[HTML][HTML] Protein kinase C δ associates with the interleukin-6 receptor subunit glycoprotein (gp) 130 via Stat3 and enhances Stat3-gp130 interaction
V Novotny-Diermayr, T Zhang, L Gu, X Cao - Journal of Biological …, 2002 - ASBMB
The transcriptional regulation of Stat proteins is controlled through their C-terminal domains,
which harbor both a tyrosine phosphorylation site, required for dimerization and subsequent
nuclear translocation, and a serine phosphorylation site, required for maximum
transcriptional activity. Previously, we reported that protein kinase Cδ (PKCδ)
phosphorylates and interacts with Stat3 in an interleukin (IL)-6-dependent manner. In this
study, we further characterized this interaction, and investigated the potential role of such an …
which harbor both a tyrosine phosphorylation site, required for dimerization and subsequent
nuclear translocation, and a serine phosphorylation site, required for maximum
transcriptional activity. Previously, we reported that protein kinase Cδ (PKCδ)
phosphorylates and interacts with Stat3 in an interleukin (IL)-6-dependent manner. In this
study, we further characterized this interaction, and investigated the potential role of such an …