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Crosstalk Between Acetylation and Ubiquitination Contributes to PRMT1 methyltransferase Homeostasis

GSE304181 Homo sapiens Expression profiling by high throughput sequencing 6 samples Submitted 2026/07/31 Platform GPL20301
Summary
PRMT1 plays pivotal roles in normal and disease biology. Understanding its regulation is crucial for therapeutic targeting. We demonstrate that p300-mediated acetylation of PRMT1 at K228 triggers degradation via FBXL17-dependent ubiquitination at K145. Using mass spectrometry, cellular biochemistry, and genetic code-expansion, we reveal the crosstalk between acetylation and ubiquitination in PRMT1 homeostasis, highlighting mechanisms governing protein stability. This study results in Identification of K228 acetylation and K145 ubiquitination sites on PRMT1, FBXL17 as the E3 ligase mediating PRMT1 ubiquitination and interdependence of p300 acetylation and FBXL17 ubiquitination in PRMT1 degradation. We have used Co-IP MS to look for protein-protein interactions (e.g., PRMT1-FBXL17/p300 complexes), IP-MS to map Acetylation/ubiquitination sites (PRMT1 post-translational modifications) and genetic code-expansion (site-specific incorporation of acetyl-lysine)
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Also filed as BioProject PRJNA1299336 and SRA study SRP605438. Searching any of these in the dataset finder brings you back here.

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