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 andT NFRSF4; is a Tcellco-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). TheT-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.
Oxidative stress-responsive 1 protein (OXSR1), also known as Serine/threonine-protein kinase OSR1, is a member of the Ser/Thr protein kinase family of proteins. OXSR1 regulates downstream kinases in response to environmental stress, and may play a role in regulating the actin cytoskeleton. OXSR1 is a 58 kDa protein of 527 amino acids that is widely expressed in mammalian tissues and cell lines. The amino acid (aa) sequence of the predicted OXSR1 protein is 39% identical to that of human SOK1. Of potential regulators surveyed, endogenous OXSR1 is activated only by osmotic stresses, notably sorbitol and to a lesser extent NaCl. OXSR1 did not increase the activity of coexpressed JNK, nor did it activate three other MAPKs, p38, ERK2, and ERK5. Phosphorylation by OXSR1 modulates the G protein sensitivity of PAK isoforms. The OXSR1 and SPAK are key enzymes in a signalling cascade regulating the activity of Na+/K+/2Cl- co-transporters (NKCCs) in response to osmotic stress. Both kinases have a conserved carboxy-terminal (CCT) domain, which recognizes a unique peptide (Arg-Phe-Xaa-Val) motif. The OXSR1 and SPAK kinases specifically recognize their upstream activators and downstream substrates.
May be the important intermediate by which p53/TP53 mediates its role as an inhibitor of cellular proliferation in response to DNA damage. Binds to and inhibits cyclin-dependent kinase activity, preventing phosphorylation of critical cyclin-dependent kinase substrates and blocking cell cycle progression. Functions in the nuclear localization and assembly of cyclin D-CDK4 complex and promotes its kinase activity towards RB1. At higher stoichiometric ratios, inhibits the kinase activity of the cyclin D-CDK4 complex.
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