{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T15:33:52Z","timestamp":1791387232850,"version":"4.3.3"},"reference-count":181,"publisher":"Elsevier BV","issue":"8","license":[{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,6,17]],"date-time":"2026-06-17T00:00:00Z","timestamp":1781654400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100012793","name":"Marquette University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100012793","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100012794","name":"Marquette University Office of Research and Sponsored Programs","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100012794","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000082","name":"National Science Foundation Division of Graduate Education","doi-asserted-by":"publisher","award":["2437845"],"award-info":[{"award-number":["2437845"]}],"id":[{"id":"10.13039\/100000082","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100023581","name":"National Science Foundation Graduate Research Fellowship Program","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100023581","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2026,8]]},"DOI":"10.1016\/j.jbc.2026.113271","type":"journal-article","created":{"date-parts":[[2026,6,19]],"date-time":"2026-06-19T16:17:09Z","timestamp":1781885829000},"page":"113271","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"title":["Integrating condensates into protein lifespan \u2013 From birth to death"],"prefix":"10.1016","volume":"302","author":[{"ORCID":"https:\/\/orcid.org\/0009-0002-6459-5202","authenticated-orcid":false,"given":"Chloe A.","family":"Langridge","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3068-6253","authenticated-orcid":false,"given":"Emily M.","family":"Sontag","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2026.113271_bib1","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1126\/science.1141448","article-title":"Adapting proteostasis for disease intervention","volume":"319","author":"Balch","year":"2008","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.113271_bib2","doi-asserted-by":"crossref","DOI":"10.3389\/fcell.2021.637084","article-title":"Regulation of age-related protein toxicity","volume":"9","author":"Pras","year":"2021","journal-title":"Front. Cell Dev. Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib3","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1083\/jcb.201012077","article-title":"Drosophila histone locus bodies form by hierarchical recruitment of components","volume":"193","author":"White","year":"2011","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib4","doi-asserted-by":"crossref","first-page":"5775","DOI":"10.1016\/j.cell.2021.10.014","article-title":"RNA promotes the formation of spatial compartments in the nucleus","volume":"184","author":"Quinodoz","year":"2021","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2026.113271_bib5","doi-asserted-by":"crossref","first-page":"1930","DOI":"10.1038\/s41467-019-09982-5","article-title":"CUT&Tag for efficient epigenomic profiling of small samples and single cells","volume":"10","author":"Kaya-Okur","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.113271_bib6","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.semcdb.2023.06.010","article-title":"P-body-like condensates in the germline","volume":"157","author":"Cassani","year":"2024","journal-title":"Semin. Cell Dev. Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib7","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1083\/jcb.136.4.761","article-title":"A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates","volume":"136","author":"Bashkirov","year":"1997","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib8","doi-asserted-by":"crossref","first-page":"6915","DOI":"10.1093\/emboj\/cdf678","article-title":"Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures","volume":"21","author":"Van Dijk","year":"2002","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2026.113271_bib9","doi-asserted-by":"crossref","first-page":"759","DOI":"10.1042\/BST20210862","article-title":"Spatial sequestration of misfolded proteins in neurodegenerative diseases","volume":"50","author":"Rolli","year":"2022","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.jbc.2026.113271_bib10","doi-asserted-by":"crossref","DOI":"10.3389\/fragi.2022.854157","article-title":"Insights into the links between proteostasis and aging from C. elegans","volume":"3","author":"Zhang","year":"2022","journal-title":"Front. Aging"},{"key":"10.1016\/j.jbc.2026.113271_bib11","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1016\/j.neuint.2012.02.012","article-title":"Amyloid precursor protein accumulates in aggresomes in response to proteasome inhibitor","volume":"60","author":"Dehvari","year":"2012","journal-title":"Neurochem. Int."},{"key":"10.1016\/j.jbc.2026.113271_bib12","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.1038\/nature07195","article-title":"Misfolded proteins partition between two distinct quality control compartments","volume":"454","author":"Kaganovich","year":"2008","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.113271_bib13","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1038\/s41556-023-01128-6","article-title":"Nuclear and cytoplasmic spatial protein quality control is coordinated by nuclear\u2013vacuolar junctions and perinuclear ESCRT","volume":"25","author":"Sontag","year":"2023","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib14","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2024.1427542","article-title":"Clearing the JUNQ: the molecular machinery for sequestration, localization, and degradation of the JUNQ compartment","volume":"11","author":"Rolli","year":"2024","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.jbc.2026.113271_bib15","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1080\/19336896.2017.1293226","article-title":"Hitchhiking vesicular transport routes to the vacuole: amyloid recruitment to the Insoluble Protein Deposit (IPOD)","volume":"11","author":"Kumar","year":"2017","journal-title":"Prion"},{"key":"10.1016\/j.jbc.2026.113271_bib16","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1016\/j.ejcb.2008.11.003","article-title":"ER-associated complexes (ERACs) containing aggregated cystic fibrosis transmembrane conductance regulator (CFTR) are degraded by autophagy","volume":"88","author":"Fu","year":"2009","journal-title":"Eur. J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib17","doi-asserted-by":"crossref","first-page":"738","DOI":"10.1016\/j.celrep.2012.08.024","article-title":"Confinement to organelle-associated inclusion structures mediates asymmetric inheritance of aggregated protein in budding yeast","volume":"2","author":"Spokoini","year":"2012","journal-title":"Cell Rep."},{"key":"10.1016\/j.jbc.2026.113271_bib18","doi-asserted-by":"crossref","first-page":"8049","DOI":"10.1073\/pnas.1324035111","article-title":"Dynamic JUNQ inclusion bodies are asymmetrically inherited in mammalian cell lines through the asymmetric partitioning of vimentin","volume":"111","author":"Ogrodnik","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113271_bib19","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2020.107680","article-title":"Chaperone-mediated protein disaggregation triggers proteolytic clearance of intra-nuclear protein inclusions","volume":"31","author":"den Brave","year":"2020","journal-title":"Cell Rep."},{"key":"10.1016\/j.jbc.2026.113271_bib20","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2022.102199","article-title":"Nuclear protein quality control in yeast: the latest INQuiries","volume":"298","author":"Kumar","year":"2022","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113271_bib21","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.semcdb.2018.07.001","article-title":"Phase separated microenvironments inside the cell nucleus are linked to disease and regulate epigenetic state, transcription and RNA processing","volume":"90","author":"Sawyer","year":"2019","journal-title":"Semin. Cell Develop. Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib22","doi-asserted-by":"crossref","first-page":"4174","DOI":"10.3390\/ijms26094174","article-title":"The nucleolus: a central hub for ribosome biogenesis and cellular regulatory signals","volume":"26","author":"Ponti","year":"2025","journal-title":"IJMS"},{"key":"10.1016\/j.jbc.2026.113271_bib23","doi-asserted-by":"crossref","first-page":"1206","DOI":"10.1016\/j.stemcr.2020.08.012","article-title":"Regulation and roles of the nucleolus in embryonic stem cells: from ribosome biogenesis to genome organization","volume":"15","author":"Gupta","year":"2020","journal-title":"Stem Cell Rep."},{"key":"10.1016\/j.jbc.2026.113271_bib24","doi-asserted-by":"crossref","first-page":"3089","DOI":"10.1101\/gad.1463706","article-title":"Direct interaction between DNMT1 and G9a coordinates DNA and histone methylation during replication","volume":"20","author":"Est\u00e8ve","year":"2006","journal-title":"Genes Dev."},{"key":"10.1016\/j.jbc.2026.113271_bib25","doi-asserted-by":"crossref","first-page":"2165","DOI":"10.1016\/j.molcel.2025.05.004","article-title":"The nucleolar granular component mediates genome-nucleolus interactions and establishes their repressive chromatin states","volume":"85","author":"Gupta","year":"2025","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2026.113271_bib26","doi-asserted-by":"crossref","first-page":"3735","DOI":"10.1091\/mbc.e10-06-0508","article-title":"High-resolution whole-genome sequencing reveals that specific chromatin domains from Most human chromosomes associate with nucleoli","volume":"21","author":"Van Koningsbruggen","year":"2010","journal-title":"MBoC"},{"key":"10.1016\/j.jbc.2026.113271_bib27","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1038\/s41467-023-36021-1","article-title":"Mapping nucleolus-associated chromatin interactions using nucleolus Hi-C reveals pattern of heterochromatin interactions","volume":"14","author":"Peng","year":"2023","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.113271_bib28","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.ceb.2014.03.001","article-title":"Nucleolus and nuclear periphery: velcro for heterochromatin","volume":"28","author":"Padeken","year":"2014","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib29","article-title":"Close to the Edge: heterochromatin at the nucleolar and nuclear peripheries","volume":"1864","author":"Bizhanova","year":"2021","journal-title":"Biochim. Biophys. Acta (Bba) - Gene Regul. Mech."},{"key":"10.1016\/j.jbc.2026.113271_bib30","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1126\/science.aaw9157","article-title":"The nucleolus functions as a phase-separated protein quality control compartment","volume":"365","author":"Frottin","year":"2019","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.113271_bib31","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/j.molcel.2010.09.024","article-title":"The Nucleolus under stress","volume":"40","author":"Boulon","year":"2010","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2026.113271_bib32","doi-asserted-by":"crossref","first-page":"R930","DOI":"10.1016\/j.cub.2019.08.013","article-title":"Nucleolus: a liquid droplet compartment for misbehaving proteins","volume":"29","author":"Alberti","year":"2019","journal-title":"Curr. Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib33","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1016\/j.ceb.2012.03.010","article-title":"Nuclear bodies: multifunctional companions of the genome","volume":"24","author":"Dundr","year":"2012","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib34","doi-asserted-by":"crossref","first-page":"1313","DOI":"10.1126\/science.277.5330.1313","article-title":"Accelerated aging and nucleolar fragmentation in yeast sgs1 mutants","volume":"277","author":"Sinclair","year":"1997","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.113271_bib35","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1038\/s41392-024-01918-w","article-title":"Crossing epigenetic frontiers: the intersection of novel histone modifications and diseases","volume":"9","author":"Yao","year":"2024","journal-title":"Sig. Transduct. Target Ther."},{"key":"10.1016\/j.jbc.2026.113271_bib36","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1016\/j.bone.2015.03.012","article-title":"Epigenetic histone modifications and master regulators as determinants of context dependent nuclear receptor activity in bone cells","volume":"81","author":"Pike","year":"2015","journal-title":"Bone"},{"key":"10.1016\/j.jbc.2026.113271_bib37","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.jot.2025.08.013","article-title":"Histone modifications: unveiling the epigenetic enigma of degenerative skeletal diseases","volume":"55","author":"Zhang","year":"2025","journal-title":"J. Orthop. Translat."},{"key":"10.1016\/j.jbc.2026.113271_bib38","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1007\/978-94-007-4525-4_13","article-title":"The role of DNA methylation and histone modifications in transcriptional regulation in humans","volume":"61","author":"Miller","year":"2013","journal-title":"Subcell Biochem."},{"key":"10.1016\/j.jbc.2026.113271_bib39","doi-asserted-by":"crossref","DOI":"10.1091\/mbc.E22-11-0532","article-title":"Coordinated expression of replication-dependent histone genes from multiple loci promotes histone homeostasis in Drosophila","volume":"34","author":"Chaubal","year":"2023","journal-title":"MBoC"},{"key":"10.1016\/j.jbc.2026.113271_bib40","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1016\/0092-8674(87)90237-6","article-title":"Histone H2B repression causes cell-cycle-specific arrest in yeast: effects on chromosomal segregation, replication, and transcription","volume":"48","author":"Han","year":"1987","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2026.113271_bib41","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1016\/j.pbi.2007.07.013","article-title":"Histone modifications and dynamic regulation of genome accessibility in plants","volume":"10","author":"Pfluger","year":"2007","journal-title":"Curr. Opin. Plant Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib42","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1038\/s41467-024-55144-7","article-title":"H3K56 acetylation regulates chromatin maturation following DNA replication","volume":"16","author":"Duan","year":"2025","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.113271_bib43","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1128\/MCB.05415-11","article-title":"Histone H3 lysine 56 acetylation and the response to DNA replication fork damage","volume":"32","author":"Wurtele","year":"2012","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib44","series-title":"The Formation And Function Of The Histone Locus Body In Histone Mrna Biogenesis","author":"Kaitlin","year":"2019"},{"key":"10.1016\/j.jbc.2026.113271_bib45","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a000653","article-title":"The cajal body and histone locus body","volume":"2","author":"Nizami","year":"2010","journal-title":"Cold Spring Harbor Perspect. Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib46","doi-asserted-by":"crossref","first-page":"942","DOI":"10.1091\/mbc.E20-10-0645","article-title":"Superresolution light microscopy of the Drosophila histone locus body reveals a core\u2013shell organization associated with expression of replication\u2013dependent histone genes","volume":"32","author":"Kemp","year":"2021","journal-title":"MBoC"},{"key":"10.1016\/j.jbc.2026.113271_bib47","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/j.molcel.2009.08.016","article-title":"FLASH, a proapoptotic protein involved in activation of Caspase-8, is essential for 3\u2032 end processing of histone Pre-mRNAs","volume":"36","author":"Yang","year":"2009","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2026.113271_bib48","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2023.112768","article-title":"Cyclin E\/CDK2 and feedback from soluble histone protein regulate the S phase burst of histone biosynthesis","volume":"42","author":"Armstrong","year":"2023","journal-title":"Cell Rep."},{"key":"10.1016\/j.jbc.2026.113271_bib49","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1080\/15476286.2016.1265198","article-title":"Coordinating cell cycle-regulated histone gene expression through assembly and function of the Histone Locus Body","volume":"14","author":"Duronio","year":"2017","journal-title":"RNA Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib50","doi-asserted-by":"crossref","DOI":"10.1080\/19491034.2023.2293604","article-title":"Histone locus bodies: a paradigm for how nuclear biomolecular condensates control cell cycle regulated gene expression","volume":"14","author":"Geisler","year":"2023","journal-title":"Nucleus"},{"key":"10.1016\/j.jbc.2026.113271_bib51","doi-asserted-by":"crossref","first-page":"33767","DOI":"10.1074\/jbc.M114.616466","article-title":"A conserved interaction that is essential for the biogenesis of histone locus bodies","volume":"289","author":"Yang","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113271_bib52","doi-asserted-by":"crossref","first-page":"2108","DOI":"10.1016\/j.bbamcr.2008.07.016","article-title":"The Cajal body","volume":"1783","author":"Morris","year":"2008","journal-title":"Biochim. et Biophys. Acta (Bba) - Mol. Cell Res."},{"key":"10.1016\/j.jbc.2026.113271_bib53","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1134\/S106236041406006X","article-title":"Cajal bodies and histone locus bodies: molecular composition and function","volume":"45","author":"Khodyuchenko","year":"2014","journal-title":"Russ. J. Dev. Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib54","doi-asserted-by":"crossref","first-page":"1661","DOI":"10.1091\/mbc.e08-05-0525","article-title":"Coilin is essential for Cajal Body Organization in Drosophila melanogaster","volume":"20","author":"Liu","year":"2009","journal-title":"MBoC"},{"key":"10.1016\/j.jbc.2026.113271_bib55","doi-asserted-by":"crossref","first-page":"1872","DOI":"10.1242\/jcs.044040","article-title":"Cajal-body formation correlates with differential coilin phosphorylation in primary and transformed cell lines","volume":"122","author":"Hearst","year":"2009","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.jbc.2026.113271_bib56","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1080\/15476286.2016.1243648","article-title":"Specific genomic cues regulate Cajal body assembly","volume":"14","author":"Sawyer","year":"2017","journal-title":"RNA Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib57","doi-asserted-by":"crossref","first-page":"1314","DOI":"10.1016\/j.biocel.2013.03.019","article-title":"Signals controlling Cajal body assembly and function","volume":"45","author":"Hebert","year":"2013","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib58","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1080\/15476286.2016.1231359","article-title":"Cajal bodies and snRNPs - friends with benefits","volume":"14","author":"Stan\u011bk","year":"2017","journal-title":"RNA Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib59","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1016\/j.celrep.2014.12.030","article-title":"SART3-Dependent accumulation of incomplete spliceosomal snRNPs in cajal bodies","volume":"10","author":"Novotn\u00fd","year":"2015","journal-title":"Cell Rep."},{"key":"10.1016\/j.jbc.2026.113271_bib60","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1080\/15476286.2016.1249091","article-title":"RNA modification in Cajal bodies","volume":"14","author":"Meier","year":"2017","journal-title":"RNA Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib61","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202309128","article-title":"Dynamic interaction of spliceosomal snRNPs with coilin explains Cajal body characteristics","volume":"224","author":"Basello","year":"2025","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib62","doi-asserted-by":"crossref","DOI":"10.1242\/jcs.263447","article-title":"Cajal body formation is regulated by coilin SUMOylation","volume":"137","author":"Tucker","year":"2024","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.jbc.2026.113271_bib63","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1016\/S0960-9822(99)80475-8","article-title":"Newly assembled snRNPs associate with coiled bodies before speckles, suggesting a nuclear snRNP maturation pathway","volume":"9","author":"Sleeman","year":"1999","journal-title":"Curr. Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib64","doi-asserted-by":"crossref","first-page":"a000646","DOI":"10.1101\/cshperspect.a000646","article-title":"Nuclear speckles","volume":"3","author":"Spector","year":"2011","journal-title":"Cold Spring Harbor Perspect. Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib65","doi-asserted-by":"crossref","first-page":"3912","DOI":"10.1083\/jcb.201801184","article-title":"Intronless mRNAs transit through nuclear speckles to gain export competence","volume":"217","author":"Wang","year":"2018","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib66","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202111151","article-title":"Stress-induced nuclear speckle reorganization is linked to activation of immediate early gene splicing","volume":"222","author":"Sung","year":"2023","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib67","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202311014","article-title":"Splicing under stress: a matter of time and place","volume":"222","author":"Podszywalow-Bartnicka","year":"2023","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib68","doi-asserted-by":"crossref","first-page":"6169","DOI":"10.1074\/jbc.M115.689414","article-title":"Nuclear speckle-related protein 70 binds to Serine\/Arginine-rich splicing factors 1 and 2 via an Arginine\/Serine-like Region and counteracts their alternative splicing activity","volume":"291","author":"Kim","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113271_bib69","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1038\/s41467-024-55469-3","article-title":"Phosphorylation of a nuclear condensate regulates cohesion and mRNA retention","volume":"16","author":"McIntyre","year":"2025","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.113271_bib70","article-title":"SRRM2 phase separation drives assembly of nuclear speckle subcompartments","volume":"43","author":"Zhang","year":"2024","journal-title":"Cell Rep."},{"key":"10.1016\/j.jbc.2026.113271_bib71","doi-asserted-by":"crossref","first-page":"a000687","DOI":"10.1101\/cshperspect.a000687","article-title":"Paraspeckles","volume":"2","author":"Fox","year":"2010","journal-title":"Cold Spring Harbor Perspect. Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib72","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2022.102563","article-title":"Paraspeckle subnuclear bodies depend on dynamic heterodimerisation of DBHS RNA-binding proteins via their structured domains","volume":"298","author":"Lee","year":"2022","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113271_bib73","doi-asserted-by":"crossref","first-page":"3989","DOI":"10.1093\/nar\/gkw271","article-title":"The DBHS proteins SFPQ, NONO and PSPC1: a multipurpose molecular scaffold","volume":"44","author":"Knott","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jbc.2026.113271_bib74","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1186\/s13024-018-0263-7","article-title":"Protective paraspeckle hyper-assembly downstream of TDP-43 loss of function in amyotrophic lateral sclerosis","volume":"13","author":"Shelkovnikova","year":"2018","journal-title":"Mol. Neurodegener"},{"key":"10.1016\/j.jbc.2026.113271_bib75","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2024.114695","article-title":"Paraspeckle-independent co-transcriptional regulation of nuclear microRNA biogenesis by SFPQ","volume":"43","author":"Thivierge","year":"2024","journal-title":"Cell Rep."},{"key":"10.1016\/j.jbc.2026.113271_bib76","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/j.ncrna.2019.11.002","article-title":"Nuclear paraspeckles function in mediating gene regulatory and apoptotic pathways","volume":"4","author":"Pisani","year":"2019","journal-title":"Noncoding RNA Res."},{"key":"10.1016\/j.jbc.2026.113271_bib77","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1016\/j.molcel.2009.06.027","article-title":"Altered nuclear retention of mRNAs containing inverted repeats in human embryonic stem cells: functional role of a nuclear noncoding RNA","volume":"35","author":"Chen","year":"2009","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2026.113271_bib78","doi-asserted-by":"crossref","first-page":"6488","DOI":"10.3390\/ijms26136488","article-title":"Nuclear retention of mRNAs through paraspeckle protein binding to a sequence determinant in 3\u2019UTR","volume":"26","author":"Jacq","year":"2025","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2026.113271_bib79","doi-asserted-by":"crossref","first-page":"2558","DOI":"10.1016\/j.neuron.2024.05.003","article-title":"Nuclear aggregates of NONO\/SFPQ and A-to-I-edited RNA in Parkinson\u2019s disease and dementia with lewy bodies","volume":"112","author":"Belur","year":"2024","journal-title":"Neuron"},{"key":"10.1016\/j.jbc.2026.113271_bib80","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1016\/S0092-8674(01)00466-4","article-title":"The fate of dsRNA in the nucleus","volume":"106","author":"Zhang","year":"2001","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2026.113271_bib81","doi-asserted-by":"crossref","first-page":"6914","DOI":"10.1021\/acs.jpclett.0c01748","article-title":"Nanoscale viscosity of cytoplasm is conserved in human cell lines","volume":"11","author":"Kwapiszewska","year":"2020","journal-title":"J. Phys. Chem. Lett."},{"key":"10.1016\/j.jbc.2026.113271_bib82","doi-asserted-by":"crossref","DOI":"10.1016\/j.ceb.2025.102507","article-title":"Dynamic structure of the cytoplasm","volume":"94","author":"Kim","year":"2025","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib83","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1038\/nrm.2017.7","article-title":"Biomolecular condensates: organizers of cellular biochemistry","volume":"18","author":"Banani","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib84","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1002\/cbf.2804","article-title":"P-bodies and their functions during mRNA cell cycle: mini-review","volume":"30","author":"Olszewska","year":"2012","journal-title":"Cell Biochem. Funct."},{"key":"10.1016\/j.jbc.2026.113271_bib85","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.41300","article-title":"Context-dependent deposition and regulation of mRNAs in P-bodies","volume":"7","author":"Wang","year":"2018","journal-title":"eLife"},{"key":"10.1016\/j.jbc.2026.113271_bib86","doi-asserted-by":"crossref","first-page":"2720","DOI":"10.1038\/s41467-024-46943-z","article-title":"A rapid inducible RNA decay system reveals fast mRNA decay in P-bodies","volume":"15","author":"Blake","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.113271_bib87","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1126\/science.1082320","article-title":"Decapping and decay of messenger RNA occur in cytoplasmic processing bodies","volume":"300","author":"Sheth","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.113271_bib88","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/j.molcel.2017.09.003","article-title":"P-Body purification reveals the condensation of repressed mRNA regulons","volume":"68","author":"Hubstenberger","year":"2017","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2026.113271_bib89","doi-asserted-by":"crossref","first-page":"3970","DOI":"10.1128\/MCB.00128-07","article-title":"P-Body formation is a consequence, not the cause, of RNA-mediated gene silencing","volume":"27","author":"Eulalio","year":"2007","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib90","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1126\/science.1115791","article-title":"Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies","volume":"310","author":"Brengues","year":"2005","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.113271_bib91","doi-asserted-by":"crossref","first-page":"2347","DOI":"10.1038\/s44319-025-00425-5","article-title":"Praja2 controls P-body assembly and translation in glioblastoma by non-proteolytic ubiquitylation of DDX6","volume":"26","author":"Senatore","year":"2025","journal-title":"EMBO Rep."},{"key":"10.1016\/j.jbc.2026.113271_bib92","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0049783","article-title":"The P body protein Dcp1a is hyper-phosphorylated during mitosis","volume":"8","author":"Aizer","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2026.113271_bib93","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.febslet.2008.12.002","article-title":"Dcp1a phosphorylation along neuronal development and stress","volume":"583","author":"Blumenthal","year":"2009","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2026.113271_bib94","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0061697","article-title":"Phosphorylation of mRNA decapping protein Dcp1a by the ERK signaling pathway during early differentiation of 3T3-L1 preadipocytes","volume":"8","author":"Chiang","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2026.113271_bib95","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1089\/ars.2022.0164","article-title":"Stress granules as causes and consequences of translation suppression","volume":"39","author":"Baymiller","year":"2023","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.jbc.2026.113271_bib96","doi-asserted-by":"crossref","first-page":"932","DOI":"10.1016\/j.molcel.2009.11.020","article-title":"Eukaryotic stress granules: the ins and outs of translation","volume":"36","author":"Buchan","year":"2009","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2026.113271_bib97","doi-asserted-by":"crossref","first-page":"3786","DOI":"10.1091\/mbc.e12-04-0296","article-title":"Translation suppression promotes stress granule formation and cell survival in response to cold shock","volume":"23","author":"Hofmann","year":"2012","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.jbc.2026.113271_bib98","doi-asserted-by":"crossref","first-page":"1801","DOI":"10.1016\/j.cell.2020.11.010","article-title":"Single-molecule imaging reveals translation of mRNAs localized to stress granules","volume":"183","author":"Mateju","year":"2020","journal-title":"Cell."},{"key":"10.1016\/j.jbc.2026.113271_bib99","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1038\/s41556-025-01834-3","article-title":"The G3BP stress-granule proteins reinforce the integrated stress response translation programme","volume":"28","author":"Smith","year":"2026","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib100","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1083\/jcb.200807043","article-title":"P bodies promote stress granule assembly in Saccharomyces cerevisiae","volume":"183","author":"Buchan","year":"2008","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib101","doi-asserted-by":"crossref","first-page":"1431","DOI":"10.1083\/jcb.147.7.1431","article-title":"RNA-binding proteins Tia-1 and tiar link the phosphorylation of Eif-2\u03b1 to the assembly of mammalian stress granules","volume":"147","author":"Kedersha","year":"1999","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib102","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1083\/jcb.200502088","article-title":"Stress granules and processing bodies are dynamically linked sites of mRNP remodeling","volume":"169","author":"Kedersha","year":"2005","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib103","series-title":"Ten Years of Progress in GW\/P Body Research","first-page":"197","article-title":"Relationship of GW\/P-Bodies with stress granules","volume":"768","author":"Stoecklin","year":"2013"},{"key":"10.1016\/j.jbc.2026.113271_bib104","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2014457118","article-title":"Local translation in nuclear condensate amyloid bodies","volume":"118","author":"Theodoridis","year":"2021","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113271_bib105","doi-asserted-by":"crossref","first-page":"3162","DOI":"10.1002\/1873-3468.13597","article-title":"Stress-specific aggregation of proteins in the amyloid bodies","volume":"593","author":"Marijan","year":"2019","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2026.113271_bib106","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-023-41712-2","article-title":"Stress-mediated aggregation of disease-associated proteins in amyloid bodies","volume":"13","author":"Chandhok","year":"2023","journal-title":"Sci Rep."},{"key":"10.1016\/j.jbc.2026.113271_bib107","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1186\/s12964-024-01791-8","article-title":"Misfolding and aggregation in neurodegenerative diseases: protein quality control machinery as potential therapeutic clearance pathways","volume":"22","author":"Kosz\u0142a","year":"2024","journal-title":"Cell Commun. Signal."},{"key":"10.1016\/j.jbc.2026.113271_bib108","doi-asserted-by":"crossref","first-page":"8065","DOI":"10.1038\/ncomms9065","article-title":"Transcription errors induce proteotoxic stress and shorten cellular lifespan","volume":"6","author":"Vermulst","year":"2015","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.113271_bib109","doi-asserted-by":"crossref","first-page":"1012","DOI":"10.1073\/pnas.98.3.1012","article-title":"Proteins associated with the promyelocytic leukemia gene product (PML)-containing nuclear body move to the nucleolus upon inhibition of proteasome-dependent protein degradation","volume":"98","author":"Mattsson","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113271_bib110","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1083\/jcb.201305148","article-title":"Oxidative stress\u2013induced assembly of PML nuclear bodies controls sumoylation of partner proteins","volume":"204","author":"Sahin","year":"2014","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib111","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1016\/j.ceb.2018.03.011","article-title":"PML nuclear bodies: from architecture to function","volume":"52","author":"Lallemand-Breitenbach","year":"2018","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib112","doi-asserted-by":"crossref","first-page":"2075","DOI":"10.3390\/cells13242075","article-title":"PML nuclear bodies and cellular senescence: a comparative study of healthy and premature aging syndrome donors\u2019 cells","volume":"13","author":"Smirnov","year":"2024","journal-title":"Cells"},{"key":"10.1016\/j.jbc.2026.113271_bib113","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":"10.1016\/j.jbc.2026.113271_bib114","first-page":"99","article-title":"The functional roles of PML nuclear bodies in genome maintenance","volume":"809","author":"Chang","year":"2018","journal-title":"Mutat. Res."},{"key":"10.1016\/j.jbc.2026.113271_bib115","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1083\/jcb.200604009","article-title":"Promyelocytic leukemia nuclear bodies behave as DNA damage sensors whose response to DNA double-strand breaks is regulated by NBS1 and the kinases ATM, Chk2, and ATR","volume":"175","author":"Dellaire","year":"2006","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib116","doi-asserted-by":"crossref","first-page":"3197","DOI":"10.1084\/jem.20160301","article-title":"PML is a ROS sensor activating p53 upon oxidative stress","volume":"214","author":"Niwa-Kawakita","year":"2017","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.jbc.2026.113271_bib117","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.molcel.2014.04.030","article-title":"A cellular system that degrades misfolded proteins and protects against neurodegeneration","volume":"55","author":"Guo","year":"2014","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2026.113271_bib118","first-page":"RP88237","article-title":"Nuclear Bodies Protect Phase Separated Proteins from Degradation in Stressed Proteome","volume":"12","author":"Jung","year":"2023","journal-title":"eLife"},{"key":"10.1016\/j.jbc.2026.113271_bib119","doi-asserted-by":"crossref","first-page":"1156","DOI":"10.1093\/nar\/gkad1176","article-title":"Spatial regulation of DNA damage tolerance protein Rad5 interconnects genome stability maintenance and proteostasis networks","volume":"52","author":"Lehmann","year":"2024","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jbc.2026.113271_bib120","doi-asserted-by":"crossref","first-page":"4027","DOI":"10.1083\/jcb.201612018","article-title":"Selective aggregation of the splicing factor Hsh155 suppresses splicing upon genotoxic stress","volume":"216","author":"Mathew","year":"2017","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib121","doi-asserted-by":"crossref","first-page":"6533","DOI":"10.1038\/ncomms7533","article-title":"Cmr1\/WDR76 defines a nuclear genotoxic stress body linking genome integrity and protein quality control","volume":"6","author":"Gallina","year":"2015","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.113271_bib122","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1038\/s41586-018-0678-x","article-title":"Distinct proteostasis circuits cooperate in nuclear and cytoplasmic protein quality control","volume":"563","author":"Samant","year":"2018","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.113271_bib123","doi-asserted-by":"crossref","first-page":"388","DOI":"10.1016\/j.cell.2014.09.012","article-title":"Surveillance of nuclear pore complex assembly by ESCRT-III\/Vps4","volume":"159","author":"Webster","year":"2014","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2026.113271_bib124","doi-asserted-by":"crossref","first-page":"2447","DOI":"10.15252\/embj.201694574","article-title":"Chm7 and Heh1 collaborate to link nuclear pore complex quality control with nuclear envelope sealing","volume":"35","author":"Webster","year":"2016","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2026.113271_bib125","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1038\/ncb2838","article-title":"Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress","volume":"15","author":"Escusa-Toret","year":"2013","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib126","doi-asserted-by":"crossref","first-page":"2698","DOI":"10.1016\/j.molcel.2024.06.024","article-title":"Polysome collapse and RNA condensation fluidize the cytoplasm","volume":"84","author":"Xie","year":"2024","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2026.113271_bib127","doi-asserted-by":"crossref","first-page":"1269","DOI":"10.1083\/jcb.201708116","article-title":"A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins","volume":"217","author":"Grousl","year":"2018","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib128","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1042\/BST20120108","article-title":"Diverse functional manifestations of intrinsic structural disorder in molecular chaperones","volume":"40","author":"Kovacs","year":"2012","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.jbc.2026.113271_bib129","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1083\/jcb.114.4.609","article-title":"Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein","volume":"114","author":"Caplan","year":"1991","journal-title":"J. Cel. Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib130","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1016\/j.cub.2017.01.069","article-title":"Compartmentalization of ER-Bound chaperone confines protein deposit formation to the aging yeast cell","volume":"27","author":"Saarikangas","year":"2017","journal-title":"Curr. Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib131","doi-asserted-by":"crossref","first-page":"8219","DOI":"10.1074\/jbc.M212725200","article-title":"Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae","volume":"278","author":"Beilharz","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113271_bib132","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1016\/j.str.2020.07.017","article-title":"Multi-scale 3D cryo-correlative microscopy for vitrified cells","volume":"28","author":"Wu","year":"2020","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2026.113271_bib133","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1016\/j.molcel.2018.03.028","article-title":"Hsp90 breaks the deadlock of the Hsp70 chaperone system","volume":"70","author":"Mor\u00e1n Luengo","year":"2018","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2026.113271_bib134","doi-asserted-by":"crossref","first-page":"1543","DOI":"10.1100\/tsw.2010.152","article-title":"Heat shock proteins: cell protection through protein triage","volume":"10","author":"Lanneau","year":"2010","journal-title":"Sci. World J."},{"key":"10.1016\/j.jbc.2026.113271_bib135","doi-asserted-by":"crossref","first-page":"4851","DOI":"10.1038\/s41467-019-12868-1","article-title":"Cellular sequestrases maintain basal Hsp70 capacity ensuring balanced proteostasis","volume":"10","author":"Ho","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.113271_bib136","doi-asserted-by":"crossref","first-page":"3041","DOI":"10.1091\/mbc.e12-03-0194","article-title":"Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates","volume":"23","author":"Malinovska","year":"2012","journal-title":"MBoC"},{"key":"10.1016\/j.jbc.2026.113271_bib137","doi-asserted-by":"crossref","first-page":"778","DOI":"10.15252\/embj.201489524","article-title":"Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition","volume":"34","author":"Miller","year":"2015","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2026.113271_bib138","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1534\/genetics.112.140467","article-title":"The ubiquitin\u2013proteasome system of Saccharomyces cerevisiae","volume":"192","author":"Finley","year":"2012","journal-title":"Genetics"},{"key":"10.1016\/j.jbc.2026.113271_bib139","doi-asserted-by":"crossref","first-page":"237","DOI":"10.3389\/fnmol.2018.00237","article-title":"The insoluble protein deposit (IPOD) in yeast","volume":"11","author":"Rothe","year":"2018","journal-title":"Front. Mol. Neurosci."},{"key":"10.1016\/j.jbc.2026.113271_bib140","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1006324","article-title":"Prion aggregates are recruited to the insoluble protein deposit (IPOD) via myosin 2-Based vesicular transport","volume":"12","author":"Kumar","year":"2016","journal-title":"PLoS Genet."},{"key":"10.1016\/j.jbc.2026.113271_bib141","doi-asserted-by":"crossref","first-page":"1564","DOI":"10.1016\/j.jmb.2015.02.006","article-title":"Spatially organized aggregation of misfolded proteins as cellular stress defense strategy","volume":"427","author":"Miller","year":"2015","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib142","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","year":"2011","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib143","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.11792","article-title":"Spatial sequestration and detoxification of huntingtin by the ribosome quality control complex","volume":"5","author":"Yang","year":"2016","journal-title":"Elife"},{"key":"10.1016\/j.jbc.2026.113271_bib144","doi-asserted-by":"crossref","first-page":"2096","DOI":"10.1016\/j.celrep.2019.07.053","article-title":"Syntaxin 5 is required for the formation and clearance of protein inclusions during proteostatic stress","volume":"28","author":"Babazadeh","year":"2019","journal-title":"Cell Rep."},{"key":"10.1016\/j.jbc.2026.113271_bib145","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1007\/s00018-015-2052-6","article-title":"The endoplasmic reticulum: structure, function and response to cellular signaling","volume":"73","author":"Schwarz","year":"2016","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.jbc.2026.113271_bib146","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1083\/jcb.200907074","article-title":"Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response","volume":"187","author":"Schuck","year":"2009","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib147","article-title":"Endoplasmic reticulum\u2013associated protein degradation","volume":"14","author":"Krshnan","year":"2022","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib148","doi-asserted-by":"crossref","first-page":"4","DOI":"10.15252\/embj.201488896","article-title":"Unfolded protein response-induced ERdj3 secretion links ER stress to extracellular proteostasis","volume":"34","author":"Genereux","year":"2015","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2026.113271_bib149","doi-asserted-by":"crossref","first-page":"908","DOI":"10.1091\/mbc.e03-07-0546","article-title":"A striking quality control subcompartment in Saccharomyces cerevisiae : the endoplasmic reticulum-associated compartment","volume":"15","author":"Huyer","year":"2004","journal-title":"MBoC"},{"key":"10.1016\/j.jbc.2026.113271_bib150","doi-asserted-by":"crossref","DOI":"10.1242\/jcs.263616","article-title":"The formation of chaperone-rich GET bodies depends on the tetratricopeptide repeat region of Sgt2 and is reversed by NADH","volume":"138","author":"Jennrich","year":"2025","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.jbc.2026.113271_bib151","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.1016\/j.cell.2007.01.036","article-title":"Identification of a targeting factor for posttranslational membrane protein insertion into the ER","volume":"128","author":"Stefanovic","year":"2007","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2026.113271_bib152","doi-asserted-by":"crossref","first-page":"1832","DOI":"10.1242\/jcs.020321","article-title":"Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins","volume":"121","author":"Favaloro","year":"2008","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.jbc.2026.113271_bib153","doi-asserted-by":"crossref","DOI":"10.15252\/embj.201899264","article-title":"Substrate relay in an Hsp70-cochaperone cascade safeguards tail-anchored membrane protein targeting","volume":"37","author":"Cho","year":"2018","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2026.113271_bib154","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1038\/s41467-023-44260-5","article-title":"Dynamic stability of Sgt2 enables selective and privileged client handover in a chaperone triad","volume":"15","author":"Cho","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.113271_bib155","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1242\/jcs.112151","article-title":"Get3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked","volume":"126","author":"Powis","year":"2013","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.jbc.2026.113271_bib156","article-title":"A Dynamic Redox Switch Turns TRC40 into a Chaperone Protecting Human Cells Against ATP-depleting Oxidative Stress","author":"Dempsey","year":"2024","journal-title":"BioRxiv"},{"key":"10.1016\/j.jbc.2026.113271_bib157","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1091\/mbc.e12-08-0639","article-title":"COPII machinery cooperates with ER-localized Hsp40 to sequester misfolded membrane proteins into ER-associated compartments","volume":"24","author":"Kakoi","year":"2013","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.jbc.2026.113271_bib158","doi-asserted-by":"crossref","DOI":"10.15252\/embj.2022111802","article-title":"Cytosolic stress granules relieve the ubiquitin-proteasome system in the nuclear compartment","volume":"42","author":"Xu","year":"2023","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2026.113271_bib159","doi-asserted-by":"crossref","DOI":"10.1042\/EBC20253033","article-title":"Role of p62 nuclear condensates in regulating ubiquitin-mediated proteasomal degradation","volume":"69","author":"Lulu-Shimron","year":"2025","journal-title":"Essays Biochem."},{"key":"10.1016\/j.jbc.2026.113271_bib160","doi-asserted-by":"crossref","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. U. S. A."},{"key":"10.1016\/j.jbc.2026.113271_bib161","doi-asserted-by":"crossref","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. U. S. A."},{"key":"10.1016\/j.jbc.2026.113271_bib162","article-title":"Excess Met1-ubiquitination Leads to Solid Aggregate Formation","author":"Kaypee","year":"2026","journal-title":"BioRxiv"},{"key":"10.1016\/j.jbc.2026.113271_bib163","doi-asserted-by":"crossref","first-page":"1943","DOI":"10.1038\/s41556-024-01522-8","article-title":"Caspase-2 is a condensate-mediated deubiquitinase in protein quality control","volume":"26","author":"Ge","year":"2024","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib164","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2405964121","article-title":"Phase separation of polyubiquitinated proteins in UBQLN2 condensates controls substrate fate","volume":"121","author":"Valentino","year":"2024","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113271_bib165","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1016\/j.molcel.2018.02.004","article-title":"Ubiquitin modulates liquid-liquid phase separation of UBQLN2 via disruption of multivalent interactions","volume":"69","author":"Dao","year":"2018","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2026.113271_bib166","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1038\/s41598-020-78775-4","article-title":"Shared and divergent phase separation and aggregation properties of brain-expressed ubiquilins","volume":"11","author":"Gerson","year":"2021","journal-title":"Sci Rep."},{"key":"10.1016\/j.jbc.2026.113271_bib167","doi-asserted-by":"crossref","first-page":"2694","DOI":"10.1038\/s44318-026-00745-9","article-title":"ALS mutations disrupt self-association between the ubiquilin STI1 hydrophobic groove and internal placeholder sequences","volume":"45","author":"Onwunma","year":"2026","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2026.113271_bib168","doi-asserted-by":"crossref","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. U. S. A."},{"key":"10.1016\/j.jbc.2026.113271_bib169","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1007\/s00018-022-04170-z","article-title":"RTL8 promotes nuclear localization of UBQLN2 to subnuclear compartments associated with protein quality control","volume":"79","author":"Mohan","year":"2022","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.jbc.2026.113271_bib170","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1080\/19420889.2022.2051843","article-title":"Arabidopsis AGO4 loses its Cajal body localization when heterologously expressed in Nicotiana benthamiana","volume":"15","author":"Wang","year":"2022","journal-title":"Commun. Integr. Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib171","doi-asserted-by":"crossref","DOI":"10.1016\/j.isci.2024.110314","article-title":"Long noncoding RNAs heat shock RNA omega nucleates TBPH and promotes intestinal stem cell differentiation upon heat shock","volume":"27","author":"Guo","year":"2024","journal-title":"iScience"},{"key":"10.1016\/j.jbc.2026.113271_bib172","doi-asserted-by":"crossref","first-page":"2664","DOI":"10.1091\/mbc.e04-02-0100","article-title":"Tissue-specific expression and dynamic Organization of SR splicing factors in Arabidopsis","volume":"15","author":"Fang","year":"2004","journal-title":"MBoC"},{"key":"10.1016\/j.jbc.2026.113271_bib173","doi-asserted-by":"crossref","first-page":"1305","DOI":"10.1038\/ncb2627","article-title":"Drosophila patterning is established by differential association of mRNAs with P bodies","volume":"14","author":"Weil","year":"2012","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib174","doi-asserted-by":"crossref","first-page":"201","DOI":"10.3389\/fpls.2014.00201","article-title":"Composition and function of P bodies in Arabidopsis thaliana","volume":"5","author":"Maldonado-Bonilla","year":"2014","journal-title":"Front. Plant Sci."},{"key":"10.1016\/j.jbc.2026.113271_bib175","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1016\/S0076-6879(08)02625-6","article-title":"Analyzing P-bodies in Saccharomyces cerevisiae","volume":"448","author":"Nissan","year":"2008","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.jbc.2026.113271_bib176","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1083\/jcb.200802128","article-title":"Maternal mRNAs are regulated by diverse P body\u2013related mRNP granules during early Caenorhabditis elegans development","volume":"182","author":"Noble","year":"2008","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113271_bib177","series-title":"The Integrated Stress Response","first-page":"229","article-title":"Detecting stress granules in drosophila neurons","volume":"2428","author":"De Graeve","year":"2022"},{"key":"10.1016\/j.jbc.2026.113271_bib178","doi-asserted-by":"crossref","first-page":"1420","DOI":"10.1111\/nph.15690","article-title":"Protein and metabolite composition of Arabidopsis stress granules","volume":"222","author":"Kosmacz","year":"2019","journal-title":"New Phytol."},{"key":"10.1016\/j.jbc.2026.113271_bib179","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2025.115738","article-title":"Large-scale purifications reveal yeast and human stress granule cores are heterogeneous particles with complex transcriptomes and proteomes","volume":"44","author":"Demeshkina","year":"2025","journal-title":"Cell Rep."},{"key":"10.1016\/j.jbc.2026.113271_bib180","doi-asserted-by":"crossref","DOI":"10.21769\/BioProtoc.2108","article-title":"P-body and stress granule quantification in Caenorhabditis elegans","volume":"7","author":"Rieckher","year":"2017","journal-title":"Bio Protoc."},{"key":"10.1016\/j.jbc.2026.113271_bib181","doi-asserted-by":"crossref","DOI":"10.1016\/j.isci.2020.101648","article-title":"Degradation of mutant protein aggregates within the endoplasmic reticulum of vasopressin neurons","volume":"23","author":"Miyata","year":"2020","journal-title":"iScience"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826021435?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826021435?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,8,20]],"date-time":"2026-08-20T19:42:09Z","timestamp":1787254929000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925826021435"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8]]},"references-count":181,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2026,8]]}},"alternative-id":["S0021925826021435"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2026.113271","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2026,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Integrating condensates into protein lifespan \u2013 From birth to death","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2026.113271","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"113271"}}