Translocation nuclear

The NHR contains also the conserved Calcineurin docking site, PxlxIT, required for the physical interaction of NEAT and Calcineurin. Dephosphorylation of at least 13 serines residues in the NHR induces a conformational change that exposes the nuclear localization sequences (NLS), allowing the nuclear translocation of NEAT. Rephosphorylation of these residues unmasks the nuclear export sequences that direct transport back to the cytoplasm. Engagement of receptors such as the antigen receptors in T and B cells is coupled to phospholipase C activation and subsequent production of inositol triphosphate. Increased levels of inositol triphosphate lead to the initial release of intracellular stores of calcium. This early increase of calcium induces opening of the plasma membrane calcium-released-activated-calcium (CRAC) channels,... 

Rel homology domain (RHD) that encompasses a sequence-specific DNA-binding domain, a dimerization domain and a nuclear translocation signal (NLS) (Fig. la). RelA, cRel, and RelB contain a transcription activation domain (TAD). NF-kB 1 and NF-kB2 are synthesized as large precursors, pi 05 and pi 00, that are posttranslationnally processed to generate the mature forms, p50 and p52, which lack a TAD. 

Fig. 2.2 Simplified scheme of oxidant/antioxidant regulation ofNF-KB activation. Different stimuli, leading to an increase of ROS generation inside the ceU, activate the phosphorylation of IkB inhibitory protein and the subsequent proteolysis. Thioredoxin (Trx) may reduce activated NF-kB proteins facilitating nuclear translocation.Qnce released from IkB, the NF-kB complex translocates into the nucleus and the binding to DNA domain in the promoters and enhancers of genes such as TNF-a, IL-1, proliferation and chemotactic factors, adhesion molecule. Some of these genes, in turn, may further induce NF-kB activation, leading to a vicious circle if the regulatory cellular system escapes from...

Mistry P, Lucier GW, Fowler BA. 1985. High affinity lead binding proteins from rat kidney cytosol mediate cell-free nuclear translocation of lead. J Pharmacol Exp Ther 232 462-469. 

Endosomal leakage and nuclear translocation of multiwalled carbon nanotubes developing a model for celluptake. Nano Letters, 9 (12), 4370-4375. 

Berezovska, O., Jack, C., McLean, P., Aster, J. C., Hicks, C., Xia, W., Wolfe, M. S., Weinmaster, G., Selkoe, D. J. and Hyman, B. T. (2000). Rapid Notch 1 nuclear translocation after ligand binding depends on presenilin-associated gamma-secretase activity. Ann. N.Y. Acad. Sci. 

Longshaw, V.M. et al. (2004) Nuclear translocation of the Hsp70/Hsp90 organizing protein mSTIl is regulated by cell cycle kinases./. Cell Sci. 117, 701-710. 

As previously noted, the LBD of the receptor presents a series of functions that are not very well delimited such as those of dimerization with another receptor, nuclear translocation, and activation of the ligand-dependent gene transcription. As was just mentioned, the interaction of a ligand with its receptor has as its immediate consequence the conformational change of the molecule, a change that also determines the molecule s functionality. The importance of this point is that the stated conformational change is predetermined by the chemical nature of the ligand and the form in which it interacts with the receptor. 

Marcus, R., Holsapple, M., and Kaminski, N., Lipopolysaccharide activation of murine splenocytes and splenic B cells increased the expression of aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator, J. Pharmacol. Exper. Therap.. 287, 1113, 1998. 

Camacho, I., et. al., Treatment of mice with 2,3,7,8-tetrachlorodibenzo-p-dioxin leads to aryl hydrocarbon receptor-dependent nuclear translocation of NF-kappa B and expression of Fas ligand in thymic stromal cells and consequent T cell apoptosis, J. Immunol., 175, 90, 2005. 

Lavin, A., Hahn, D., and Gasiewicz, T. A., Expression of functional aromatic hydrocarbon receptor and aromatic hydrocarbon nuclear translocator proteins in murine bone marrow stromal cells, Arch. Biochem. Biophys., 352, 9, 1998. 

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