[HTML][HTML] Phosphorylation of serine 468 by GSK-3β negatively regulates basal p65 NF-κB activity
H Buss, A Dorrie, ML Schmitz, R Frank… - Journal of Biological …, 2004 - ASBMB
The activity of NF-κB is controlled at several levels including the phosphorylation of the
strongly transactivating p65 (RelA) subunit. However, the overall number of phosphorylation
sites, the signaling pathways and protein kinases that target p65 NF-κB and the functional
role of these phosphorylations are still being uncovered. Using a combination of peptide
arrays with in vitro kinase assays we identify serine 468 as a novel phosphorylation site of
p65 NF-κB. Serine 468 lies within a GSK-3β consensus site, and recombinant GSK-3β …
strongly transactivating p65 (RelA) subunit. However, the overall number of phosphorylation
sites, the signaling pathways and protein kinases that target p65 NF-κB and the functional
role of these phosphorylations are still being uncovered. Using a combination of peptide
arrays with in vitro kinase assays we identify serine 468 as a novel phosphorylation site of
p65 NF-κB. Serine 468 lies within a GSK-3β consensus site, and recombinant GSK-3β …