Regular ArticleProtein Kinase C Is Not Involved in Ah Receptor Transformation and DNA Binding
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The complex biology of aryl hydrocarbon receptor activation in cancer and beyond
2023, Biochemical PharmacologyThe significance of the nongenomic pathway in mediating inflammatory signaling of the dioxin-activated Ah receptor to cause toxic effects
2009, Biochemical PharmacologyCitation Excerpt :Despite the generally held notion that signaling transmitted through nongenomic modes produces only short and acute effects, moves are now being made to re-evaluate the validity of such a notion [77]. In studies on the classical model of ligand-activated AHR action, the topic of the possible involvement of protein kinases and phosphatases has largely been centered around the effect of phosphorylation on the AHR protein proper [78]. This certainly is important particularly in the case of resolving the cause for the ligand-independent activation (LIA) of AHR [79], but it should not be confused with the case of nongenomic signaling of the ligand-activated AHR, since so far as known the consequence of the latter action is totally different from LIA.
Role of cAMP in mediating AHR signaling
2009, Biochemical PharmacologyCitation Excerpt :In line with this, treatment with dioxin plus the PKC inhibitor staurosporine almost completely blocked dioxin-initiated induction of CYP1A1 transcription [71]. In contrast, it has also been reported that staurosporine (under conditions where no protein kinase activity was detectable in cytosol) did not inhibit translocation of the liganded AHR to the nucleus nor its binding to DNA [73]. These authors concluded that protein kinase activity does not appear to be necessary for dioxin-dependent AHR transformation and DNA bindig [73].
The aryl hydrocarbon receptor (AhR) tyrosine 9, a residue that is essential for AhR DNA binding activity, is not a phosphoresidue but augments AhR phosphorylation
2004, Journal of Biological ChemistryCitation Excerpt :Immunopurified AhR Is Phosphorylated by PKC, and AhRY9F Inhibits PKC-elicited Phosphorylation—The inability of the anti-AhRpY9 antibody to recognize the AhR together with the two-dimensional gel electrophoresis data suggesting that a mutation of tyrosine 9 still results in a less negatively charged receptor support a hypothesis that tyrosine 9 is required for normal post-translational modification of other AhR residues. There is much published data implicating the importance of phosphorylation for AhR activity and, in particular, PKC has been observed to be important in the regulation of AhR activity in whole cells (for example, Refs. 26 and 29–32). In an attempt to determine if PKC was capable of phosphorylating the full-length AhR, wild-type and mutant AhRs were immunoprecipitated from rabbit reticulocyte lysate and incubated with purified PKC and [32P]ATP.