Functional dissection of lysine deacetylases reveals that HDAC1 and p300 regulate AMPK.
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ABSTRACT: First identified as histone-modifying proteins, lysine acetyltransferases (KATs) and deacetylases (KDACs) antagonize each other through modification of the side chains of lysine residues in histone proteins. Acetylation of many non-histone proteins involved in chromatin, metabolism or cytoskeleton regulation were further identified in eukaryotic organisms, but the corresponding enzymes and substrate-specific functions of the modifications are unclear. Moreover, mechanisms underlying functional specificity of individual KDACs remain enigmatic, and the substrate spectra of each KDAC lack comprehensive definition. Here we dissect the functional specificity of 12 critical human KDACs using a genome-wide synthetic lethality screen in cultured human cells. The genetic interaction profiles reveal
SUBMITTER: Lin YY
PROVIDER: S-EPMC3277212 | biostudies-literature | 2012 Feb
REPOSITORIES: biostudies-literature
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