[HTML][HTML] Phosphorylation of RelA/p65 on serine 536 defines an IκBα-independent NF-κB pathway

CY Sasaki, TJ Barberi, P Ghosh, DL Longo - Journal of Biological …, 2005 - ASBMB
The association of the NF-κB p65/p50 dimer with IκBα plays a pivotal role in regulating its
nuclear translocation and gene transcription. In addition, serine phosphorylation at various
sites of the p65 subunit has been shown to be important in initiating transcription. Here we
demonstrate that the regulation of nuclear translocation of p65 phosphorylated at serine 536
is not dependent on IκBα. Stimulation of either Jurkat or normal human T cells resulted in the
nuclear translocation of phospho-p65 (Ser 536). In addition, the phospho-p65 (Ser 536) was …