Unraveling Lysine Deacetylase Inhibitor Specificities for Endogenous Acetylation Sites

ABSTRACT: Data from ProteomeXchange: PXD ID: PXD001377. Experiment: Bufexamacproteome_hs_LH, file: 20120521_QE3_LC2_CHS_SA_Bufexamacproteome_03.mzml. From ProteomeXchange: {{i}} Lysine deacetylases (KDACs) are important regulators of biological processes. KDAC inhibitors (KDACIs) are important tools for basic research and attractive therapeutic candidates, yet their effects on in-vivo acetylation sites are poorly known. Here we obtained acetylation signatures for 19 different KDACIs that cover all known deacetylases. Most KDACIs targeting non-sirtuin deacetylases increased acetylation of a small, but specific, subset of the acetylome, and included sites on histone and other chromatin-associated proteins. Using a combination of genetic deletion and inhibitor treatment we found that the sirtuin inhibitor nicotinamide increased acetylation via SIRT1 inhibition, whereas tubacin and bufexamac affected cytoplasmic proteins through inhibition of HDAC6 ... {{/i}}

INSTRUMENT(S): Instrument

ORGANISM(S): Homo_sapiens_viruses, Human

DISEASE(S): Not Available

SUBMITTER: Schoelz C, et al.  

PROVIDER: GPM32320007813 | GPMDB |

REPOSITORIES: GPMDB