{"doi":"10.1016/j.cellsig.2019.109440","title":"SCFFBXO28-mediated self-ubiquitination of FBXO28 promotes its degradation","abstract":null,"journal":"Cellular Signalling","year":2020,"id":609801,"datarank":0.4943755299006494,"base_score":3.295836866004329,"endowment":3.295836866004329,"self_citation_contribution":0.4943755299006494,"citation_network_contribution":0.0,"self_endowment_contribution":0.4943755299006494,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":26,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":271361,"name":"Liang Liu","orcid":"0000-0003-0568-4264","position":1,"is_corresponding":false},{"id":1289258,"name":"Lihui Li","orcid":null,"position":2,"is_corresponding":false},{"id":273261,"name":"Lijun Jia","orcid":null,"position":3,"is_corresponding":false},{"id":275403,"name":"Lili Cai","orcid":"0000-0003-3260-2367","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"SCFFBXO28-mediated self-ubiquitination of FBXO28 promotes its degradation","abstract":"The F-box protein is the substrate recognition subunit of SCF (SKP1/CUL1/F-box) E3 ubiquitin ligase complex, a multicomponent RING-type E3 ligase involved in the regulation of numerous cellular processes by targeting critical regulatory proteins for ubiquitination. However, whether and how F-box proteins are regulated is largely unknown. Here we report that FBXO28, a poorly characterized F-box protein, is a novel substrate of SCF E3 ligase. Pharmaceutical or genetic inhibition of neddylation pathway that is required for the activation of SCF stabilizes FBXO28 and prolongs its half-life. Meanwhile, FBXO28 is subjected to ubiquitination and cullin1-based SCF complex promotes FBXO28 degradation. Moreover, deletion of F-box domain stabilizes FBXO28 and knockdown of endogenous FBXO28 strongly upregulates exogenous FBXO28 expression. Taken together, these data reveal that SCF<sup>FBXO28</sup> is the E3 ligase responsible for the self-ubiquitination and proteasomal degradation of FBXO28, providing a new clue for the upstream signaling regulation for F-box proteins.","is_dataset_classified":null,"base_score":3.295836866004329,"endowment":3.295836866004329,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"31678254","pmcid":null,"openalex_id":"https://openalex.org/W2988041907","authors":[],"funders":[{"funder_name":"Innovation Program of Shanghai Municipal Education Commission","grant_id":"2019-01-07-00-10-E00056","title":null},{"funder_name":"National Natural Science Foundation of China","grant_id":"81625018","title":null},{"funder_name":"National Thirteenth Five-Year Science and Technology Major Special Project for New Drug and Development","grant_id":"2017ZX09304001","title":null},{"funder_name":"The Chinese Minister of Science and Technology","grant_id":"2016YFA0501800","title":null},{"funder_name":"Shanghai Education Development Foundation","grant_id":"14SG07","title":null},{"funder_name":"Program of Shanghai Academic/Technology Research Leader","grant_id":"18XD1403800","title":null},{"funder_name":"National Natural Science Foundation of China","grant_id":"81572340","title":null},{"funder_name":"National Natural Science Foundation of China","grant_id":"81802743","title":null}],"total_grants":8,"fwci":0.2275,"citation_percentile":0.52234765,"influential_citations":0,"citation_trend":[{"year":2021,"count":2},{"year":2022,"count":1},{"year":2023,"count":4},{"year":2024,"count":14},{"year":2025,"count":3},{"year":2026,"count":2}],"oa_status":"closed","license":"https://www.elsevier.com/legal/tdmrep-license","oa_locations":[{"url":"https://api.elsevier.com/content/article/PII:S0898656819302360?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0898656819302360?httpAccept=text/plain","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.cellsig.2019.109440","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/31678254","host_type":"repository"}],"fields_of_study":["Ubiquitin and proteasome pathways","Protein Degradation and Inhibitors","Peptidase Inhibition and Analysis"],"mesh_terms":["Antineoplastic Agents","Cell Line","Chromatography, Liquid","Cyclopentanes","Enzyme Inhibitors","Humans","Leupeptins","Pyrimidines","Signal Transduction","Transcriptional Activation","Cysteine Proteinase Inhibitors","Proteome","F-Box Proteins","Cullin Proteins","SKP Cullin F-Box Protein Ligases","Proteasome Endopeptidase Complex","Tandem Mass Spectrometry","Ubiquitination"],"keywords":["Ubiquitin ligase","F-box protein","Skp1","Ubiquitin","Neddylation","Cell division control protein 4","Cell biology","Ubiquitin-Protein Ligases","Ubiquitin-conjugating enzyme","Cullin","DNA ligase","Protein degradation","DDB1","Protein subunit","NEDD8","Chemistry","Biology","Biochemistry","DNA","Gene","SCF","Cullin-ring E3 Ubiquitin Ligase","Fbxo28","Self-ubiquitination"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-31T15:41:28.472968Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}