Project description:The functions of MYC acetylation have remained unclear. In this study we identified the major lysine residues of MYC that are acetylated by p300 and GCN5 in cancer cell lines and established the requirment of three specific acetyl-lysine (AcK) residues for MYC transformation of Rat1a fibroblasts and MCF10 mammary epithelial cells. We further uncovered gene-selective regulatory functions and conserved genetic programs and biolofical processes regulated by MYC AcK residues in both cell types.
Project description:The functions of MYC acetylation have remained unclear. In this study we identified the major lysine residues of MYC that are acetylated by p300 and GCN5 in cancer cell lines and established the requirment of three specific acetyl-lysine (AcK) residues for MYC transformation of Rat1a fibroblasts and MCF10 mammary epithelial cells. We further uncovered gene-selective regulatory functions and conserved genetic programs and biolofical processes regulated by MYC AcK residues in both cell types.
Project description:Detection the acetylated lysine residues of Acs (between the TPA editor-mediated acetylation (At2-dCas12a-crRNA) and the true acetylation in vivo (dCas12a-crRNA))
Project description:detection the acetylated lysine residues of RNase II (between the TPA editor-mediated acetylation (At2-dCas12a-crRNA) and the true acetylation in vivo (dCas12a-crRNA))
Project description:Peroxisome proliferator-activated receptorg (PPARg), which is expressed in a variety of malignancies, governs biological functions through transcriptional programs. Defining the molecular mechanisms governing selection of canonical versus non-canonical PPARg binding sequences may provide the opportunity to design regulators with distinct functions and side effects. PPARg is acetylated at multiple residues including K268/293 in mouse Pparg2 and the conserved lysine residues (K154/155) in mouse Pparg1. Herein, the PPARg acetylated residues K154/155 were shown to be essential for growth control, and the induction of transcriptional modules governing growth factor signaling, cellular apoptosis and autophagy. The K154/155 residues determined the selection of genome wide DNA binding sites, altering the selection from canonical to non-canonical (C/EBP) DNA sequence specific binding. The gene signature reflecting the acetylation-dependent genomic occupancy provided predictive value in patient survival outcome. Pparg1 participates in ErbB2-induced tumor growth and inflammation and represents a relevant target for therapeutic coextinction.