Raimundo, Nuno

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Sathyanarayanan, Udhayabhaskar"],["dc.contributor.author","Musa, Marina"],["dc.contributor.author","Bou Dib, Peter"],["dc.contributor.author","Raimundo, Nuno"],["dc.contributor.author","Milosevic, Ira"],["dc.contributor.author","Krisko, Anita"],["dc.date.accessioned","2021-04-14T08:31:49Z"],["dc.date.available","2021-04-14T08:31:49Z"],["dc.date.issued","2020"],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.1038/s41467-020-19104-1"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83720"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","2041-1723"],["dc.relation.orgunit","Abteilung Experimentelle Neurodegeneration"],["dc.rights","CC BY 4.0"],["dc.title","ATP hydrolysis by yeast Hsp104 determines protein aggregate dissolution and size in vivo"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","994"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Aging Cell"],["dc.bibliographiccitation.lastpage","1005"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Perić, Matea"],["dc.contributor.author","Lovrić, Anita"],["dc.contributor.author","Šarić, Ana"],["dc.contributor.author","Musa, Marina"],["dc.contributor.author","Bou Dib, Peter"],["dc.contributor.author","Rudan, Marina"],["dc.contributor.author","Nikolić, Andrea"],["dc.contributor.author","Sobočanec, Sandra"],["dc.contributor.author","Mikecin, Ana-Matea"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Milošević, Ira"],["dc.contributor.author","Vlahoviček, Kristian"],["dc.contributor.author","Raimundo, Nuno"],["dc.contributor.author","Kriško, Anita"],["dc.date.accessioned","2019-07-09T11:44:59Z"],["dc.date.available","2019-07-09T11:44:59Z"],["dc.date.issued","2017"],["dc.description.abstract","Protein quality control mechanisms, required for normal cellular functioning, encompass multiple functions related to protein production and maintenance. However, the existence of communication between proteostasis and metabolic networks and its underlying mechanisms remain elusive. Here, we report that enhanced chaperone activity and consequent improved proteostasis are sensed by TORC1 via the activity of Hsp82. Chaperone enrichment decreases the level of Hsp82, which deactivates TORC1 and leads to activation of Snf1/AMPK, regardless of glucose availability. This mechanism culminates in the extension of yeast replicative lifespan (RLS) that is fully reliant on both TORC1 deactivation and Snf1/AMPK activation. Specifically, we identify oxygen consumption increase as the downstream effect of Snf1 activation responsible for the entire RLS extension. Our results set a novel paradigm for the role of proteostasis in aging: modulation of the misfolded protein level can affect cellular metabolic features as well as mitochondrial activity and consequently modify lifespan. The described mechanism is expected to open new avenues for research of aging and age-related diseases."],["dc.identifier.doi","10.1111/acel.12623"],["dc.identifier.pmid","28613034"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14988"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59133"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","315997"],["dc.relation","316289"],["dc.relation","337327"],["dc.relation.issn","1474-9726"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","612"],["dc.title","TORC1-mediated sensing of chaperone activity alters glucose metabolism and extends lifespan."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","28751"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Peric, Matea"],["dc.contributor.author","Dib, Peter Bou"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Musa, Marina"],["dc.contributor.author","Rudan, Marina"],["dc.contributor.author","Lovric, Anita"],["dc.contributor.author","Nikolic, Andrea"],["dc.contributor.author","Saric, Ana"],["dc.contributor.author","Sobocanec, Sandra"],["dc.contributor.author","Macak, Zeljka"],["dc.contributor.author","Raimundo, Nuno"],["dc.contributor.author","Krisko, Anita"],["dc.date.accessioned","2018-11-07T10:12:38Z"],["dc.date.available","2018-11-07T10:12:38Z"],["dc.date.issued","2016"],["dc.description.abstract","In cells living under optimal conditions, protein folding defects are usually prevented by the action of chaperones. Here, we investigate the cell-wide consequences of loss of chaperone function in cytosol, mitochondria or the endoplasmic reticulum (ER) in budding yeast. We find that the decline in chaperone activity in each compartment results in loss of respiration, demonstrating the dependence of mitochondrial activity on cell-wide proteostasis. Furthermore, each chaperone deficiency triggers a response, presumably via the communication among the folding environments of distinct cellular compartments, termed here the cross-organelle stress response (CORE). The proposed CORE pathway encompasses activation of protein conformational maintenance machineries, antioxidant enzymes, and metabolic changes simultaneously in the cytosol, mitochondria, and the ER. CORE induction extends replicative and chronological lifespan in budding yeast, highlighting its protective role against moderate proteotoxicity and its consequences such as the decline in respiration. Our findings accentuate that organelles do not function in isolation, but are integrated in a functional crosstalk, while also highlighting the importance of organelle communication in aging and age-related diseases."],["dc.identifier.doi","10.1038/srep28751"],["dc.identifier.isi","000378491700002"],["dc.identifier.pmid","27346163"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13472"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40278"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","2045-2322"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Crosstalk between cellular compartments protects against proteotoxicity and extends lifespan"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]