{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,29]],"date-time":"2026-08-29T08:15:59Z","timestamp":1787991359121,"version":"build-2784847793"},"reference-count":101,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,8,29]],"date-time":"2026-08-29T00:00:00Z","timestamp":1787961600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,8,29]],"date-time":"2026-08-29T00:00:00Z","timestamp":1787961600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100012166","name":"National Key Research and Development Program of China","doi-asserted-by":"publisher","award":["2024YFA1210700"],"award-info":[{"award-number":["2024YFA1210700"]}],"id":[{"id":"10.13039\/501100012166","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"abstract":"<jats:p>\n                    Disrupted protein homeostasis is a shared characteristic in ageing, obesity\u2010induced lipotoxicity and neurodegenerative diseases. The accumulation of misfolded or unfolded proteins within the cell triggers endoplasmic reticulum (ER) stress. In response, the unfolded protein response (UPR) and ER\u2010associated degradation (ERAD) pathways are activated. A key mechanism to alleviate intracellular protein aggregation involves ubiquitination of substrates and their subsequent degradation by the proteasome. The ubiquitin\u2013proteasome system (UPS) is indispensable for cellular protein quality control, and its dysfunction contributes to various proteopathies. However, the crosstalk between the proteasome subunit Rpt3 and the Ire1\u2010Hac1 pathway appears to be rarely reported. In\n                    <jats:italic>Saccharomyces cerevisiae<\/jats:italic>\n                    , growth curve and spotting assay demonstrated that overexpression of Rpt3 reduced the sensitivity of\n                    <jats:italic>ire1<\/jats:italic>\n                    \u0394 or\n                    <jats:italic>hac1<\/jats:italic>\n                    \u0394 to ER stressors. The growth\u2010promoting effect of Rpt3 is not a common feature of the BASE subunits, as overexpression of Rpt6 failed to rescue the growth inhibition. Deletion of\n                    <jats:italic>hac1<\/jats:italic>\n                    resulted in stoichiometric imbalance among proteasomal subunits, which may be key for Rpt3\u2010mediated rescue of\n                    <jats:italic>hac1<\/jats:italic>\n                    \u0394 growth, as deletion of the proteasome transcriptional factor Rpn4 impedes Rpt3 from restoring the growth of\n                    <jats:italic>hac1<\/jats:italic>\n                    \u0394 from ER stress. Overexpression of Rpt3 enhanced proteasome assembly and activity, reducing intracellular ubiquitin levels in\n                    <jats:italic>hac1<\/jats:italic>\n                    \u0394. Moreover, Rpt3 increased the protein level of Hac1, and its alleviation of proteotoxic stress was dependent on the collaboration of ubiquitinating enzymes and chaperones. Western blot and proteasome activity assay in human cells confirmed the cross\u2010species conservation of Rpt3 function. These results highlight a dual role for Rpt3 in proteostasis: beyond enhancing proteasomal activity, Rpt3 upregulates Hac1 protein abundance, thereby ensuring proteostasis maintenance.\n                  <\/jats:p>","DOI":"10.1111\/febs.70714","type":"journal-article","created":{"date-parts":[[2026,8,29]],"date-time":"2026-08-29T07:15:41Z","timestamp":1787987741000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["The dual role of Rpt3 in protecting cells from proteotoxic damage"],"prefix":"10.1111","author":[{"given":"Ziting","family":"Zhu","sequence":"first","affiliation":[{"name":"State Key Laboratory of Bioreactor Engineering East China University of Science and Technology  Shanghai China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiao","family":"Feng","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Bioreactor Engineering East China University of Science and Technology  Shanghai China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Boyi","family":"Song","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Bioreactor Engineering East China University of Science and Technology  Shanghai China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hongzhen","family":"Zhu","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Bioreactor Engineering East China University of Science and Technology  Shanghai China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chunyi","family":"Lv","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Bioreactor Engineering East China University of Science and Technology  Shanghai China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Qiaoqiao","family":"Zheng","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Bioreactor Engineering East China University of Science and Technology  Shanghai China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Siyu","family":"Pan","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Bioreactor Engineering East China University of Science and Technology  Shanghai China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zheyu","family":"Fan","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Bioreactor Engineering East China University of Science and Technology  Shanghai China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhiwei","family":"Huang","sequence":"additional","affiliation":[{"name":"College of Biological Science and Medical Engineering Donghua University  Shanghai China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6904-2802","authenticated-orcid":false,"given":"Ping","family":"Shi","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Bioreactor Engineering East China University of Science and Technology  Shanghai China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,8,29]]},"reference":[{"key":"e_1_2_10_2_1","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1038\/s12276-021-00560-8","article-title":"The aftermath of the interplay between the endoplasmic reticulum stress response and redox signaling","volume":"53","author":"Bhattarai KR","year":"2021","journal-title":"Exp Mol Med"},{"key":"e_1_2_10_3_1","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/S0092-8674(01)00505-0","article-title":"Block of HAC1 mRNA translation by long\u2010range base pairing is released by cytoplasmic splicing upon induction of the unfolded protein response","volume":"107","author":"R\u00fcegsegger U","year":"2001","journal-title":"Cell"},{"key":"e_1_2_10_4_1","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1038\/415092a","article-title":"IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP\u20101 mRNA","volume":"415","author":"Calfon M","year":"2002","journal-title":"Nature"},{"key":"e_1_2_10_5_1","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.1016\/S0092-8674(00)80369-4","article-title":"The transmembrane kinase Ire1p is a site\u2010specific endonuclease that initiates mRNA splicing in the unfolded protein response","volume":"90","author":"Sidrauski C","year":"1997","journal-title":"Cell"},{"key":"e_1_2_10_6_1","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1016\/S0092-8674(00)81360-4","article-title":"A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response","volume":"87","author":"Cox JS","year":"1996","journal-title":"Cell"},{"key":"e_1_2_10_7_1","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.74342","article-title":"Endoplasmic reticulum stress activates human IRE1alpha through reversible assembly of inactive dimers into small oligomers","volume":"11","author":"Belyy V","year":"2022","journal-title":"elife"},{"key":"e_1_2_10_8_1","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a041247","article-title":"Endoplasmic reticulum\u2010associated protein degradation","volume":"14","author":"Krshnan L","year":"2022","journal-title":"Cold Spring Harb Perspect Biol"},{"key":"e_1_2_10_9_1","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1038\/nature23314","article-title":"Cryo\u2010EM structure of the protein\u2010conducting ERAD channel Hrd1 in complex with Hrd3","volume":"548","author":"Schoebel S","year":"2017","journal-title":"Nature"},{"key":"e_1_2_10_10_1","doi-asserted-by":"crossref","DOI":"10.1126\/science.aaz2449","article-title":"Structural basis of ER\u2010associated protein degradation mediated by the Hrd1 ubiquitin ligase complex","volume":"368","author":"Wu X","year":"2020","journal-title":"Science"},{"key":"e_1_2_10_11_1","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-024-46409-2","article-title":"Substrate recognition mechanism of the endoplasmic reticulum\u2010associated ubiquitin ligase Doa10","volume":"15","author":"Wu K","year":"2024","journal-title":"Nat Commun"},{"key":"e_1_2_10_12_1","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/j.semcdb.2018.09.013","article-title":"Ubiquitin\u2010dependent protein degradation at the endoplasmic reticulum and nuclear envelope","volume":"93","author":"Mehrtash AB","year":"2019","journal-title":"Semin Cell Dev Biol"},{"key":"e_1_2_10_13_1","doi-asserted-by":"crossref","first-page":"1086","DOI":"10.1126\/science.1209235","article-title":"Road to ruin: targeting proteins for degradation in the endoplasmic reticulum","volume":"334","author":"Smith MH","year":"2011","journal-title":"Science"},{"key":"e_1_2_10_14_1","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1038\/ncb1298","article-title":"Ubx2 links the Cdc48 complex to ER\u2010associated protein degradation","volume":"7","author":"Neuber O","year":"2005","journal-title":"Nat Cell Biol"},{"key":"e_1_2_10_15_1","doi-asserted-by":"crossref","first-page":"999","DOI":"10.1038\/ncb1299","article-title":"Membrane\u2010bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER\u2010associated protein degradation","volume":"7","author":"Schuberth C","year":"2005","journal-title":"Nat Cell Biol"},{"key":"e_1_2_10_16_1","first-page":"147","article-title":"Protein quality control of the endoplasmic reticulum and ubiquitin\u2013proteasome triggered degradation of aberrant proteins: yeast pioneers the path","volume":"69","author":"Strasser R","year":"2018","journal-title":"Annu Rev Plant Biol"},{"key":"e_1_2_10_17_1","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1038\/s41580-023-00633-8","article-title":"Mechanisms of substrate processing during ER\u2010associated protein degradation","volume":"24","author":"Christianson JC","year":"2023","journal-title":"Nat Rev Mol Cell Biol"},{"key":"e_1_2_10_18_1","doi-asserted-by":"crossref","first-page":"17442","DOI":"10.1074\/jbc.270.29.17442","article-title":"A proteolytic pathway that recognizes ubiquitin as a degradation signal *","volume":"270","author":"Johnson ES","year":"1995","journal-title":"J Biol Chem"},{"key":"e_1_2_10_19_1","doi-asserted-by":"crossref","first-page":"4313","DOI":"10.1038\/s41467-025-59569-6","article-title":"Structural visualization of HECT\u2010type E3 ligase Ufd4 accepting and transferring ubiquitin to form K29\/K48\u2010branched polyubiquitination","volume":"16","author":"Wu XW","year":"2025","journal-title":"Nat Commun"},{"key":"e_1_2_10_20_1","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.cell.2004.11.013","article-title":"A series of ubiquitin binding factors connects CDC48\/p97 to substrate multiubiquitylation and proteasomal targeting","volume":"120","author":"Richly H","year":"2005","journal-title":"Cell"},{"key":"e_1_2_10_21_1","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms14274","article-title":"Ufd2p synthesizes branched ubiquitin chains to promote the degradation of substrates modified with atypical chains","volume":"8","author":"Liu C","year":"2017","journal-title":"Nat Commun"},{"key":"e_1_2_10_22_1","doi-asserted-by":"crossref","first-page":"20390","DOI":"10.1074\/jbc.M110.112532","article-title":"The yeast E4 ubiquitin ligase Ufd2 interacts with the ubiquitin\u2010like domains of Rad23 and Dsk2 via a novel and distinct ubiquitin\u2010like binding domain","volume":"285","author":"H\u00e4nzelmann P","year":"2010","journal-title":"J Biol Chem"},{"key":"e_1_2_10_23_1","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1038\/s41589-025-01985-2","article-title":"Structural basis for E4 enzyme Ufd2\u2010catalyzed K48\/K29 branched ubiquitin chains","volume":"22","author":"Tong ZB","year":"2025","journal-title":"Nat Chem Biol"},{"key":"e_1_2_10_24_1","doi-asserted-by":"crossref","first-page":"1528","DOI":"10.1128\/MCB.00962-10","article-title":"Cellular functions of Ufd2 and Ufd3 in proteasomal protein degradation depend on Cdc48 binding","volume":"31","author":"B\u00f6hm S","year":"2011","journal-title":"Mol Cell Biol"},{"key":"e_1_2_10_25_1","doi-asserted-by":"crossref","first-page":"16197","DOI":"10.1073\/pnas.0908321106","article-title":"An armadillo motif in Ufd3 interacts with Cdc48 and is involved in ubiquitin homeostasis and protein degradation","volume":"106","author":"Zhao G","year":"2009","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_2_10_26_1","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1038\/cr.2016.86","article-title":"The life cycle of the 26S proteasome: from birth, through regulation and function, and onto its death","volume":"26","author":"Livneh I","year":"2016","journal-title":"Cell Res"},{"key":"e_1_2_10_27_1","doi-asserted-by":"crossref","first-page":"2642","DOI":"10.1073\/pnas.1601561113","article-title":"Structure of an endogenous yeast 26S proteasome reveals two major conformational states","volume":"113","author":"Luan B","year":"2016","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_2_10_28_1","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-018-03785-w","article-title":"Structural mechanism for nucleotide\u2010driven remodeling of the AAA\u2010ATPase unfoldase in the activated human 26S proteasome","volume":"9","author":"Zhu YA","year":"2018","journal-title":"Nat Commun"},{"key":"e_1_2_10_29_1","doi-asserted-by":"crossref","DOI":"10.1126\/science.aav0725","article-title":"Substrate\u2010engaged 26S proteasome structures reveal mechanisms for ATP\u2010hydrolysis\u2010driven translocation","volume":"362","author":"Pe\u00f1a AH","year":"2018","journal-title":"Science"},{"key":"e_1_2_10_30_1","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1016\/j.molcel.2007.06.033","article-title":"Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry","volume":"27","author":"Smith DM","year":"2007","journal-title":"Mol Cell"},{"key":"e_1_2_10_31_1","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1038\/s42003-023-05082-9","article-title":"Minimal mechanistic component of HbYX\u2010dependent proteasome activation that reverses impairment by neurodegenerative\u2010associated oligomers","volume":"6","author":"Chuah JJY","year":"2023","journal-title":"Commun Biol"},{"key":"e_1_2_10_32_1","doi-asserted-by":"crossref","first-page":"1301","DOI":"10.1016\/j.celrep.2018.07.004","article-title":"Expanded coverage of the 26S proteasome conformational landscape reveals mechanisms of peptidase gating","volume":"24","author":"Eisele MR","year":"2018","journal-title":"Cell Rep"},{"key":"e_1_2_10_33_1","doi-asserted-by":"crossref","first-page":"1150","DOI":"10.1016\/j.molcel.2019.01.018","article-title":"Structural snapshots of 26S proteasome reveal Tetraubiquitin\u2010induced conformations","volume":"73","author":"Ding Z","year":"2019","journal-title":"Mol Cell"},{"key":"e_1_2_10_34_1","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2020.107680","article-title":"Chaperone\u2010mediated protein disaggregation triggers proteolytic clearance of intra\u2010nuclear protein inclusions","volume":"31","author":"Brave F","year":"2020","journal-title":"Cell Rep"},{"key":"e_1_2_10_35_1","doi-asserted-by":"crossref","DOI":"10.3390\/cells10113075","article-title":"Conserved mitotic phosphorylation of a proteasome subunit regulates cell proliferation","volume":"10","author":"Duan J","year":"2021","journal-title":"Cells"},{"key":"e_1_2_10_36_1","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1038\/s41418-020-00648-0","article-title":"Ubiquitin signaling in cell cycle control and tumorigenesis","volume":"28","author":"Dang F","year":"2021","journal-title":"Cell Death Differ"},{"key":"e_1_2_10_37_1","doi-asserted-by":"crossref","first-page":"1032","DOI":"10.1038\/s41586-025-08615-w","article-title":"Cell\u2010autonomous innate immunity by proteasome\u2010derived defence peptides","volume":"639","author":"Goldberg K","year":"2025","journal-title":"Nature"},{"key":"e_1_2_10_38_1","first-page":"629","article-title":"The proteasome regulator PSME4 modulates proteasome activity and antigen diversity to abrogate antitumor immunity in NSCLC","volume":"4","author":"Javitt A","year":"2023","journal-title":"Nat Can"},{"key":"e_1_2_10_39_1","doi-asserted-by":"crossref","first-page":"1894","DOI":"10.1016\/j.molcel.2025.04.025","article-title":"Proteasome: an antibiotic arsenal in anti\u2010bacterial innate immunity","volume":"85","author":"Zheng Y","year":"2025","journal-title":"Mol Cell"},{"key":"e_1_2_10_40_1","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2025.116041","article-title":"19S proteasome loss regulates mitotic spindle assembly through a ubiquitin\u2010independent degradation mechanism","volume":"44","author":"Marescal O","year":"2025","journal-title":"Cell Rep"},{"key":"e_1_2_10_41_1","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.adj4605","article-title":"Lipid\u2010anchored proteasomes control membrane protein homeostasis","volume":"9","author":"Zhang R","year":"2023","journal-title":"Sci Adv"},{"key":"e_1_2_10_42_1","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1038\/nsmb.3389","article-title":"A mammalian nervous\u2010system\u2010specific plasma membrane proteasome complex that modulates neuronal function","volume":"24","author":"Ramachandran KV","year":"2017","journal-title":"Nat Struct Mol Biol"},{"key":"e_1_2_10_43_1","doi-asserted-by":"crossref","first-page":"24748","DOI":"10.1073\/pnas.1911622116","article-title":"Contribution of proteasome\u2010catalyzed peptide cis\u2010splicing to viral targeting by CD8(+) T\u00a0cells in HIV\u20101 infection","volume":"116","author":"Paes W","year":"2019","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_2_10_44_1","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1126\/science.aaf4384","article-title":"A large fraction of HLA class I ligands are proteasome\u2010generated spliced peptides","volume":"354","author":"Liepe J","year":"2016","journal-title":"Science"},{"key":"e_1_2_10_45_1","doi-asserted-by":"crossref","first-page":"14220","DOI":"10.1073\/pnas.2003277117","article-title":"cGMP via PKG activates 26S proteasomes and enhances degradation of proteins, including ones that cause neurodegenerative diseases","volume":"117","author":"VerPlank JJS","year":"2020","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_2_10_46_1","doi-asserted-by":"crossref","first-page":"4372","DOI":"10.1093\/brain\/awaf222","article-title":"Early proteasome downregulation and dysfunction drive proteostasis failure in Alzheimer's disease","volume":"148","author":"Jiang S","year":"2025","journal-title":"Brain"},{"key":"e_1_2_10_47_1","doi-asserted-by":"crossref","first-page":"7166","DOI":"10.1074\/jbc.M705893200","article-title":"A proteasomal ATPase contributes to dislocation of endoplasmic reticulum\u2010associated degradation (ERAD) substrates","volume":"283","author":"Lipson C","year":"2008","journal-title":"J Biol Chem"},{"key":"e_1_2_10_48_1","doi-asserted-by":"crossref","DOI":"10.3389\/fnmol.2023.1298560","article-title":"Differential expression of PSMC4, SKP1, and HSPA8 in Parkinson's disease: insights from a Mexican mestizo population","volume":"16","author":"Salas\u2010Leal AC","year":"2023","journal-title":"Front Mol Neurosci"},{"key":"e_1_2_10_49_1","doi-asserted-by":"crossref","DOI":"10.1186\/1750-1326-7-26","article-title":"A molecular signature in blood identifies early Parkinson's disease","volume":"7","author":"Molochnikov L","year":"2012","journal-title":"Mol Neurodegener"},{"key":"e_1_2_10_50_1","doi-asserted-by":"crossref","first-page":"3500","DOI":"10.1016\/j.jmb.2017.05.027","article-title":"Proteasome structure and assembly","volume":"429","author":"Budenholzer L","year":"2017","journal-title":"J Mol Biol"},{"key":"e_1_2_10_51_1","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1038\/nature18943","article-title":"An evolutionarily conserved pathway controls proteasome homeostasis","volume":"536","author":"Rousseau A","year":"2016","journal-title":"Nature"},{"key":"e_1_2_10_52_1","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1016\/S1097-2765(02)00638-X","article-title":"Multiple associated proteins regulate proteasome structure and function","volume":"10","author":"Leggett DS","year":"2002","journal-title":"Mol Cell"},{"key":"e_1_2_10_53_1","doi-asserted-by":"crossref","first-page":"879","DOI":"10.1016\/j.molcel.2010.06.016","article-title":"Ecm29 fulfils quality control functions in proteasome assembly","volume":"38","author":"Lehmann A","year":"2010","journal-title":"Mol Cell"},{"key":"e_1_2_10_54_1","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1016\/j.molcel.2014.06.017","article-title":"An inducible chaperone adapts proteasome assembly to stress","volume":"55","author":"Hanssum A","year":"2014","journal-title":"Mol Cell"},{"key":"e_1_2_10_55_1","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1083\/jcb.201106037","article-title":"Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae","volume":"195","author":"Specht S","year":"2011","journal-title":"J Cell Biol"},{"key":"e_1_2_10_56_1","doi-asserted-by":"crossref","first-page":"1269","DOI":"10.1083\/jcb.201708116","article-title":"A prion\u2010like domain in Hsp42 drives chaperone\u2010facilitated aggregation of misfolded proteins","volume":"217","author":"Grousl T","year":"2018","journal-title":"J Cell Biol"},{"key":"e_1_2_10_57_1","doi-asserted-by":"crossref","first-page":"638","DOI":"10.1038\/sj.emboj.7600080","article-title":"Hsp42 is the general small heat shock protein in the cytosol of","volume":"23","author":"Haslbeck M","year":"2004","journal-title":"EMBO J"},{"key":"e_1_2_10_58_1","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1038\/nrm2199","article-title":"Signal integration in the endoplasmic reticulum unfolded protein response","volume":"8","author":"Ron D","year":"2007","journal-title":"Nat Rev Mol Cell Biol"},{"key":"e_1_2_10_59_1","doi-asserted-by":"crossref","DOI":"10.3390\/cells9040890","article-title":"Overexpression of GRP78\/BiP in P\u2010glycoprotein\u2010positive L1210 cells is responsible for altered response of cells to Tunicamycin as a stressor of the endoplasmic reticulum","volume":"9","author":"Seres M","year":"2020","journal-title":"Cells\u2010Basel"},{"key":"e_1_2_10_60_1","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/S0092-8674(00)80835-1","article-title":"Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER\u2010associated degradation","volume":"101","author":"Travers KJ","year":"2000","journal-title":"Cell"},{"key":"e_1_2_10_61_1","doi-asserted-by":"crossref","first-page":"15271","DOI":"10.1073\/pnas.1304928110","article-title":"Previously unknown role for the ubiquitin ligase Ubr1 in endoplasmic reticulum\u2010associated protein degradation","volume":"110","author":"Stolz A","year":"2013","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_2_10_62_1","doi-asserted-by":"crossref","first-page":"12046","DOI":"10.1016\/S0021-9258(19)50306-4","article-title":"N\u2010recognin\/Ubc2 interactions in the N\u2010end rule pathway","volume":"268","author":"Madura K","year":"1993","journal-title":"J Biol Chem"},{"key":"e_1_2_10_63_1","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.67659","article-title":"High and stable ATP levels prevent aberrant intracellular protein aggregation in yeast","volume":"11","author":"Takaine M","year":"2022","journal-title":"elife"},{"key":"e_1_2_10_64_1","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.molcel.2006.08.025","article-title":"ATP binding and ATP hydrolysis play distinct roles in the function of 26S proteasome","volume":"24","author":"Liu CW","year":"2006","journal-title":"Mol Cell"},{"key":"e_1_2_10_65_1","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1146\/annurev-biochem-062917-011931","article-title":"Structure and function of the 26S proteasome","volume":"87","author":"Bard JAM","year":"2018","journal-title":"Annu Rev Biochem"},{"key":"e_1_2_10_66_1","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1146\/annurev.bi.65.070196.004101","article-title":"Structure and functions of the 20S and 26S proteasomes","volume":"65","author":"Coux O","year":"1996","journal-title":"Annu Rev Biochem"},{"key":"e_1_2_10_67_1","doi-asserted-by":"crossref","DOI":"10.1016\/j.arr.2020.101078","article-title":"Ubiquitin biology in neurodegenerative disorders: from impairment to therapeutic strategies","volume":"61","author":"Kumar D","year":"2020","journal-title":"Ageing Res Rev"},{"key":"e_1_2_10_68_1","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1016\/j.tcb.2024.10.003","article-title":"Central role of the ER proteostasis network in healthy aging","volume":"35","author":"Hetz C","year":"2025","journal-title":"Trends Cell Biol"},{"key":"e_1_2_10_69_1","doi-asserted-by":"crossref","first-page":"39523","DOI":"10.1074\/jbc.M110.153627","article-title":"The C terminus of Rpt3, an ATPase subunit of PA700 (19 S) regulatory complex, is essential for 26 S proteasome assembly but not for activation","volume":"285","author":"Kumar B","year":"2010","journal-title":"J Biol Chem"},{"key":"e_1_2_10_70_1","doi-asserted-by":"crossref","first-page":"1143","DOI":"10.1016\/S1097-2765(01)00274-X","article-title":"The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release","volume":"7","author":"K\u00f6hler A","year":"2001","journal-title":"Mol Cell"},{"key":"e_1_2_10_71_1","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1016\/S0076-6879(05)98030-0","article-title":"Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates","volume":"398","author":"Kisselev AF","year":"2005","journal-title":"Methods Enzymol"},{"key":"e_1_2_10_72_1","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-020-76239-3","article-title":"Ribosomal protein S7 ubiquitination during ER stress in yeast is associated with selective mRNA translation and stress outcome","volume":"10","author":"Matsuki Y","year":"2020","journal-title":"Sci Rep"},{"key":"e_1_2_10_73_1","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-023-38161-w","article-title":"Molecular basis for recognition and deubiquitination of 40S ribosomes by Otu2","volume":"14","author":"Ikeuchi K","year":"2023","journal-title":"Nat Commun"},{"key":"e_1_2_10_74_1","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-025-57360-1","article-title":"Crucial roles of Grr1 in splicing and translation of HAC1 mRNA upon unfolded stress response","volume":"16","author":"Sato N","year":"2025","journal-title":"Nat Commun"},{"key":"e_1_2_10_75_1","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1371\/journal.pgen.1002862","article-title":"The yeast Rab GTPase Ypt1 modulates unfolded protein response dynamics by regulating the stability of RNA","volume":"8","author":"Tsvetanova NG","year":"2012","journal-title":"PLoS Genet"},{"key":"e_1_2_10_76_1","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1080\/10985549.2023.2227016","article-title":"The sequential recruitments of Rab\u2010GTPase Ypt1p and the NNS complex onto pre\u2010mRNA promote its nuclear degradation in Baker's yeast","volume":"43","author":"Paira S","year":"2023","journal-title":"Mol Cell Biol"},{"key":"e_1_2_10_77_1","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.3003086","article-title":"A nonenzymatic dependency on inositol\u2010requiring enzyme 1 controls cancer cell cycle progression and tumor growth","volume":"23","author":"Zuazo\u2010Gaztelu I","year":"2025","journal-title":"PLoS Biol"},{"key":"e_1_2_10_78_1","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2024.107169","article-title":"Exploring the IRE1 interactome: from canonical signaling functions to unexpected roles","volume":"300","author":"Le Goupil S","year":"2024","journal-title":"J Biol Chem"},{"key":"e_1_2_10_79_1","doi-asserted-by":"crossref","first-page":"850","DOI":"10.1016\/j.celrep.2014.09.016","article-title":"Ire1 has distinct catalytic mechanisms for XBP1\/HAC1 splicing and RIDD","volume":"9","author":"Tam AB","year":"2014","journal-title":"Cell Rep"},{"key":"e_1_2_10_80_1","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1126\/science.1129631","article-title":"Decay of endoplasmic reticulum\u2010localized mRNAs during the unfolded protein response","volume":"313","author":"Hollien J","year":"2006","journal-title":"Science"},{"key":"e_1_2_10_81_1","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.201909165","article-title":"Stress sensor Ire1 deploys a divergent transcriptional program in response to lipid bilayer stress","volume":"219","author":"Ho N","year":"2020","journal-title":"J Cell Biol"},{"key":"e_1_2_10_82_1","doi-asserted-by":"crossref","first-page":"3520","DOI":"10.1091\/mbc.e11-04-0295","article-title":"Membrane aberrancy and unfolded proteins activate the endoplasmic reticulum stress sensor Ire1 in different ways","volume":"22","author":"Promlek T","year":"2011","journal-title":"Mol Biol Cell"},{"key":"e_1_2_10_83_1","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1038\/s41556-019-0329-y","article-title":"Non\u2010canonical function of IRE1alpha determines mitochondria\u2010associated endoplasmic reticulum composition to control calcium transfer and bioenergetics","volume":"21","author":"Carreras\u2010Sureda A","year":"2019","journal-title":"Nat Cell Biol"},{"key":"e_1_2_10_84_1","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2021.109717","article-title":"Substrate ubiquitination retains misfolded membrane proteins in the endoplasmic reticulum for degradation","volume":"36","author":"Sun Z","year":"2021","journal-title":"Cell Rep"},{"key":"e_1_2_10_85_1","doi-asserted-by":"crossref","first-page":"5934","DOI":"10.1073\/pnas.1603079113","article-title":"Direct and essential function for Hrd3 in ER\u2010associated degradation","volume":"113","author":"Vashistha N","year":"2016","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_2_10_86_1","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1126\/science.1255638","article-title":"Quality control of inner nuclear membrane proteins by the Asi complex","volume":"346","author":"Foresti O","year":"2014","journal-title":"Science"},{"key":"e_1_2_10_87_1","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1126\/science.aaf6846","article-title":"ATP as a biological hydrotrope","volume":"356","author":"Patel A","year":"2017","journal-title":"Science"},{"key":"e_1_2_10_88_1","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-020-19104-1","article-title":"ATP hydrolysis by yeast Hsp104 determines protein aggregate dissolution and size in vivo","volume":"11","author":"Sathyanarayanan U","year":"2020","journal-title":"Nat Commun"},{"key":"e_1_2_10_89_1","doi-asserted-by":"crossref","first-page":"E7176","DOI":"10.1073\/pnas.1522332112","article-title":"cAMP\u2010induced phosphorylation of 26S proteasomes on Rpn6\/PSMD11 enhances their activity and the degradation of misfolded proteins","volume":"112","author":"Lokireddy S","year":"2015","journal-title":"P Natl Acad Sci USA"},{"key":"e_1_2_10_90_1","doi-asserted-by":"crossref","first-page":"3189","DOI":"10.1534\/g3.120.401526","article-title":"Precise replacement of Saccharomyces cerevisiae proteasome genes with human Orthologs by an integrative targeting method","volume":"10","author":"Yellman CM","year":"2020","journal-title":"G3"},{"key":"e_1_2_10_91_1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/978-3-030-58971-4_1","article-title":"Structure, dynamics and function of the 26S proteasome","volume":"96","author":"Mao Y","year":"2021","journal-title":"Subcell Biochem"},{"key":"e_1_2_10_92_1","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1038\/ncb3289","article-title":"Site\u2010specific proteasome phosphorylation controls cell proliferation and tumorigenesis","volume":"18","author":"Guo X","year":"2016","journal-title":"Nat Cell Biol"},{"key":"e_1_2_10_93_1","first-page":"859","article-title":"Inducible Rpt3, a proteasome component, knockout in adult skeletal muscle results in muscle atrophy, front cell","volume":"8","author":"Kitajima Y","year":"2020","journal-title":"Dev Biol"},{"key":"e_1_2_10_94_1","doi-asserted-by":"crossref","first-page":"1523","DOI":"10.1016\/j.stemcr.2018.10.009","article-title":"The ubiquitin\u2010proteasome system is indispensable for the maintenance of muscle stem cells","volume":"11","author":"Kitajima Y","year":"2018","journal-title":"Stem Cell Rep"},{"key":"e_1_2_10_95_1","first-page":"5204","article-title":"Proteasome dysfunction induces muscle growth defects and protein aggregation","volume":"127","author":"Kitajima Y","year":"2014","journal-title":"J Cell Sci"},{"key":"e_1_2_10_96_1","doi-asserted-by":"crossref","first-page":"42984","DOI":"10.1074\/jbc.M112.417600","article-title":"Motor neuron\u2010specific disruption of proteasomes, but not autophagy, replicates amyotrophic lateral sclerosis","volume":"287","author":"Tashiro Y","year":"2012","journal-title":"J Biol Chem"},{"key":"e_1_2_10_97_1","doi-asserted-by":"crossref","DOI":"10.1126\/science.adf2018","article-title":"An abundance of free regulatory (19S) proteasome particles regulates neuronal synapses","volume":"380","author":"Sun C","year":"2023","journal-title":"Science"},{"key":"e_1_2_10_98_1","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1038\/nprot.2007.13","article-title":"High\u2010efficiency yeast transformation using the LiAc\/SS carrier DNA\/PEG method","volume":"2","author":"Gietz RD","year":"2007","journal-title":"Nat Protoc"},{"key":"e_1_2_10_99_1","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1002\/(SICI)1097-0061(199807)14:10<953::AID-YEA293>3.0.CO;2-U","article-title":"Additional modules for versatile and economical PCR\u2010based gene deletion and modification in Saccharomyces cerevisiae","volume":"14","author":"Longtine MS","year":"1998","journal-title":"Yeast"},{"key":"e_1_2_10_100_1","doi-asserted-by":"crossref","DOI":"10.1093\/femsyr\/fov061","article-title":"Amyloid\u2010beta peptide\u2010induced cytotoxicity and mitochondrial dysfunction in yeast","volume":"15","author":"Chen X","year":"2015","journal-title":"FEMS Yeast Res"},{"key":"e_1_2_10_101_1","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1007\/978-1-4939-8706-1_16","article-title":"Native gel approaches in studying proteasome assembly and chaperones","volume":"1844","author":"Roelofs J","year":"2018","journal-title":"Methods Mol Biol"},{"key":"e_1_2_10_102_1","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1016\/S0076-6879(05)98029-4","article-title":"Characterization of the proteasome using native gel electrophoresis","volume":"398","author":"Elsasser S","year":"2005","journal-title":"Methods Enzymol"}],"container-title":["The FEBS Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/pdf\/10.1111\/febs.70714","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/full-xml\/10.1111\/febs.70714","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/pdf\/10.1111\/febs.70714","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,29]],"date-time":"2026-08-29T07:15:53Z","timestamp":1787987753000},"score":1,"resource":{"primary":{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/10.1111\/febs.70714"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8,29]]},"references-count":101,"alternative-id":["10.1111\/febs.70714"],"URL":"https:\/\/doi.org\/10.1111\/febs.70714","archive":["Portico"],"relation":{},"ISSN":["1742-464X","1742-4658"],"issn-type":[{"value":"1742-464X","type":"print"},{"value":"1742-4658","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,8,29]]},"assertion":[{"value":"2025-12-23","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2026-06-15","order":2,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2026-08-29","order":3,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}],"article-number":"febs.70714"}}