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48887BiochemicalReaction2482

Source:http://www.reactome.org/biopax/48887BiochemicalReaction2482

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Authored: Luo, F, 2005-11-10 11:23:18, Edited: Shamovsky, V, 2009-12-16, In humans, the IKKs - IkB kinase (IKK) complex serves as the master regulator for the activation of NF-kB by various stimuli. It contains two catalytic subunits, IKK alpha and IKK beta, and a regulatory subunit, IKKgamma/NEMO. The activation of the IKK complex and the NFkB mediated antiviral response are dependent on the phosphorylation of IKK alpha/beta at its activation loop and the ubiquitination of NEMO [Solt et al 2009; Li et al 2002]. NEMO ubiquitination by TRAF6 is required for optimal activation of IKKalpha/beta; it is unclear if NEMO subunit undergoes K63-linked or linear ubiquitination.<p>This basic trimolecular complex is referred to as the IKK complex. Each catalytic IKK subunit has a N-term kinase domain and leucine zipper (LZ) motifs, a helix-loop-helix (HLH) and a C-ter NEMO binding domain (NBD). IKK catalytic subunits are dimerized through their LZ motifs.<p>IKK beta is the major IKK catalytic subunit for NF-kB activation. Phosphorylation in the activation loop of IKK beta requires Ser177 and Ser181 and thus activates the IKK kinase activity, leading to the IkB alpha phosphorylation and NF-kB activation., Reviewed: Kufer, TA, 2011-04-28, Reviewed: Rittinger, K, 2011-06-06, Reviewed: Wong, Edmond, 2011-06-06
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Activated TAK1 mediates phosphorylation of the IKK Complex
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2.7.11
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