{"doi":"10.1016/j.molcel.2010.09.012","title":"Proteasomal Degradation Is Transcriptionally Controlled by TCF11 via an ERAD-Dependent Feedback Loop","abstract":null,"journal":"Molecular Cell","year":2010,"id":688461,"datarank":0.8941508009434912,"base_score":5.961005339623274,"endowment":5.961005339623274,"self_citation_contribution":0.8941508009434912,"citation_network_contribution":0.0,"self_endowment_contribution":0.8941508009434912,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":387,"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":1798557,"name":"Michael Seeger","orcid":null,"position":1,"is_corresponding":false},{"id":1798558,"name":"Annett Koch","orcid":null,"position":2,"is_corresponding":false},{"id":709964,"name":"Elke Krüger","orcid":"0000-0002-2551-242X","position":3,"is_corresponding":false},{"id":1798556,"name":"Janos Steffen","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Proteasomal Degradation Is Transcriptionally Controlled by TCF11 via an ERAD-Dependent Feedback Loop","abstract":"Coordinated regulation of the ubiquitin-proteasome system (UPS) is crucial for the cell to adjust its protein degradation capacity to changing proteolytic requirements. We have shown previously that mammalian cells upregulate proteasome gene expression in response to proteasome inhibition. Here, we report the identification of the transcription factor TCF11 (long isoform of Nrf1) as a key regulator for 26S proteasome formation in human cells to compensate for reduced proteolytic activity. Under noninducing conditions, TCF11 resides in the endoplasmic reticulum (ER) membrane. There, TCF11 is targeted to ER-associated protein degradation requiring the E3 ubiquitin ligase HRD1 and the AAA ATPase p97. Proteasome inhibitors trigger the accumulation of oxidant-damaged proteins and promote the nuclear translocation of TCF11 from the ER, permitting activation of proteasome gene expression by binding to antioxidant response elements in their promoter regions. Thus, we uncovered the transcriptional control loop regulating human proteasome-dependent protein degradation to counteract proteotoxic stress caused by proteasome inhibition.","is_dataset_classified":null,"base_score":5.961005339623274,"endowment":5.961005339623274,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"20932482","pmcid":null,"openalex_id":"https://openalex.org/W2054827827","authors":[],"funders":[{"funder_name":"Deutsche Forschungsgemeinschaft","grant_id":"SFB740","title":null},{"funder_name":"Deutsche Forschungsgemeinschaft","grant_id":"TPB3","title":null},{"funder_name":"Deutsche Forschungsgemeinschaft","grant_id":"unidentified","title":"unidentified"}],"total_grants":3,"fwci":6.4365,"citation_percentile":0.97508358,"influential_citations":0,"citation_trend":[{"year":2012,"count":19},{"year":2013,"count":17},{"year":2014,"count":25},{"year":2015,"count":28},{"year":2016,"count":24},{"year":2017,"count":21},{"year":2018,"count":27},{"year":2019,"count":34},{"year":2020,"count":32},{"year":2021,"count":31},{"year":2022,"count":15},{"year":2023,"count":28},{"year":2024,"count":29},{"year":2025,"count":26},{"year":2026,"count":15}],"oa_status":"bronze","license":"Elsevier Non-Commercial","oa_locations":[{"url":"http://www.cell.com/article/S1097276510007148/pdf","host_type":"journal"},{"url":"http://www.cell.com/article/S1097276510007148/pdf","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S1097276510007148?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S1097276510007148?httpAccept=text/plain","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.molcel.2010.09.012","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/20932482","host_type":"repository"},{"url":"http://dx.doi.org/10.1016/j.molcel.2010.09.012","host_type":""},{"url":"https://dx.doi.org/10.1016/j.molcel.2010.09.012","host_type":""}],"fields_of_study":["Endoplasmic Reticulum Stress and Disease","Ubiquitin and proteasome pathways","Autophagy in Disease and Therapy","0301 basic medicine","0303 health sciences","03 medical and health sciences","ATPases Associated with Diverse Cellular Activities","Active Transport, Cell Nucleus","Adenosine Triphosphatases","Amino Acid Sequence","Antioxidants","Cell Line","Endoplasmic Reticulum","Endothelial Cells","Feedback, Physiological","Gene Expression Regulation","Homeostasis","Humans","Molecular Sequence Data","NF-E2-Related Factor 1","Nuclear Proteins","Oxidative Stress","Protease Inhibitors","Proteasome Endopeptidase Complex","Proteasome Inhibitors","Protein Processing, Post-Translational","RNA Interference","RNA, Messenger","Response Elements","Transcription, Genetic","Transfection","Ubiquitin","Ubiquitin-Protein Ligases","Ubiquitination"],"mesh_terms":["ATPases Associated with Diverse Cellular Activities","Adenosine Triphosphatases","Amino Acid Sequence","Antioxidants","Cell Line","Endoplasmic Reticulum","Gene Expression Regulation","Homeostasis","Humans","Molecular Sequence Data","Nuclear Proteins","Protease Inhibitors","Protein Processing, Post-Translational","RNA, Messenger","Transcription, Genetic","Transfection","Oxidative Stress","Response Elements","Active Transport, Cell Nucleus","Feedback, Physiological","Ubiquitin","RNA Interference","Endothelial Cells","Ubiquitin-Protein Ligases","Proteasome Endopeptidase Complex","NF-E2-Related Factor 1","Ubiquitination","Proteasome Inhibitors"],"keywords":["Proteasome","Endoplasmic-reticulum-associated protein degradation","Biology","Cell biology","Endoplasmic reticulum","Ubiquitin ligase","Protein degradation","Ubiquitin","Transcription factor","Ubiquitin-conjugating enzyme","Regulator","Degron","Unfolded protein response","Biochemistry","Gene","Adenosine Triphosphatases","Feedback, Physiological","Proteasome Endopeptidase Complex","Molecular Sequence Data","Active Transport, Cell Nucleus","NF-E2-Related Factor 1","Endothelial Cells","Nuclear Proteins","Antioxidants","Cell Line","Oxidative Stress","Gene Expression Regulation","ATPases Associated with Diverse Cellular Activities","Homeostasis","Humans","Protease Inhibitors","Amino Acid Sequence","Molecular Biology","Proteasome Inhibitors","Protein Processing, Post-Translational"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-19T16:26:30.327853Z","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":[]}