Work

The Interplay of Acetylation and Ubiquitination Controls PRMT1 Homeostasis

Year: 2024

Type: preprint

Abstract: PRMT1 plays many important roles in both normal and disease biology, thus understanding it's regulation is crucial. Herein, we report the role of p300-mediated acetylation at K228 in triggering PRMT1 degradation through FBXL17-mediated ubiquitination. Utilizing mass-spectrometry, cellular biochemistry, and genetic code-expansion technologies, we elucidate a crucial mechanism independent of PRMT1 transcript levels. These results underscore the significance of acetylation in governing protein stability and expand our understanding of PRMT1 homeostasis. By detailing the molecular interplay between acetylation and ubiquitination involved in PRMT1 degradation, this work contributes to broader efforts in deciphering post-translational mechanisms that influence protein homeostasis.

Source: bioRxiv (Cold Spring Harbor Laboratory)

DOI: 10.1101/2024.06.18.599616

Authors: Mohd. Altaf Najar, Jenna N. Beyer, Callie E. W. Crawford, George M. Burslem

Institution: University of Pennsylvania

Language: English

Topic: Cancer-related gene regulation

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Institute of General Medical Sciences

Award: Editing Acetylation and Protein Homeostasis

OpenAlex ID: W4399821435

Cites: 55

Cited by: 3

Related to: 10