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The 26S proteasome is the catalytic arm of the system that acts downstream to the conjugation machinery. For a long time, it has been considered to be a constitutive multi-subunit proteolytic complex that recognizes in a non-discriminatory manner ubiquitin-marked target substrates with less than a handful of exceptions. However, emerging evidence reveals that the 26S proteasome function is also dynamically regulated by multiple factors, such as subunit composition and synthesis, post-translational modifications, and spatial localization, all of which are tightly regulated by the metabolic and stress states of the cell. Importantly, dysregulation of these newly emerging regulatory mechanisms has pathogenic sequelae. These mechanisms fine-tune proteasome activity and expand its role as an active regulator of protein homeostasis rather than being a passive degradation machinery. Given the rapid expansion of these findings and their impact on our understanding of proteasome biology, an integrated overview of these regulatory mechanisms is timely.<\/jats:p>","DOI":"10.3390\/cells15141247","type":"journal-article","created":{"date-parts":[[2026,7,10]],"date-time":"2026-07-10T09:46:47Z","timestamp":1783676807000},"page":"1247","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Regulation of the 26S Proteasome: From Homeostasis to Stress and Disease"],"prefix":"10.3390","volume":"15","author":[{"given":"Victoria","family":"Cohen-Kaplan","sequence":"first","affiliation":[{"name":"Rappaport-Technion Integrated Center (R-TICC) and the Rappaport Faculty of Medicine and Research Institute, Technion-Israel Institute of Technology, Haifa 3109601, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9184-8944","authenticated-orcid":false,"given":"Aaron","family":"Ciechanover","sequence":"additional","affiliation":[{"name":"Rappaport-Technion Integrated Center (R-TICC) and the Rappaport Faculty of Medicine and Research Institute, Technion-Israel Institute of Technology, Haifa 3109601, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yelena","family":"Kravtsova-Ivantsiv","sequence":"additional","affiliation":[{"name":"Rappaport-Technion Integrated Center (R-TICC) and the Rappaport Faculty of Medicine and Research Institute, Technion-Israel Institute of Technology, Haifa 3109601, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,7,10]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.ajpath.2018.09.004","article-title":"Protein Degradation and the Pathologic Basis of Disease","volume":"189","author":"Hanna","year":"2019","journal-title":"Am. J. Pathol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1016\/j.tibs.2024.06.006","article-title":"UPS-Dependent Strategies of Protein Quality Control Degradation","volume":"49","author":"Hoppe","year":"2024","journal-title":"Trends Biochem. Sci."},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Zou, T., and Lin, Z. (2021). The Involvement of Ubiquitination Machinery in Cell Cycle Regulation and Cancer Progression. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22115754"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"2174","DOI":"10.1002\/1878-0261.70033","article-title":"Ubiquitination of Transcription Factors in Cancer: Unveiling Therapeutic Potential","volume":"19","author":"Kim","year":"2025","journal-title":"Mol. Oncol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1038\/354395a0","article-title":"Generation of P50 Subunit of NF-Kappa B by Processing of P105 through an ATP-Dependent Pathway","volume":"354","author":"Fan","year":"1991","journal-title":"Nature"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1016\/j.tibs.2025.06.007","article-title":"Proteasome-Derived Peptides: Separating the Trash from the Recycling","volume":"50","author":"Brennan","year":"2025","journal-title":"Trends Biochem. Sci."},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Enenkel, C., and Ernst, O.P. (2025). Proteasome Dynamics in Response to Metabolic Changes. Front. Cell Dev. Biol., 13.","DOI":"10.3389\/fcell.2025.1523382"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1469","DOI":"10.1042\/BST20253082","article-title":"Regulation via Compartmentation: Adaptive Localization of the Proteasome under Stress","volume":"53","author":"Ciechanover","year":"2025","journal-title":"Biochem. Soc. Trans."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1146\/annurev.biochem.67.1.425","article-title":"The Ubiquitin System","volume":"67","author":"Hershko","year":"1998","journal-title":"Annu. Rev. Biochem."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1002\/anie.201205656","article-title":"The Lysine48-Based Polyubiquitin Chain Proteasomal Signal: Not a Single Child Anymore","volume":"52","author":"Sommer","year":"2013","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1700027","DOI":"10.1002\/bies.201700027","article-title":"Monoubiquitination Joins Polyubiquitination as an Esteemed Proteasomal Targeting Signal","volume":"39","author":"Livneh","year":"2017","journal-title":"BioEssays"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1074\/mcp.O111.013706","article-title":"A Human Ubiquitin Conjugating Enzyme (E2)-HECT E3 Ligase Structure-Function Screen","volume":"11","author":"Sheng","year":"2012","journal-title":"Mol. Cell. Proteom."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"2167","DOI":"10.1016\/j.cell.2026.01.029","article-title":"The E3-Ome Gene-Centric Compendium Reveals the Human E3 Ligase Landscape","volume":"189","author":"Chua","year":"2026","journal-title":"Cell"},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Zachor-Movshovitz, D., Leushkin, Y., Zittlau, K.I., Ben-Nissan, G., and Sharon, M. (2025). Cleaving Expectations: A Review of Proteasome Functional and Catalytic Diversity. Biomolecules, 15.","DOI":"10.3390\/biom15111524"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1016\/j.tplants.2023.01.013","article-title":"Interplay between Autophagy and Proteasome during Protein Turnover","volume":"28","author":"Raffeiner","year":"2023","journal-title":"Trends Plant Sci."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"4931","DOI":"10.1073\/pnas.78.8.4931","article-title":"The Product of the Lon (capR) Gene in Escherichia Coli Is the ATP-Dependent Protease, Protease La","volume":"78","author":"Chung","year":"1981","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"2400","DOI":"10.1016\/S0021-9258(17)35950-1","article-title":"Ubiquitin-Lysozyme Conjugates. Identification and Characterization of an ATP-Dependent Protease from Rabbit Reticulocyte Lysates","volume":"261","author":"Hough","year":"1986","journal-title":"J. Biol. Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1172","DOI":"10.1111\/j.1471-4159.1980.tb07873.x","article-title":"Cation-Sensitive Neutral Endopeptidase: Isolation and Specificity of the Bovine Pituitary Enzyme","volume":"35","author":"Wilk","year":"1980","journal-title":"J. Neurochem."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"842","DOI":"10.1111\/j.1471-4159.1983.tb08056.x","article-title":"Evidence That Pituitary Cation-Sensitive Neutral Endopeptidase Is a Multicatalytic Protease Complex","volume":"40","author":"Wilk","year":"1983","journal-title":"J. Neurochem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1146\/annurev.biochem.78.081507.101607","article-title":"Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome","volume":"78","author":"Finley","year":"2009","journal-title":"Annu. Rev. Biochem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1012","DOI":"10.1016\/j.cell.2013.04.032","article-title":"Acetylation-Mediated Proteasomal Degradation of Core Histones during DNA Repair and Spermatogenesis","volume":"153","author":"Qian","year":"2013","journal-title":"Cell"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"e2116826119","DOI":"10.1073\/pnas.2116826119","article-title":"Proteasome Complexes Experience Profound Structural and Functional Rearrangements throughout Mammalian Spermatogenesis","volume":"119","author":"Menneteau","year":"2022","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"500","DOI":"10.1038\/sj.emboj.7600059","article-title":"Plasticity in Eucaryotic 20S Proteasome Ring Assembly Revealed by a Subunit Deletion in Yeast","volume":"23","author":"Velichutina","year":"2004","journal-title":"EMBO J."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1038\/s41420-025-02698-0","article-title":"Current Landscape of the Immunoproteasome: Implications for Disease and Therapy","volume":"11","author":"Zou","year":"2025","journal-title":"Cell Death Discov."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1016\/j.cell.2011.12.030","article-title":"Immuno- and Constitutive Proteasome Crystal Structures Reveal Differences in Substrate and Inhibitor Specificity","volume":"148","author":"Huber","year":"2012","journal-title":"Cell"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"6979","DOI":"10.1073\/pnas.1222244110","article-title":"Thymoproteasome Subunit-\u03b25T Generates Peptide-MHC Complexes Specialized for Positive Selection","volume":"110","author":"Xing","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1016\/j.chembiol.2010.05.027","article-title":"Activity-Based Profiling Reveals Reactivity of the Murine Thymoproteasome-Specific Subunit Beta5t","volume":"17","author":"Florea","year":"2010","journal-title":"Chem. Biol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1016\/S0092-8674(00)81603-7","article-title":"A Subcomplex of the Proteasome Regulatory Particle Required for Ubiquitin-Conjugate Degradation and Related to the COP9-Signalosome and eIF3","volume":"94","author":"Glickman","year":"1998","journal-title":"Cell"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"7059","DOI":"10.1016\/S0021-9258(17)37244-7","article-title":"A 26 S Protease Subunit That Binds Ubiquitin Conjugates","volume":"269","author":"Deveraux","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1038\/nature06926","article-title":"Proteasome Subunit Rpn13 Is a Novel Ubiquitin Receptor","volume":"453","author":"Husnjak","year":"2008","journal-title":"Nature"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1038\/ncb845","article-title":"Proteasome Subunit Rpn1 Binds Ubiquitin-like Protein Domains","volume":"4","author":"Elsasser","year":"2002","journal-title":"Nat. Cell Biol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"8055","DOI":"10.1128\/MCB.24.18.8055-8068.2004","article-title":"Sequestosome 1\/P62 Is a Polyubiquitin Chain Binding Protein Involved in Ubiquitin Proteasome Degradation","volume":"24","author":"Seibenhener","year":"2004","journal-title":"Mol. Cell. Biol."},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Fabijan, A., Polis, B., Zawadzka-Fabijan, A., Korabiewska, I., Zakrzewski, K., Nowos\u0142awska, E., and Chojnacki, M. (2024). Domains in Action: Understanding Ddi1\u2019s Diverse Functions in the Ubiquitin-Proteasome System. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms25074080"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1018","DOI":"10.1016\/j.molcel.2009.11.012","article-title":"Together, Rpn10 and Dsk2 Can Serve as a Polyubiquitin Chain-Length Sensor","volume":"36","author":"Zhang","year":"2009","journal-title":"Mol. Cell"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1257","DOI":"10.1016\/j.str.2016.05.018","article-title":"Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome","volume":"24","author":"Chen","year":"2016","journal-title":"Structure"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"100450","DOI":"10.1016\/j.jbc.2021.100450","article-title":"Polyubiquitin and Ubiquitin-like Signals Share Common Recognition Sites on Proteasomal Subunit Rpn1","volume":"296","author":"Boughton","year":"2021","journal-title":"J. Biol. Chem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"jcs259622","DOI":"10.1242\/jcs.259622","article-title":"Chaperone-Mediated Assembly of the Proteasome Core Particle\u2013Recent Developments and Structural Insights","volume":"135","author":"Schnell","year":"2022","journal-title":"J. Cell Sci."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"2403","DOI":"10.1038\/s41594-025-01695-2","article-title":"Structural Landscape of the Degrading 26S Proteasome Reveals Conformation-Specific Binding of TXNL1","volume":"32","author":"Arkinson","year":"2025","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1016\/j.molcel.2015.01.016","article-title":"Structural Basis for the Activation and Inhibition of the UCH37 Deubiquitylase","volume":"57","author":"VanderLinden","year":"2015","journal-title":"Mol. Cell"},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"Ambroggio, X.I., Rees, D.C., and Deshaies, R.J. (2003). JAMM: A Metalloprotease-Like Zinc Site in the Proteasome and Signalosome. PLoS Biol., 2.","DOI":"10.2210\/pdb1r5x\/pdb"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"398","DOI":"10.1038\/nature17433","article-title":"USP14 Deubiquitinates Proteasome-Bound Substrates That Are Ubiquitinated at Multiple Sites","volume":"532","author":"Lee","year":"2016","journal-title":"Nature"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"10725","DOI":"10.1038\/s41467-025-65752-6","article-title":"In-Situ Cross-Linking Mass Spectrometry Reveals Compartment-Specific Proteasomal Interactions and Structural Heterogeneity","volume":"16","author":"Zhao","year":"2025","journal-title":"Nat. Commun."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1096\/fj.10-160895","article-title":"Enhancement of Proteasome Function by PA28\u03b1 Overexpression Protects against Oxidative Stress","volume":"25","author":"Li","year":"2011","journal-title":"FASEB J."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"2857","DOI":"10.1007\/s10571-023-01322-y","article-title":"Inhibition of the Proteasome Regulator PA28 Aggravates Oxidized Protein Overload in the Diabetic Rat Brain","volume":"43","author":"Wu","year":"2023","journal-title":"Cell. Mol. Neurobiol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"e45566","DOI":"10.15252\/embr.201745566","article-title":"DNA Damage-Induced Replication Stress Results in PA200-Proteasome-Mediated Degradation of Acetylated Histones","volume":"19","author":"Mandemaker","year":"2018","journal-title":"EMBO Rep."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1032","DOI":"10.1038\/s41586-025-08615-w","article-title":"Cell-Autonomous Innate Immunity by Proteasome-Derived Defence Peptides","volume":"639","author":"Goldberg","year":"2025","journal-title":"Nature"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1101\/gad.319905","article-title":"A Mechanism of Ubiquitin-Independent Proteasomal Degradation of the Tumor Suppressors P53 and P73","volume":"19","author":"Asher","year":"2005","journal-title":"Genes Dev."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/j.molcel.2012.05.049","article-title":"A Mutually Inhibitory Feedback Loop between the 20S Proteasome and Its Regulator, NQO1","volume":"47","author":"Moscovitz","year":"2012","journal-title":"Mol. Cell"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"6609","DOI":"10.1038\/ncomms7609","article-title":"The Parkinson\u2019s-Associated Protein DJ-1 Regulates the 20S Proteasome","volume":"6","author":"Moscovitz","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1089\/ars.2019.7816","article-title":"Regulation of the 20S Proteasome by a Novel Family of Inhibitory Proteins","volume":"32","author":"Olshina","year":"2020","journal-title":"Antioxid. Redox Signal."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"104862","DOI":"10.1016\/j.jbc.2023.104862","article-title":"High-Resolution Structure of Mammalian PI31\u201320S Proteasome Complex Reveals Mechanism of Proteasome Inhibition","volume":"299","author":"Hsu","year":"2023","journal-title":"J. Biol. Chem."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"15949","DOI":"10.1016\/S0021-9258(18)71571-8","article-title":"Degradation of Ornithine Decarboxylase in Reticulocyte Lysate Is ATP-Dependent but Ubiquitin-Independent","volume":"264","author":"Bercovich","year":"1989","journal-title":"J. Biol. Chem."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"12135","DOI":"10.1074\/jbc.M211802200","article-title":"Ubiquitin-Independent Mechanisms of Mouse Ornithine Decarboxylase Degradation Are Conserved between Mammalian and Fungal Cells","volume":"278","author":"Hoyt","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1038\/360597a0","article-title":"Ornithine Decarboxylase Is Degraded by the 26S Proteasome without Ubiquitination","volume":"360","author":"Murakami","year":"1992","journal-title":"Nature"},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Kors, S., Geijtenbeek, K., Reits, E., and Schipper-Krom, S. (2019). Regulation of Proteasome Activity by (Post-)Transcriptional Mechanisms. Front. Mol. Biosci., 6.","DOI":"10.3389\/fmolb.2019.00048"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.jprot.2015.11.016","article-title":"Biological Significance of Co- and Post-Translational Modifications of the Yeast 26S Proteasome","volume":"134","author":"Hirano","year":"2016","journal-title":"J. Proteom."},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Sokolov, M., Taniguchi, H., and Weber, J.J. (2026). Multilayer Modulation of the Proteasome: New Strategies for Neuroprotection. Front. Mol. Neurosci., 19.","DOI":"10.3389\/fnmol.2026.1748434"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"13246","DOI":"10.1073\/pnas.1805353115","article-title":"Ubiquitin-Dependent Switch during Assembly of the Proteasomal ATPases Mediated by Not4 Ubiquitin Ligase","volume":"115","author":"Fu","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_59","first-page":"E7490","article-title":"P62- and Ubiquitin-Dependent Stress-Induced Autophagy of the Mammalian 26S Proteasome","volume":"113","author":"Livneh","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"12960","DOI":"10.1038\/ncomms12960","article-title":"Structure of Ubiquitylated-Rpn10 Provides Insight into Its Autoregulation Mechanism","volume":"7","author":"Attali","year":"2016","journal-title":"Nat. Commun."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1042\/BJ20150609","article-title":"Rpn10 Monoubiquitination Orchestrates the Association of the Ubiquilin-Type DSK2 Receptor with the Proteasome","volume":"472","author":"Zuin","year":"2015","journal-title":"Biochem. J."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"2461","DOI":"10.1021\/bi3001006","article-title":"Ubiquitylation of Drosophila P54\/Rpn10\/S5a Regulates Its Interaction with the UBA\u2013UBL Polyubiquitin Receptors","volume":"51","author":"Lipinszki","year":"2012","journal-title":"Biochemistry"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1016\/j.molcel.2010.05.001","article-title":"Monoubiquitination of RPN10 Regulates Substrate Recruitment to the Proteasome","volume":"38","author":"Isasa","year":"2010","journal-title":"Mol. Cell"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"3988","DOI":"10.1091\/mbc.e13-11-0697","article-title":"VWA Domain of S5a Restricts the Ability to Bind Ubiquitin and Ubl to the 26S Proteasome","volume":"25","author":"Piterman","year":"2014","journal-title":"Mol. Biol. Cell"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1002\/embj.201386906","article-title":"Autoubiquitination of the 26S Proteasome on Rpn13 Regulates Breakdown of Ubiquitin Conjugates","volume":"33","author":"Besche","year":"2014","journal-title":"EMBO J."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1824","DOI":"10.1091\/mbc.e13-10-0585","article-title":"Autoregulation of the 26S Proteasome by in Situ Ubiquitination","volume":"25","author":"Jacobson","year":"2014","journal-title":"Mol. Biol. Cell"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1002\/jcb.25259","article-title":"Involvement of ALAD-20S Proteasome Complexes in Ubiquitination and Acetylation of Proteasomal A2 Subunits","volume":"117","author":"Schmitt","year":"2016","journal-title":"J. Cell. Biochem."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.bbamcr.2013.03.023","article-title":"Proteasome Dynamics","volume":"1843","author":"Enenkel","year":"2014","journal-title":"Biochim. Biophys. Acta BBA\u2013Mol. Cell Res."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"940","DOI":"10.3390\/biom4040940","article-title":"Nuclear Transport of Yeast Proteasomes","volume":"4","author":"Enenkel","year":"2014","journal-title":"Biomolecules"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"3333","DOI":"10.1016\/j.molcel.2023.08.016","article-title":"Regulation of Nucleo-Cytosolic 26S Proteasome Translocation by Aromatic Amino Acids via mTOR Is Essential for Cell Survival under Stress","volume":"83","author":"Livneh","year":"2023","journal-title":"Mol. Cell"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"387","DOI":"10.3390\/cells4030387","article-title":"Nuclear Import of Yeast Proteasomes","volume":"4","author":"Burcoglu","year":"2015","journal-title":"Cells"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"jcs236158","DOI":"10.1242\/jcs.236158","article-title":"The Sts1 Nuclear Import Adapter Uses a Non-Canonical Bipartite Nuclear Localization Signal and Is Directly Degraded by the Proteasome","volume":"133","author":"Budenholzer","year":"2020","journal-title":"J. Cell Sci."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"2697","DOI":"10.1038\/emboj.2013.192","article-title":"Blm10 Facilitates Nuclear Import of Proteasome Core Particles","volume":"32","author":"Weberruss","year":"2013","journal-title":"EMBO J."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1038\/s41586-021-04035-8","article-title":"AKIRIN2 Controls the Nuclear Import of Proteasomes in Vertebrates","volume":"599","author":"Hinterndorfer","year":"2021","journal-title":"Nature"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1706","DOI":"10.1091\/mbc.e07-07-0637","article-title":"A Novel Role for PA28gamma-Proteasome in Nuclear Speckle Organization and SR Protein Trafficking","volume":"19","author":"Baldin","year":"2008","journal-title":"Mol. Biol. Cell"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"3516","DOI":"10.1093\/emboj\/cdf333","article-title":"PA200, a Nuclear Proteasome Activator Involved in DNA Repair","volume":"21","author":"Ustrell","year":"2002","journal-title":"EMBO J."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"827","DOI":"10.3390\/biom4030827","article-title":"The 26S Proteasome and Initiation of Gene Transcription","volume":"4","author":"Durairaj","year":"2014","journal-title":"Biomolecules"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"5801","DOI":"10.1038\/s41598-020-62697-2","article-title":"Cell Cycle-Dependent Localization of the Proteasome to Chromatin","volume":"10","author":"Kito","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"864","DOI":"10.1016\/j.exger.2007.03.010","article-title":"The Proteasome and Its Role in Nuclear Protein Maintenance","volume":"42","author":"Bader","year":"2007","journal-title":"Exp. Gerontol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/j.biocel.2016.07.019","article-title":"The Ubiquitin-Proteasome System and Autophagy: Coordinated and Independent Activities","volume":"79","author":"Livneh","year":"2016","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"11890","DOI":"10.1093\/nar\/gkaa828","article-title":"PML Nuclear Bodies and Chromatin Dynamics: Catch Me If You Can!","volume":"48","author":"Corpet","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1026","DOI":"10.3390\/biom4041026","article-title":"Functions of the Proteasome on Chromatin","volume":"4","author":"McCann","year":"2014","journal-title":"Biomolecules"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"10350","DOI":"10.1093\/nar\/gkx759","article-title":"Nuclear Speckles: Molecular Organization, Biological Function and Role in Disease","volume":"45","author":"Galganski","year":"2017","journal-title":"Nucleic Acids Res."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/j.semcdb.2023.08.002","article-title":"Proteotoxic Stress and the Ubiquitin Proteasome System","volume":"156","author":"Kandel","year":"2024","journal-title":"Semin. Cell Dev. Biol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1111\/j.1600-0854.2008.00729.x","article-title":"The Recognition and Retrotranslocation of Misfolded Proteins from the Endoplasmic Reticulum","volume":"9","author":"Nakatsukasa","year":"2008","journal-title":"Traffic"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1038\/nature737","article-title":"Deubiquitination of P53 by HAUSP Is an Important Pathway for P53 Stabilization","volume":"416","author":"Li","year":"2002","journal-title":"Nature"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"e2529422123","DOI":"10.1073\/pnas.2529422123","article-title":"Proteasomal Proteolysis in P62 Condensates Directs Tumor Suppression or Growth Depending on Their Subcellular Localization","volume":"123","author":"Luo","year":"2026","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"112701","DOI":"10.1016\/j.celrep.2023.112701","article-title":"ECPAS\/Ecm29-Mediated 26S Proteasome Disassembly Is an Adaptive Response to Glucose Starvation","volume":"42","author":"Choi","year":"2023","journal-title":"Cell Rep."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1016\/j.cell.2025.12.035","article-title":"Metabolically Regulated Proteasome Supramolecular Organization in Situ","volume":"189","author":"Tang","year":"2026","journal-title":"Cell"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"3239","DOI":"10.1074\/jbc.M115.699124","article-title":"Starvation Induces Proteasome Autophagy with Different Pathways for Core and Regulatory Particles","volume":"291","author":"Waite","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"1140","DOI":"10.1016\/S0960-9822(03)00417-2","article-title":"Proteasome Disassembly and Downregulation Is Correlated with Viability during Stationary Phase","volume":"13","author":"Bajorek","year":"2003","journal-title":"Curr. Biol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1007\/s00294-020-01059-x","article-title":"Microautophagy Regulates Proteasome Homeostasis","volume":"66","author":"Li","year":"2020","journal-title":"Curr. Genet."},{"key":"ref_93","doi-asserted-by":"crossref","unstructured":"Li, J., Breker, M., Graham, M., Schuldiner, M., and Hochstrasser, M. (2019). AMPK Regulates ESCRT-Dependent Microautophagy of Proteasomes Concomitant with Proteasome Storage Granule Assembly during Glucose Starvation. PLoS Genet., 15.","DOI":"10.1101\/751420"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1038\/nature21378","article-title":"SZT2 Dictates GATOR Control of mTORC1 Signalling","volume":"543","author":"Peng","year":"2017","journal-title":"Nature"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1038\/nature21423","article-title":"KICSTOR Recruits GATOR1 to the Lysosome and Is Necessary for Nutrients to Regulate mTORC1","volume":"543","author":"Wolfson","year":"2017","journal-title":"Nature"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"1052","DOI":"10.1038\/s41556-018-0148-6","article-title":"A Nutrient-Induced Affinity Switch Controls mTORC1 Activation by Its Rag GTPase-Ragulator Lysosomal Scaffold","volume":"20","author":"Lawrence","year":"2018","journal-title":"Nat. Cell Biol."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.1016\/j.molcel.2015.04.023","article-title":"Autophagic Degradation of the 26S Proteasome Is Mediated by the Dual ATG8\/Ubiquitin Receptor RPN10 in Arabidopsis","volume":"58","author":"Marshall","year":"2015","journal-title":"Mol. Cell"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1126\/science.aab2674","article-title":"Sestrin2 Is a Leucine Sensor for the mTORC1 Pathway","volume":"351","author":"Wolfson","year":"2016","journal-title":"Science"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/j.cell.2016.02.035","article-title":"The CASTOR Proteins Are Arginine Sensors for the mTORC1 Pathway","volume":"165","author":"Chantranupong","year":"2016","journal-title":"Cell"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1126\/science.1257132","article-title":"Lysosomal Amino Acid Transporter SLC38A9 Signals Arginine Sufficiency to mTORC1","volume":"347","author":"Wang","year":"2015","journal-title":"Science"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"1242","DOI":"10.1038\/s41418-024-01370-x","article-title":"Inhibition of Nucleo-Cytoplasmic Proteasome Translocation by the Aromatic Amino Acids or Silencing Sestrin3\u2014Their Sensing Mediator\u2014Is Tumor Suppressive","volume":"31","author":"Livneh","year":"2024","journal-title":"Cell Death Differ."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"e2107321118","DOI":"10.1073\/pnas.2107321118","article-title":"P62-Containing, Proteolytically Active Nuclear Condensates, Increase the Efficiency of the Ubiquitin-Proteasome System","volume":"118","author":"Fu","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"e2414377121","DOI":"10.1073\/pnas.2414377121","article-title":"Nuclear P62 Condensates Stabilize the Promyelocytic Leukemia Nuclear Bodies by Sequestering Their Ubiquitin Ligase RNF4","volume":"121","author":"Fu","year":"2024","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1038\/s41422-018-0017-7","article-title":"Polyubiquitin Chain-Induced P62 Phase Separation Drives Autophagic Cargo Segregation","volume":"28","author":"Sun","year":"2018","journal-title":"Cell Res."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1007\/s43188-026-00349-9","article-title":"The Oncogenic Signalosome: SQSTM1\/P62 as a Master Integrator of Signaling, Metabolism, and Autophagy in Cancer","volume":"42","author":"Choi","year":"2026","journal-title":"Toxicol. Res."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"EMBJ201798308","DOI":"10.15252\/embj.201798308","article-title":"P62 Filaments Capture and Present Ubiquitinated Cargos for Autophagy","volume":"37","author":"Zaffagnini","year":"2018","journal-title":"EMBO J."},{"key":"ref_107","doi-asserted-by":"crossref","unstructured":"Lipskerov, F., Cohen-Kaplan, V., and Ciechanover, A. (2026). Precise Mapping of the Proteasome Interaction Region (PIR) of P62\/SQSTM1: Decoupling Condensate Formation from Proteasome Recruitment. Cells, 15.","DOI":"10.3390\/cells15040335"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"e2310756121","DOI":"10.1073\/pnas.2310756121","article-title":"Proteasome Condensate Formation Is Driven by Multivalent Interactions with Shuttle Factors and Ubiquitin Chains","volume":"121","author":"Waite","year":"2024","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"EBC20253033","DOI":"10.1042\/EBC20253033","article-title":"Role of P62 Nuclear Condensates in Regulating Ubiquitin-Mediated Proteasomal Degradation","volume":"69","author":"Ciechanover","year":"2025","journal-title":"Essays Biochem."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/j.cell.2018.12.035","article-title":"Considerations and Challenges in Studying Liquid-Liquid Phase Separation and Biomolecular Condensates","volume":"176","author":"Alberti","year":"2019","journal-title":"Cell"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1016\/j.jmb.2019.06.026","article-title":"Phase Separation in Regulation of Aggrephagy","volume":"432","author":"Sun","year":"2020","journal-title":"J. Mol. Biol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1038\/s41586-020-1982-9","article-title":"Stress- and Ubiquitylation-Dependent Phase Separation of the Proteasome","volume":"578","author":"Yasuda","year":"2020","journal-title":"Nature"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"8951","DOI":"10.1074\/jbc.M212841200","article-title":"Rad23 Ubiquitin-Associated Domains (UBA) Inhibit 26 S Proteasome-Catalyzed Proteolysis by Sequestering Lysine 48-Linked Polyubiquitin Chains","volume":"278","author":"Raasi","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1038\/s41580-018-0040-z","article-title":"Regulation of Proteasome Assembly and Activity in Health and Disease","volume":"19","author":"Rousseau","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_115","doi-asserted-by":"crossref","unstructured":"Brancolini, C., and Iuliano, L. (2020). Proteotoxic Stress and Cell Death in Cancer Cells. Cancers, 12.","DOI":"10.20944\/preprints202007.0344.v1"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"2158","DOI":"10.1091\/mbc.E20-04-0238","article-title":"Regulation of NRF1, a Master Transcription Factor of Proteasome Genes: Implications for Cancer and Neurodegeneration","volume":"31","author":"Northrop","year":"2020","journal-title":"Mol. Biol. Cell"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"960","DOI":"10.1016\/j.cell.2017.02.004","article-title":"mTOR Signaling in Growth, Metabolism, and Disease","volume":"168","author":"Saxton","year":"2017","journal-title":"Cell"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"2489","DOI":"10.1182\/blood-2007-08-104950","article-title":"Molecular Basis of Bortezomib Resistance: Proteasome Subunit \u03925 (PSMB5) Gene Mutation and Overexpression of PSMB5 Protein","volume":"112","author":"Oerlemans","year":"2008","journal-title":"Blood"},{"key":"ref_119","doi-asserted-by":"crossref","unstructured":"Ho Zhi Guang, M., Kavanagh, E., Dunne, L., Dowling, P., Zhang, L., Lindsay, S., Bazou, D., Goh, C., Hanley, C., and Bianchi, G. (2019). Targeting Proteotoxic Stress in Cancer: A Review of the Role That Protein Quality Control Pathways Play in Oncogenesis. Cancers, 11.","DOI":"10.3390\/cancers11010066"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"1552","DOI":"10.1126\/science.292.5521.1552","article-title":"Impairment of the Ubiquitin-Proteasome System by Protein Aggregation","volume":"292","author":"Bence","year":"2001","journal-title":"Science"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1016\/j.molcel.2004.12.021","article-title":"Global Impairment of the Ubiquitin-Proteasome System by Nuclear or Cytoplasmic Protein Aggregates Precedes Inclusion Body Formation","volume":"17","author":"Bennett","year":"2005","journal-title":"Mol. Cell"},{"key":"ref_122","doi-asserted-by":"crossref","unstructured":"Dantuma, N.P., and Bott, L.C. (2014). The Ubiquitin-Proteasome System in Neurodegenerative Diseases: Precipitating Factor, yet Part of the Solution. Front. Mol. Neurosci., 7.","DOI":"10.3389\/fnmol.2014.00070"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1093\/cvr\/cvp255","article-title":"Stressing the Ubiquitin-Proteasome System","volume":"85","author":"Dantuma","year":"2010","journal-title":"Cardiovasc. Res."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1016\/j.cell.2015.07.047","article-title":"A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation","volume":"162","author":"Patel","year":"2015","journal-title":"Cell"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.cell.2015.09.015","article-title":"Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization","volume":"163","author":"Molliex","year":"2015","journal-title":"Cell"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"588","DOI":"10.1016\/j.molcel.2018.04.007","article-title":"A Liquid to Solid Phase Transition Underlying Pathological Huntingtin Exon1 Aggregation","volume":"70","author":"Peskett","year":"2018","journal-title":"Mol. Cell"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"3734","DOI":"10.1074\/jbc.RA117.000357","article-title":"Profilin Reduces Aggregation and Phase Separation of Huntingtin N-Terminal Fragments by Preferentially Binding to Soluble Monomers and Oligomers","volume":"293","author":"Posey","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_128","doi-asserted-by":"crossref","unstructured":"Bett, J.S., Cook, C., Petrucelli, L., and Bates, G.P. (2009). The Ubiquitin-Proteasome Reporter GFPu Does Not Accumulate in Neurons of the R6\/2 Transgenic Mouse Model of Huntington\u2019s Disease. PLoS ONE, 4.","DOI":"10.1371\/journal.pone.0005128"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"1461","DOI":"10.1016\/S1357-2725(02)00085-7","article-title":"Impairment of Proteasome Structure and Function in Aging","volume":"34","author":"Carrard","year":"2002","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"28026","DOI":"10.1074\/jbc.M301048200","article-title":"Central Role of the Proteasome in Senescence and Survival of Human Fibroblasts: Induction of a Senescence-like Phenotype upon Its Inhibition and Resistance to Stress upon Its Activation","volume":"278","author":"Chondrogianni","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1038\/nrm2630","article-title":"Molecular Mechanisms of Proteasome Assembly","volume":"10","author":"Murata","year":"2009","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1146\/annurev-biochem-060410-150257","article-title":"Molecular Architecture and Assembly of the Eukaryotic Proteasome","volume":"82","author":"Tomko","year":"2013","journal-title":"Annu. Rev. Biochem."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1016\/S0531-5565(00)00136-4","article-title":"Age-Related Alterations of Proteasome Structure and Function in Aging Epidermis","volume":"35","author":"Bulteau","year":"2000","journal-title":"Exp. Gerontol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"B220","DOI":"10.1093\/gerona\/55.5.B220","article-title":"Increase of Oxidatively Modified Protein Is Associated With a Decrease of Proteasome Activity and Content in Aging Epidermal Cells","volume":"55","author":"Petropoulos","year":"2000","journal-title":"J. Gerontol. Ser. A Biol. Sci. Med. Sci."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/S0047-6374(99)00101-3","article-title":"Possible Involvement of Proteasome Inhibition in Aging: Implications for Oxidative Stress","volume":"113","author":"Keller","year":"2000","journal-title":"Mech. Ageing Dev."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1111\/j.1749-6632.2000.tb06643.x","article-title":"Protein Degradation by the Proteasome and Its Implications in Aging","volume":"908","author":"Friguet","year":"2000","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"1250","DOI":"10.1080\/10715760600918142","article-title":"Protein Oxidation and Aging","volume":"40","author":"Stadtman","year":"2006","journal-title":"Free Radic. Res."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"2519","DOI":"10.1016\/j.biocel.2004.04.020","article-title":"Decreased Proteolysis Caused by Protein Aggregates, Inclusion Bodies, Plaques, Lipofuscin, Ceroid, and \u201caggresomes\u201d during Oxidative Stress, Aging, and Disease","volume":"36","author":"Grune","year":"2004","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"1442","DOI":"10.1007\/PL00000787","article-title":"Protein Oxidation and 20S Proteasome-Dependent Proteolysis in Mammalian Cells","volume":"58","author":"Shringarpure","year":"2001","journal-title":"Cell. Mol. Life Sci. 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