ T cells upon engagement of the TCR by antigen presenting cells along with co-stimulation by CD40-CD40 Ligand and CD28-B7. The interaction between OX40 and OX40 ligand (OX40L) will occur when activated T cells bind to professional antigen-presenting cells (APCs). The T-cell functions; including cytokine production; expansion; and survival; are then enhanced by the OX40 costimulatory signals. OX40 signals are critical for controlling the function and differentiation of Foxp3+ regulatory T cells. OX40-OX40L interaction regulates T-cell tolerance; peripheral T-cell homeostasis; and T-cell-mediated inflammatory diseases.
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