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NAT10 promotes cancer metastasis by modulating p300/CBP activity through chromatin-associated tRNA

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

ORGANISM(S): Mus musculus

PROVIDER: GSE250430 | GEO | 2025/11/17

REPOSITORIES: GEO

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NAT10 promotes cancer metastasis by modulating p300/CBP activity through chromatin-associated tRNA [ChIP-seq]

Project description:Acetylation of proteins and RNA is crucial for development and cancer progression. NAT10 is the sole RNA acetylase responsible for N4-acetylcytidine (ac4C) modification of various RNAs. Our study reveals that NAT10 loss significantly reduces lung metastasis in breast cancer mouse models. NAT10 interacts with a mechanosensitive, metastasis-susceptibility protein complex at the nuclear pore. Mechanistically, NAT10-mediated acetylation of chromatin-associated tRNAs enhances p300/CBP activity. Without NAT10, acetylation of these tRNAs decreases, leading to p300/CBP inactivation and mislocalization. As a result, NAT10 depletion disrupts enhancer organization, altering gene transcription critical for metastasis, including reduced chemokines that recruit myeloid cells and create a less metastasis-prone tumor microenvironment. Our findings highlight the distinct role of NAT10 in acetylated tRNA-dependent regulation of enhancer function in metastatic tumor cells and its impact on tumor-immune interactions influencing metastasis.

2025-11-17 | GSE250428 | GEO

NAT10 promotes cancer metastasis by modulating p300/CBP activity through chromatin-associated tRNA [RNA-seq]

2025-11-17 | GSE250284 | GEO

NAT10 promotes cancer metastasis by modulating p300/CBP activity through chromatin-associated tRNA [RNA-ChIP]

2025-11-17 | GSE280504 | GEO

NAT10 promotes cancer metastasis by modulating p300/CBP activity through chromatin-associated tRNA

Project description:NAT10 promotes cancer metastasis by modulating p300/CBP activity through chromatin-associated tRNA

| PRJNA1054048 | ENA

NAT10 promotes cancer metastasis by modulating p300/CBP activity through chromatin-associated tRNA [RNA-seq]

Project description:NAT10 promotes cancer metastasis by modulating p300/CBP activity through chromatin-associated tRNA [RNA-seq]

| PRJNA1053299 | ENA

NAT10 promotes cancer metastasis by modulating p300/CBP activity through chromatin-associated tRNA [ChIP-seq]

Project description:NAT10 promotes cancer metastasis by modulating p300/CBP activity through chromatin-associated tRNA [ChIP-seq]

| PRJNA1054053 | ENA

NAT10 promotes cancer metastasis by modulating p300/CBP activity through chromatin-associated tRNA [RNA-ChIP]

Project description:NAT10 promotes cancer metastasis by modulating p300/CBP activity through chromatin-associated tRNA [RNA-ChIP]

| PRJNA1178712 | ENA

p300/CBP-associated factor promotes autophagic degradation of δ-catenin through acetylation and decreases prostate cancer tumorigenicity.

Project description:δ-Catenin shares common binding partners with β-catenin. As acetylation and deacetylation regulate β-catenin stability, we searched for histone acetyltransferases (HATs) or histone deacetylases (HDACs) affecting δ-catenin acetylation status and protein levels. We showed that p300/CBP-associated factor (PCAF) directly bound to and acetylated δ-catenin, whereas several class I and class II HDACs reversed this effect. Unlike β-catenin, δ-catenin was downregulated by PCAF-mediated acetylation and upregulated by HDAC-mediated deacetylation. The HDAC inhibitor trichostatin A attenuated HDAC1-mediated δ-catenin upregulation, whereas HAT or autophagy inhibitors, but not proteasome inhibitors, abolished PCAF-mediated δ-catenin downregulation. The results suggested that PCAF-mediated δ-catenin acetylation promotes its autophagic degradation in an Atg5/LC3-dependent manner. Deletions or point mutations identified several lysine residues in different δ-catenin domains involved in PCAF-mediated δ-catenin downregulation. PCAF overexpression in prostate cancer cells markedly reduced δ-catenin levels and suppressed cell growth and motility. PCAF-mediated δ-catenin downregulation inhibited E-cadherin processing and decreased the nuclear distribution of β-catenin, resulting in the suppression of β-catenin/LEF-1-mediated downstream effectors. These data demonstrate that PCAF downregulates δ-catenin by promoting its autophagic degradation and suppresses δ-catenin-mediated oncogenic signals.

| S-EPMC6399259 | biostudies-literature

Modulating the masters: chemical tools to dissect CBP and p300 function.

Project description:Dysregulation of transcription is found in nearly every human disease, and as a result there has been intense interest in developing new therapeutics that target regulators of transcription. CREB binding protein (CBP) and its paralogue p300 are attractive targets due to their function as `master coactivators'. Although inhibitors of several CBP/p300 domains have been identified, the selectivity of many of these compounds has remained underexplored. Here, we review recent successes in the development of chemical tools targeting several CBP/p300 domains with selectivity acceptable for use as chemical probes. Additionally, we highlight recent studies which have used these probes to expand our understanding of interdomain interactions and differential coactivator usage.

| S-EPMC7469456 | biostudies-literature

Dimeric structure of p300/CBP associated factor.

Project description:BACKGROUND:p300/CBP associating factor (PCAF, also known as KAT2B for lysine acetyltransferase 2B) is a catalytic subunit of megadalton metazoan complex ATAC (Ada-Two-A containing complex) for acetylation of histones. However, relatively little is known about the regulation of the enzymatic activity of PCAF. RESULTS:Here we present two dimeric structures of the PCAF acetyltransferase (HAT) domain. These dimerizations are mediated by either four-helical hydrophobic interactions or a ß-sheet extension. Our chemical cross-linking experiments in combined with site-directed mutagenesis demonstrated that the PCAF HAT domain mainly forms a dimer in solution through one of the observed interfaces. The results of maltose binding protein (MBP)-pulldown, co-immunoprecipitation and multiangle static light scattering experiments further indicated that PCAF dimeric state is detectable and may possibly exist in vivo. CONCLUSIONS:Taken together, our structural and biochemical studies indicate that PCAF appears to be a dimer in its functional ATAC complex.

| S-EPMC3897949 | biostudies-literature

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