IκBβ is part of the NFκB complex and it inactivates NFκB complex by binding to it and trapping it in the cytoplasm. Phosphorylation of serine residues on IκBβ mediated by IκB kinases leads to its destruction via the ubiquitination pathway thereby allowing activation of the NFκB complex which translocates into the nucleus and binds DNA at kappa-B-binding motifs. The PEST domain of IkBβ can interact with two proteins KBRAS1 and KBRAS2 and this interaction can decrease the rate of degradation IκBβ. IκBβ has been shown to participate in multiple signaling pathways including adipocytokine signaling pathway, B-cell receptor signaling pathway, T-cell receptor signaling pathway and Hypoxia.
Science (New York, N.Y.), 298(5596), 1241-1245 (2002-11-09)
Nuclear localization of the transcriptional activator NF-kappaB (nuclear factor kappaB) is controlled in mammalian cells by three isoforms of NF-kappaB inhibitor protein: IkappaBalpha, -beta, and - epsilon. Based on simplifying reductions of the IkappaB-NF-kappaB signaling module in knockout cell lines
Science (New York, N.Y.), 287(5454), 869-873 (2000-02-05)
Small guanosine triphosphatases, typified by the mammalian Ras proteins, play major roles in the regulation of numerous cellular pathways. A subclass of evolutionarily conserved Ras-like proteins was identified, members of which differ from other Ras proteins in containing amino acids
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