{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T07:56:33Z","timestamp":1790841393527,"version":"4.1.0"},"reference-count":197,"publisher":"The Royal Society","issue":"1960","license":[{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R35 GM136660"],"award-info":[{"award-number":["R35 GM136660"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,10,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Proteostasis, the process governing the dynamic regulation of protein synthesis, folding and degradation, is critical for maintaining cell function and organismal health. Ageing disrupts this intricate system, leading to inactive, misfolded and\/or aggregated proteins that contribute to age-associated pathologies. Here, we explore current findings on proteostasis and its deterioration during ageing with an attention to three major pathways: molecular chaperone (MC), ubiquitin\u2013proteasome system (UPS) and autophagy\u2013lysosomal pathway. Components in all three paths undergo age-dependent decline in both expression and function, with each impairment having select initial outcomes on the health of a proteome. For example, loss in the MC path may cause nascent chain defects, whereas a decline in the UPS may result in the accumulation of toxic aggregates. Notably, the interconnectedness of these pathways results in reciprocal reactions in all three. Understanding how each path connects to the others and how these connections are regulated offers promising strategies to restore proteome integrity and extend a healthy lifespan.<\/jats:p>\n                  <jats:p>This article is part of the Theo Murphy meeting issue \u2018ProteostaSys: a systems view of proteostasis'.<\/jats:p>","DOI":"10.1098\/rstb.2025.0266","type":"journal-article","created":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T07:07:15Z","timestamp":1790838435000},"source":"Crossref","is-referenced-by-count":0,"title":["Proteostasis and ageing dissidence"],"prefix":"10.1098","volume":"381","author":[{"given":"Neethu","family":"Babu","sequence":"first","affiliation":[{"name":"Cell and Developmental Biology, University of Illinois at Urbana-Champaign , Urbana, IL 61801, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katie","family":"Whalen","sequence":"additional","affiliation":[{"name":"Cell and Developmental Biology, University of Illinois at Urbana-Champaign , Urbana, IL 61801, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0851-5423","authenticated-orcid":false,"given":"Brian","family":"Freeman","sequence":"additional","affiliation":[{"name":"Cell and Developmental Biology, University of Illinois at Urbana-Champaign , Urbana, IL 61801, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"175","published-online":{"date-parts":[[2026,10,1]]},"reference":[{"key":"2026100103070673800_RSTB20250266C1","doi-asserted-by":"crossref","first-page":"168615","DOI":"10.1016\/j.jmb.2024.168615","article-title":"Interplay of proteostasis capacity and protein aggregation: implications for cellular function and disease","volume":"436","author":"Hipp","year":"2024","journal-title":"J. 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Sci."},{"key":"2026100103070673800_RSTB20250266C56","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1016\/j.molcel.2019.03.012","article-title":"Dual role of ribosome-binding domain of NAC as a potent suppressor of protein aggregation and ageing-related proteinopathies","volume":"74","author":"Shen","year":"2019","journal-title":"Mol. Cell."},{"key":"2026100103070673800_RSTB20250266C57","doi-asserted-by":"crossref","first-page":"1632","DOI":"10.1007\/PL00012490","article-title":"Nascent-polypeptide-associated complex","volume":"59","author":"Rospert","year":"2002","journal-title":"Cell. Mol. Life Sci."},{"key":"2026100103070673800_RSTB20250266C58","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1021\/cb800059u","article-title":"Chain dynamics of nascent polypeptides emerging from the ribosome","volume":"3","author":"Ellis","year":"2008","journal-title":"ACS Chem. Biol."},{"key":"2026100103070673800_RSTB20250266C59","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1038\/23301","article-title":"Trigger factor and DnaK cooperate in folding of newly synthesized proteins","volume":"400","author":"Deuerling","year":"1999","journal-title":"Nature"},{"key":"2026100103070673800_RSTB20250266C60","doi-asserted-by":"crossref","first-page":"1442","DOI":"10.1016\/j.bbamcr.2013.11.007","article-title":"Chaperone networking facilitates protein targeting to the bacterial cytoplasmic membrane","volume":"1843","author":"Castani\u00e9-Cornet","year":"2014","journal-title":"Biochim. Biophys. 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Biol."},{"key":"2026100103070673800_RSTB20250266C89","doi-asserted-by":"crossref","first-page":"35194","DOI":"10.1074\/jbc.273.52.35194","article-title":"Hop as an adaptor in the heat shock protein 70 (Hsp70) and Hsp90 chaperone machinery","volume":"273","author":"Chen","year":"1998","journal-title":"J. Biol. Chem."},{"key":"2026100103070673800_RSTB20250266C90","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1016\/j.tcb.2018.10.004","article-title":"The Hsp70\u2013Hsp90 chaperone cascade in protein folding","volume":"29","author":"Mor\u00e1n","year":"2019","journal-title":"Trends Cell Biol."},{"key":"2026100103070673800_RSTB20250266C91","doi-asserted-by":"crossref","first-page":"8385","DOI":"10.1128\/MCB.02188-05","article-title":"The middle domain of Hsp90 acts as a discriminator between different types of client proteins","volume":"26","author":"Hawle","year":"2006","journal-title":"Mol. Cell. Biol."},{"key":"2026100103070673800_RSTB20250266C92","doi-asserted-by":"crossref","first-page":"168460","DOI":"10.1016\/j.jmb.2024.168460","article-title":"Establishing order through disorder by the Hsp90 molecular chaperone","volume":"436","author":"Babu","year":"2024","journal-title":"J. Mol. Biol."},{"key":"2026100103070673800_RSTB20250266C93","doi-asserted-by":"crossref","first-page":"2035","DOI":"10.1016\/j.molcel.2023.05.021","article-title":"The Hsp90 molecular chaperone governs client proteins by targeting intrinsically disordered regions","volume":"83","author":"Kolhe","year":"2023","journal-title":"Mol. Cell"},{"key":"2026100103070673800_RSTB20250266C94","doi-asserted-by":"crossref","first-page":"7288","DOI":"10.1074\/jbc.270.13.7288","article-title":"Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo","volume":"270","author":"Jakob","year":"1995","journal-title":"J. Biol. Chem."},{"key":"2026100103070673800_RSTB20250266C95","doi-asserted-by":"crossref","first-page":"2969","DOI":"10.1002\/j.1460-2075.1996.tb00660.x","article-title":"The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding","volume":"15","author":"Freeman","year":"1996","journal-title":"EMBO J."},{"key":"2026100103070673800_RSTB20250266C96","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1038\/348166a0","article-title":"Reduced levels of hsp90 compromise steroid receptor action in vivo","volume":"348","author":"Picard","year":"1990","journal-title":"Nature"},{"key":"2026100103070673800_RSTB20250266C97","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/S0092-8674(02)01250-3","article-title":"Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70","volume":"112","author":"Young","year":"2003","journal-title":"Cell"},{"key":"2026100103070673800_RSTB20250266C98","doi-asserted-by":"crossref","first-page":"4993","DOI":"10.1016\/j.jmb.2019.09.007","article-title":"The Hsp90 molecular chaperone regulates the transcription factor network controlling chromatin accessibility","volume":"431","author":"Gvozdenov","year":"2019","journal-title":"J. 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Lett."},{"key":"2026100103070673800_RSTB20250266C158","doi-asserted-by":"crossref","first-page":"28026","DOI":"10.1074\/jbc.M301048200","article-title":"Central role of the proteasome in senescence and survival of human fibroblasts: induction of a senescence-like phenotype upon its inhibition and resistance to stress upon its activation","volume":"278","author":"Chondrogianni","year":"2003","journal-title":"J. Biol. Chem."},{"key":"2026100103070673800_RSTB20250266C159","doi-asserted-by":"crossref","first-page":"1208","DOI":"10.1016\/j.freeradbiomed.2005.06.009","article-title":"Protein oxidation and degradation during postmitotic senescence","volume":"39","author":"Grune","year":"2005","journal-title":"Free Radical Biol. Med."},{"key":"2026100103070673800_RSTB20250266C160","doi-asserted-by":"crossref","first-page":"748","DOI":"10.1016\/j.mad.2009.09.004","article-title":"Inverse correlation of protein oxidation and proteasome activity in liver and lung","volume":"130","author":"Breusing","year":"2009","journal-title":"Mech. 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Biol."},{"key":"2026100103070673800_RSTB20250266C164","doi-asserted-by":"crossref","first-page":"2672","DOI":"10.1096\/fj.06-6751com","article-title":"Ageing perturbs 26S proteasome assembly in Drosophila melanogaster","volume":"21","author":"Vernace","year":"2007","journal-title":"FASEB J."},{"key":"2026100103070673800_RSTB20250266C165","doi-asserted-by":"crossref","first-page":"102415","DOI":"10.1016\/j.jbc.2022.102415","article-title":"Hyperactivation of the proteasome in Caenorhabditis elegans protects against proteotoxic stress and extends lifespan","volume":"298","author":"Anderson","year":"2022","journal-title":"J. Biol. Chem."},{"key":"2026100103070673800_RSTB20250266C166","first-page":"515","article-title":"Identification and functional clustering of global gene expression differences between human age-related cataract and clear lenses and aged human lenses","volume":"9","author":"Hawse","year":"2003","journal-title":"Mol. 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Biophys."},{"key":"2026100103070673800_RSTB20250266C169","doi-asserted-by":"crossref","first-page":"2990","DOI":"10.1038\/emboj.2011.195","article-title":"EGF signalling activates the ubiquitin proteasome system to modulate C. elegans lifespan","volume":"30","author":"Liu","year":"2011","journal-title":"EMBO J."},{"key":"2026100103070673800_RSTB20250266C170","doi-asserted-by":"crossref","first-page":"e32835","DOI":"10.1371\/journal.pone.0032835","article-title":"Mutation in E1, the ubiquitin activating enzyme, reduces Drosophila lifespan and results in motor impairment","volume":"8","author":"Liu","year":"2013","journal-title":"PLoS One"},{"key":"2026100103070673800_RSTB20250266C171","first-page":"8638","article-title":"Parkin overexpression during ageing reduces proteotoxicity, alters mitochondrial dynamics, and extends lifespan","volume-title":"Proc. Natl Acad. Sci. 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Neurol."},{"key":"2026100103070673800_RSTB20250266C180","doi-asserted-by":"crossref","first-page":"1184","DOI":"10.1038\/ng1884","article-title":"Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase","volume":"38","author":"Ramirez","year":"2006","journal-title":"Nat. Genet."},{"key":"2026100103070673800_RSTB20250266C181","doi-asserted-by":"crossref","first-page":"6926","DOI":"10.1523\/JNEUROSCI.0800-08.2008","article-title":"Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease","volume":"28","author":"Boland","year":"2008","journal-title":"J. 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