Nuclear Factor – kappa B (NF-?B) is a major transcription factor that controls the survival and functioning of cells. Deregulated NF-?B is associated with auto-immune disorders and Cancer. NF-?B in T cells decides the fate of an immune reaction. NF-?B is turned on by T cell receptor (TCR) activation by a signaling cascade that involves CARMA1-BCL10-MALT1 (CBM) and Inhibitor of kappa B kinase (IKK) complex. TCR inducibly phosphorylates and ubiquitinates IKK complex to activate NF-?B. However, the molecular mechanism of IKK complex activation and the events that interconnect CBM and IKK complexes are not well understood. This study evaluates the roles and requirements of IKK phosphorylation and ubiquitination. This study finds that the phosphorylation of IKK is mediated by PKC- TAK1 complex and ubiquitination is mediated by CBM complex independently. Thus, phosphorylation and ubiquitination of the IKK complex are controlled by two distinct signaling pathways. This study proposes a working model for TCR induced NF-?B activation, which depicts that the CBM complex regulates IKK ubiquitination, whereas PKC-TAK1 regulates IKK phosphorylation.

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