A protein phosphatase is involved in the inhibition of histone deacetylation by sodium butyrate.
Treatment of cells with sodium butyrate is known to increase histone acetylation by inhibiting deacetylases. Here we have observed, in cultured hepatoma cells, that the potent serine-threonine phosphatase inhibitors, okadaic acid or calyculin A, inhibited phosphatase activity and concomitantly decreased the histone acetylation classically maintained by sodium butyrate. These results suggest that a protein phosphatase may mediate the sodium butyrate effect on deacetylases. Since we have previously found that such a protein would also mediate the sodium butyrate effect on gene expression, we propose that a phosphatase activity constitutes an early and essential step in the sodium butyrate-triggered signalling pathway.
Cuisset
L
L
Laboratoire de Biologie Moléculaire des Cellules Eucaryotes, I.C.G.M-EA 1501, Université Paris V, Faculté de Médecine, France.
Tichonicky
L
L
Delpech
M
M
D000123:Acetyltransferases / Q000187:drug effects*; D002087:Butyrates / Q000494:pharmacology*; D020148:Butyric Acid; D051548:Histone Acetyltransferases; D006655:Histone Deacetylases / Q000187:drug effects*; D006657:Histones / Q000378:metabolism*; D008387:Marine Toxins; D019319:Okadaic Acid / Q000494:pharmacology; D010080:Oxazoles / Q000494:pharmacology; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors / Q000187:drug effects*; D029701:Saccharomyces cerevisiae Proteins
D002087:Butyrates; D006657:Histones; D008387:Marine Toxins; D010080:Oxazoles; D029701:Saccharomyces cerevisiae Proteins; D020148:Butyric Acid; D019319:Okadaic Acid; C059041:calyculin A; D000123:Acetyltransferases; D051548:Histone Acetyltransferases; D010749:Phosphoprotein Phosphatases; D006655:Histone Deacetylases