{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jin B"],"funding":["BLRD VA"],"pagination":["755"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11047997"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(4)"],"pubmed_abstract":["Interleukin-17 (IL-17) is a pro-inflammatory cytokine that participates in innate and adaptive immune responses and plays an important role in host defense, autoimmune diseases, tissue regeneration, metabolic regulation, and tumor progression. Post-translational modifications (PTMs) are crucial for protein function, stability, cellular localization, cellular transduction, and cell death. However, PTMs of IL-17 receptor A (IL-17RA) have not been investigated. Here, we show that human IL-17RA was targeted by F-box and WD repeat domain-containing 11 (FBXW11) for ubiquitination, followed by proteasome-mediated degradation. We used bioinformatics tools and biochemical techniques to determine that FBXW11 ubiquitinated IL-17RA through a lysine 27-linked polyubiquitin chain, targeting IL-17RA for proteasomal degradation. Domain 665-804 of IL-17RA was critical for interaction with FBXW11 and subsequent ubiquitination. Our study demonstrates that FBXW11 regulates IL-17 signaling pathways at the IL-17RA level."],"journal":["Biomedicines"],"pubmed_title":["SCF<sup>FBXW11</sup> Complex Targets Interleukin-17 Receptor A for Ubiquitin-Proteasome-Mediated Degradation."],"pmcid":["PMC11047997"],"funding_grant_id":["I01 BX004158"],"pubmed_authors":["Ge D","You Z","Liu YZ","Jin B","Zhou P","Moududee SA","Wang AR"],"additional_accession":[]},"is_claimable":false,"name":"SCF<sup>FBXW11</sup> Complex Targets Interleukin-17 Receptor A for Ubiquitin-Proteasome-Mediated Degradation.","description":"Interleukin-17 (IL-17) is a pro-inflammatory cytokine that participates in innate and adaptive immune responses and plays an important role in host defense, autoimmune diseases, tissue regeneration, metabolic regulation, and tumor progression. Post-translational modifications (PTMs) are crucial for protein function, stability, cellular localization, cellular transduction, and cell death. However, PTMs of IL-17 receptor A (IL-17RA) have not been investigated. Here, we show that human IL-17RA was targeted by F-box and WD repeat domain-containing 11 (FBXW11) for ubiquitination, followed by proteasome-mediated degradation. We used bioinformatics tools and biochemical techniques to determine that FBXW11 ubiquitinated IL-17RA through a lysine 27-linked polyubiquitin chain, targeting IL-17RA for proteasomal degradation. Domain 665-804 of IL-17RA was critical for interaction with FBXW11 and subsequent ubiquitination. Our study demonstrates that FBXW11 regulates IL-17 signaling pathways at the IL-17RA level.","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Mar","modification":"2026-04-08T15:21:56.073Z","creation":"2026-04-08T04:27:34.054Z"},"accession":"S-EPMC11047997","cross_references":{"pubmed":["38672111"],"doi":["10.3390/biomedicines12040755"]}}