{"doi":"10.1038/nature05542","title":"A ubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate","abstract":null,"journal":"Nature","year":2007,"id":604682,"datarank":9.761561400701071,"base_score":5.420534999272286,"endowment":5.420534999272286,"self_citation_contribution":0.813080249890843,"citation_network_contribution":8.948481150810228,"self_endowment_contribution":0.813080249890843,"citer_contribution":8.948481150810228,"corpus_percentile":null,"corpus_rank":null,"citation_count":225,"citer_count":200,"citers_with_citation_signal":168,"citers_with_endowment":168,"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":1551538,"name":"Daqi Tu","orcid":null,"position":1,"is_corresponding":false},{"id":1551539,"name":"Axel T. Brunger","orcid":null,"position":2,"is_corresponding":false},{"id":239793,"name":"Yihong Ye","orcid":"0000-0002-9512-7922","position":3,"is_corresponding":false},{"id":717111,"name":"Wei Li","orcid":"0000-0002-7530-4872","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"A ubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate","abstract":"In eukaryotic cells, many short-lived proteins are conjugated with Lys 48-linked ubiquitin chains and degraded by the proteasome. Ubiquitination requires an activating enzyme (E1), a conjugating enzyme (E2) and a ligase (E3). Most ubiquitin ligases use either a HECT (homologous to E6-associated protein C terminus) or a RING (really interesting new gene) domain to catalyse polyubiquitination, but the mechanism of E3 catalysis is poorly defined. Here we dissect this process using mouse Ube2g2 (E2; identical at the amino acid level to human Ube2g2) and human gp78 (E3), an endoplasmic reticulum (ER)-associated conjugating system essential for the degradation of misfolded ER proteins. We demonstrate by expressing recombinant proteins in Escherichia coli that Ube2g2/gp78-mediated polyubiquitination involves preassembly of Lys 48-linked ubiquitin chains at the catalytic cysteine of Ube2g2. The growth of Ube2g2-anchored ubiquitin chains seems to be mediated by an aminolysis-based transfer reaction between two Ube2g2 molecules that each carries a ubiquitin moiety in its active site. Intriguingly, polyubiquitination of a substrate can be achieved by transferring preassembled ubiquitin chains from Ube2g2 to a lysine residue in a substrate.","is_dataset_classified":null,"base_score":5.420534999272286,"endowment":5.420534999272286,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"17310145","pmcid":null,"openalex_id":"https://openalex.org/W2083690210","authors":[],"funders":[{"funder_name":"Intramural NIH HHS","grant_id":"","title":null},{"funder_name":"Intramural NIH HHS","grant_id":"","title":null}],"total_grants":2,"fwci":10.3092,"citation_percentile":0.99024872,"influential_citations":0,"citation_trend":[{"year":2012,"count":18},{"year":2013,"count":15},{"year":2014,"count":20},{"year":2015,"count":11},{"year":2016,"count":9},{"year":2017,"count":7},{"year":2018,"count":9},{"year":2019,"count":8},{"year":2020,"count":7},{"year":2021,"count":3},{"year":2022,"count":5},{"year":2023,"count":1},{"year":2024,"count":5},{"year":2025,"count":6},{"year":2026,"count":3}],"oa_status":"closed","license":"http://www.springer.com/tdm","oa_locations":[{"url":"http://www.nature.com/articles/nature05542.pdf","host_type":"publisher"},{"url":"http://www.nature.com/articles/nature05542","host_type":"publisher"},{"url":"https://doi.org/10.1038/nature05542","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/17310145","host_type":"repository"},{"url":"https://www.nature.com/articles/nature05542","host_type":"repository"}],"fields_of_study":["Ubiquitin and proteasome pathways","Genetics and Neurodevelopmental Disorders","Endoplasmic Reticulum Stress and Disease","Animals","Binding Sites","Catalysis","Humans","Lysine","Mice","Polyubiquitin","Receptors, Autocrine Motility Factor","Receptors, Cytokine","Substrate Specificity","Ubiquitin-Conjugating Enzymes","Ubiquitin-Protein Ligases"],"mesh_terms":["Animals","Binding Sites","Catalysis","Humans","Lysine","Substrate Specificity","Receptors, Cytokine","Polyubiquitin","Ubiquitin-Conjugating Enzymes","Ubiquitin-Protein Ligases","Mice","Receptors, Autocrine Motility Factor"],"keywords":["Ubiquitin","Ubiquitin ligase","Deubiquitinating enzyme","Ubiquitin-conjugating enzyme","Ubiquitin-Protein Ligases","Biochemistry","DNA ligase","Endoplasmic reticulum","Biology","Cell biology","Endoplasmic-reticulum-associated protein degradation","Enzyme","Chemistry","Gene"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-30T00:42:22.018002Z","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":[]}