Dennerlein, Sven

[["dc.bibliographiccitation.artnumber","4230"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Fornasiero, Eugenio F."],["dc.contributor.author","Mandad, Sunit"],["dc.contributor.author","Wildhagen, Hanna"],["dc.contributor.author","Alevra, Mihai"],["dc.contributor.author","Rammner, Burkhard"],["dc.contributor.author","Keihani, Sarva"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Urban, Inga"],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Sakib, M. Sadman"],["dc.contributor.author","Fard, Maryam K."],["dc.contributor.author","Kirli, Koray"],["dc.contributor.author","Centeno, Tonatiuh Pena"],["dc.contributor.author","Vidal, Ramon O."],["dc.contributor.author","Rahman, Raza-Ur"],["dc.contributor.author","Benito, Eva"],["dc.contributor.author","Fischer, André"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Bonn, Stefan"],["dc.contributor.author","Simons, Mikael"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Rizzoli, Silvio O."],["dc.date.accessioned","2019-07-09T11:46:03Z"],["dc.date.available","2019-07-09T11:46:03Z"],["dc.date.issued","2018"],["dc.description.abstract","The turnover of brain proteins is critical for organism survival, and its perturbations are linked to pathology. Nevertheless, protein lifetimes have been difficult to obtain in vivo. They are readily measured in vitro by feeding cells with isotopically labeled amino acids, followed by mass spectrometry analyses. In vivo proteins are generated from at least two sources: labeled amino acids from the diet, and non-labeled amino acids from the degradation of pre-existing proteins. This renders measurements difficult. Here we solved this problem rigorously with a workflow that combines mouse in vivo isotopic labeling, mass spectrometry, and mathematical modeling. We also established several independent approaches to test and validate the results. This enabled us to measure the accurate lifetimes of ~3500 brain proteins. The high precision of our data provided a large set of biologically significant observations, including pathway-, organelle-, organ-, or cell-specific effects, along with a comprehensive catalog of extremely long-lived proteins (ELLPs)."],["dc.identifier.doi","10.1038/s41467-018-06519-0"],["dc.identifier.pmid","30315172"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15388"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59372"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/42"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/41"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.intern","In goescholar not merged with http://resolver.sub.uni-goettingen.de/purl?gs-1/15611 but duplicate"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/339580/EU//MITRAC"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/614765/EU//NEUROMOLANATOMY"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P09: Proteinsortierung in der Synapse: Prinzipien und molekulare Organisation"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | A03: Dynamische Analyse der Remodellierung der extrazellulären Matrix (ECM) als Mechanismus der Synapsenorganisation und Plastizität"],["dc.relation.issn","2041-1723"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.relation.workinggroup","RG Rizzoli (Quantitative Synaptology in Space and Time)"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","573"],["dc.subject.ddc","612"],["dc.title","Precisely measured protein lifetimes in the mouse brain reveal differences across tissues and subcellular fractions."],["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"]]