{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lai Y"],"funding":["NHLBI NIH HHS","National Institutes of Health"],"pagination":["3578-3587"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5665448"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["130(20)"],"pubmed_abstract":["E3 ubiquitin ligase recognizes its protein substrates via specific molecular signatures for ubiquitin proteasomal degradation. However, the role of acetylation/deacetylation in the process of E3 ubiquitin ligase recognizing its protein substrates is not fully studied. Here, we report that a tandem IK motif in protein arginine methyltransferase 1 (PRMT1) forms an acetyldegron to recruit the F-box/LRR-repeat protein 17 (FBXL17), a component of the SKP1-CUL1-F-box protein (SCF)-type E3 ubiquitin ligase complex. PRMT1 is polyubiquitylated for proteasome degradation with a half-life of approximately 4 h in lung epithelial cells. SCF<sup>Fbxl17</sup> mediates PRMT1 polyubiquitylation at K117. SCF<sup>Fbxl17</sup> specifically binds PRMT1 via a unique motif IKxxxIK. Strikingly, the acetylation/de"],"journal":["Journal of cell science"],"pubmed_title":["Lipopolysaccharide modulates p300 and Sirt1 to promote PRMT1 stability via an SCF<sup>Fbxl17</sup>-recognized acetyldegron."],"pmcid":["PMC5665448"],"funding_grant_id":["R01 grant HL125435","R01 HL125435"],"pubmed_authors":["Lai Y","Li X","Li J","Zou C"],"additional_accession":[]},"is_claimable":false,"name":"Lipopolysaccharide modulates p300 and Sirt1 to promote PRMT1 stability via an SCF<sup>Fbxl17</sup>-recognized acetyldegron.","description":"E3 ubiquitin ligase recognizes its protein substrates via specific molecular signatures for ubiquitin proteasomal degradation. However, the role of acetylation/deacetylation in the process of E3 ubiquitin ligase recognizing its protein substrates is not fully studied. Here, we report that a tandem IK motif in protein arginine methyltransferase 1 (PRMT1) forms an acetyldegron to recruit the F-box/LRR-repeat protein 17 (FBXL17), a component of the SKP1-CUL1-F-box protein (SCF)-type E3 ubiquitin ligase complex. PRMT1 is polyubiquitylated for proteasome degradation with a half-life of approximately 4 h in lung epithelial cells. SCF<sup>Fbxl17</sup> mediates PRMT1 polyubiquitylation at K117. SCF<sup>Fbxl17</sup> specifically binds PRMT1 via a unique motif IKxxxIK. Strikingly, the acetylation/de","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Oct","modification":"2025-06-01T03:54:17.183Z","creation":"2025-06-01T03:54:17.183Z"},"accession":"S-EPMC5665448","cross_references":{"pubmed":["28883095"],"doi":["10.1242/jcs.206904"]}}