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Role of MYC acetylated lysine residues in cell transformation and gene-selective regulation

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Rattus norvegicus Homo sapiens

PROVIDER: GSE220920 | GEO | 2024/03/20

REPOSITORIES: GEO

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Role of MYC acetylated lysine residues in cell transformation and gene-selective regulation [MCF10A]

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.

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Role of MYC acetylated lysine residues in cell transformation and gene-selective regulation [Rat1A]

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Role of MYC acetylated lysine residues in cell transformation and gene-selective regulation

Project description:Role of MYC acetylated lysine residues in cell transformation and gene-selective regulation

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Role of MYC acetylated lysine residues in cell transformation and gene-selective regulation [Rat1A]

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Role of MYC acetylated lysine residues in cell transformation and gene-selective regulation [MCF10A]

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MYC acetylated lysine residues drive oncogenic cell transformation and regulate select genetic programs for cell adhesion-independent growth and survival.

Project description:The MYC oncogenic transcription factor is acetylated by the p300 and GCN5 histone acetyltransferases. The significance of MYC acetylation and the functions of specific acetylated lysine (AcK) residues have remained unclear. Here, we show that the major p300-acetylated K148(149) and K157(158) sites in human (or mouse) MYC and the main GCN5-acetylated K323 residue are reversibly acetylated in various malignant and nonmalignant cells. Oncogenic overexpression of MYC enhances its acetylation and alters the regulation of site-specific acetylation by proteasome and deacetylase inhibitors. Acetylation of MYC at different K residues differentially affects its stability in a cell type-dependent manner. Lysine-to-arginine substitutions indicate that although none of the AcK residues is required for MYC stimulation of adherent cell proliferation, individual AcK sites have gene-specific functions controlling select MYC-regulated processes in cell adhesion, contact inhibition, apoptosis, and/or metabolism and are required for the malignant cell transformation activity of MYC. Each AcK site is required for anchorage-independent growth of MYC-overexpressing cells in vitro, and both the AcK148(149) and AcK157(158) residues are also important for the tumorigenic activity of MYC transformed cells in vivo. The MYC AcK site-specific signaling pathways identified may offer new avenues for selective therapeutic targeting of MYC oncogenic activities.

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Project description:This SuperSeries is composed of the SubSeries listed below. Refer to individual Series

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STAT3 is constitutively acetylated on lysine 685 residues in chronic lymphocytic leukemia cells.

Project description:Signal transducer and activator of transcription (STAT)-3 might be phosphorylated or acetylated. Unlike the phosphorylation of STAT3, little is known about the acetylation of STAT3 in chronic lymphocytic leukemia (CLL) cells. Because acetylation activates STAT3 transcription, we sought to study the acetylation status of STAT3 in CLL cells. Using Western immunoblotting, immunoprecipitation, and flow cytometry we found that, apart from its constitutive serine phosphorylation, STAT3 is constitutively acetylated on lysine 685 residues. Because the acetyltransferase p300 was found to acetylate STAT3 on lysine 685 residues, we wondered whether p300 acetylates STAT3 in CLL cells. Using Western immunoblotting we detected high levels of p300 protein in CLL but not normal B cells. Transfection of CLL cells with p300 small-interfering (si) RNA downregulated p300 transcripts as well as p300 and acetyl-STAT3 protein levels. In addition, p300 siRNA attenuated STAT3-DNA binding and downregulated mRNA levels of STAT3-regulated genes. Furthermore, transfection of CLL cells with p300-siRNA induced a 3-fold increase in the rate of spontaneous apoptosis. Taken together, our data suggest that in CLL cells STAT3 p300 induces constitutive acetylation and activation of STAT3. Whether inhibition of STAT3 acetylation might provide clinical benefit in patients with CLL remains to be determined.

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