Transient and Selective NF-κB p65 Serine 536 Phosphorylation Induced by T Cell Costimulation Is Mediated by IκB Kinase β and Controls the Kinetics of p65 Nuclear Import 1

By Ivan Mattioli, A. Sebald, Cyril Bucher, R. Charles, H. Nakano, T. Doi, M. Kracht, M. Schmitz. Journal of Immunology, 2004

225 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Good cop, bad cop: the different faces of NF-κB (2006, background): “For example, IKKb has been shown to phosphorylate RelA at serine 536, a modification reported to stimulate NF-kB transcriptional activity,(11,13) decrease its affinity for IkBa(27) and promote its nuclear import.(28,29) In addition, various stimuli in T cells can promote nuclear translocation of Ser”
Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway (2006, background): “Interestingly, one of the Ser-536 kinases is IKKb (Sakurai et al., 1999; Haller Oncogene et al., 2002; Mattioli et al., 2004; Buss et al., 2004b).”
IκB Kinase α-Mediated Derepression of SMRT Potentiates Acetylation of RelA/p65 by p300 (2006, background): “In contrast to previous reports (37), in which phosphorylation of RelA/p65(S536) contributes to nuclear export of NF- B, we failed to observe differences in cytoplasmic or nuclear localization of the mutant RelA/p65 protein compared to the wild-type RelA/p65 protein in our model system (Fig.”