Article
Phosphorylation of RelA/p65 on serine 536 defines an I{kappa}B{alpha}-independent NF-{kappa}B pathway.
The Journal of biological chemistry - 14 Oct 2005
Sasaki Carl Y, Barberi Theresa J, Ghosh Paritosh, Longo Dan L
Abstract excerpt
The association of the NF-kappaB p65/p50 dimer with IkappaBalpha 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 IkappaBalpha....
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
