Biochemical pathways that regulate acetyltransferase and deacetylase activity in mammalian cells.
Protein phosphorylation is regulated dynamically in eukaryotic cells via modulation of the enzymatic activity of kinases and phosphatases. Like phosphorylation, acetylation has emerged as a critical regulatory protein modification that is altered dynamically in response to diverse cellular cues. Moreover, acetyltransferases and deacetylases are tightly linked to cellular signaling pathways. Recent studies provide clues about the mechanisms utilized to regulate acetyltransferases and deacetylases. The therapeutic value of deacetylase inhibitors suggests that understanding acetylation pathways will directly impact our ability to rationally target these enzymes in patients. Recently discovered mechanisms that directly regulate the catalytic activity of acetyltransferases and deacetylases provide exciting new insights about these enzymes.
Mellert
Hestia S
HS
Biomedical Graduate Studies, University of Pennsylvania, Philadelphia, PA 19104, USA.
McMahon
Steven B
SB
D000107:Acetylation; D000123:Acetyltransferases / Q000378:metabolism*; D000818:Animals; D002384:Catalysis; D006655:Histone Deacetylases / Q000378:metabolism*; D006657:Histones / Q000378:metabolism; D006801:Humans; D008954:Models, Biological; D015398:Signal Transduction; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism
D006657:Histones; D016159:Tumor Suppressor Protein p53; D000123:Acetyltransferases; D006655:Histone Deacetylases