Dennerlein, Sven

[["dc.bibliographiccitation.artnumber","e9561"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","EMBO Molecular Medicine"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Mohanraj, Karthik"],["dc.contributor.author","Wasilewski, Michal"],["dc.contributor.author","Benincá, Cristiane"],["dc.contributor.author","Cysewski, Dominik"],["dc.contributor.author","Poznanski, Jaroslaw"],["dc.contributor.author","Sakowska, Paulina"],["dc.contributor.author","Bugajska, Zaneta"],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Fernandez‐Vizarra, Erika"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Dadlez, Michal"],["dc.contributor.author","Zeviani, Massimo"],["dc.contributor.author","Chacinska, Agnieszka"],["dc.date.accessioned","2019-07-09T11:51:37Z"],["dc.date.available","2019-07-09T11:51:37Z"],["dc.date.issued","2019"],["dc.description.abstract","Nuclear and mitochondrial genome mutations lead to various mitochondrial diseases, many of which affect the mitochondrial respiratory chain. The proteome of the intermembrane space (IMS) of mitochondria consists of several important assembly factors that participate in the biogenesis of mitochondrial respiratory chain complexes. The present study comprehensively analyzed a recently identified IMS protein cytochrome c oxidase assembly factor 7 (COA7), or RESpiratory chain Assembly 1 (RESA1) factor that is associated with a rare form of mitochondrial leukoencephalopathy and complex IV deficiency. We found that COA7 requires the mitochondrial IMS import and assembly (MIA) pathway for efficient accumulation in the IMS. We also found that pathogenic mutant versions of COA7 are imported slower than the wild‐type protein, and mislocalized proteins are degraded in the cytosol by the proteasome. Interestingly, proteasome inhibition rescued both the mitochondrial localization of COA7 and complex IV activity in patient‐derived fibroblasts. We propose proteasome inhibition as a novel therapeutic approach for a broad range of mitochondrial pathologies associated with the decreased levels of mitochondrial proteins."],["dc.identifier.doi","10.15252/emmm.201809561"],["dc.identifier.pmid","30885959"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16155"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59974"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/64"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/322424/EU//MITCARE"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/339580/EU//MITRAC"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P13: Protein Transport über den mitochondrialen Carrier Transportweg"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","540"],["dc.title","Inhibition of proteasome rescues a pathogenic variant of respiratory chain assembly factor COA7"],["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","323"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta"],["dc.bibliographiccitation.lastpage","333"],["dc.bibliographiccitation.volume","1865"],["dc.contributor.author","Lorenzi, Isotta"],["dc.contributor.author","Oeljeklaus, Silke"],["dc.contributor.author","Aich, Abhishek"],["dc.contributor.author","Ronsör, Christin"],["dc.contributor.author","Callegari, Sylvie"],["dc.contributor.author","Dudek, Jan"],["dc.contributor.author","Warscheid, Bettina"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2018-01-09T14:12:01Z"],["dc.date.available","2018-01-09T14:12:01Z"],["dc.date.issued","2018"],["dc.description.abstract","The three mitochondrial-encoded proteins, COX1, COX2, and COX3, form the core of the cytochrome c oxidase. Upon synthesis, COX2 engages with COX20 in the inner mitochondrial membrane, a scaffold protein that recruits metallochaperones for copper delivery to the CuA-Site of COX2. Here we identified the human protein, TMEM177 as a constituent of the COX20 interaction network. Loss or increase in the amount of TMEM177 affects COX20 abundance leading to reduced or increased COX20 levels respectively. TMEM177 associates with newly synthesized COX2 and SCO2 in a COX20-dependent manner. Our data shows that by unbalancing the amount of TMEM177, newly synthesized COX2 accumulates in a COX20-associated state. We conclude that TMEM177 promotes assembly of COX2 at the level of CuA-site formation."],["dc.identifier.doi","10.1016/j.bbamcr.2017.11.010"],["dc.identifier.pmid","29154948"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15209"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11600"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/16"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P13: Protein Transport über den mitochondrialen Carrier Transportweg"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.rights","CC BY-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nd/4.0"],["dc.title","The mitochondrial TMEM177 associates with COX20 during COX2 biogenesis"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","16913"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Mandad, Sunit"],["dc.contributor.author","Rahman, Raza-Ur"],["dc.contributor.author","Centeno, Tonatiuh Pena"],["dc.contributor.author","Vidal, Ramon O."],["dc.contributor.author","Wildhagen, Hanna"],["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","Kirli, Koray"],["dc.contributor.author","Benito, Eva"],["dc.contributor.author","Fischer, André"],["dc.contributor.author","Yousefi, Roya Y."],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Feußner, Ivo"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Bonn, Stefan"],["dc.contributor.author","Rizzoli, Silvio O."],["dc.contributor.author","Fornasiero, Eugenio F."],["dc.date.accessioned","2019-07-09T11:50:21Z"],["dc.date.available","2019-07-09T11:50:21Z"],["dc.date.issued","2018"],["dc.description.abstract","The homeostasis of the proteome depends on the tight regulation of the mRNA and protein abundances, of the translation rates, and of the protein lifetimes. Results from several studies on prokaryotes or eukaryotic cell cultures have suggested that protein homeostasis is connected to, and perhaps regulated by, the protein and the codon sequences. However, this has been little investigated for mammals in vivo. Moreover, the link between the coding sequences and one critical parameter, the protein lifetime, has remained largely unexplored, both in vivo and in vitro. We tested this in the mouse brain, and found that the percentages of amino acids and codons in the sequences could predict all of the homeostasis parameters with a precision approaching experimental measurements. A key predictive element was the wobble nucleotide. G-/C-ending codons correlated with higher protein lifetimes, protein abundances, mRNA abundances and translation rates than A-/U-ending codons. Modifying the proportions of G-/C-ending codons could tune these parameters in cell cultures, in a proof-of-principle experiment. We suggest that the coding sequences are strongly linked to protein homeostasis in vivo, albeit it still remains to be determined whether this relation is causal in nature."],["dc.identifier.doi","10.1038/s41598-018-35277-8"],["dc.identifier.pmid","30443017"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15918"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59754"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/209"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/44"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/339580/EU//MITRAC"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/614765/EU//NEUROMOLANATOMY"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P09: Proteinsortierung in der Synapse: Prinzipien und molekulare Organisation"],["dc.relation.issn","2045-2322"],["dc.relation.workinggroup","RG A. Fischer (Epigenetics and Systems Medicine in Neurodegenerative Diseases)"],["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","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","The codon sequences predict protein lifetimes and other parameters of the protein life cycle in the mouse brain"],["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","1570"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","1580"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Bareth, Bettina"],["dc.contributor.author","Nikolov, Miroslav"],["dc.contributor.author","Lorenzi, Isotta"],["dc.contributor.author","Hildenbeutel, Markus"],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Helbig, Christin"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Ott, Martin"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.editor","Fox, Thomas D."],["dc.date.accessioned","2020-12-10T18:16:05Z"],["dc.date.available","2020-12-10T18:16:05Z"],["dc.date.issued","2016"],["dc.description.abstract","The mitochondrial cytochrome c oxidase assembles in the inner membrane from subunits of dual genetic origin. The assembly process of the enzyme is initiated by membrane insertion of the mitochondria-encoded Cox1 subunit. During complex maturation, transient assembly intermediates, consisting of structural subunits and specialized chaperone-like assembly factors, are formed. In addition, cofactors such as heme and copper have to be inserted into the nascent complex. To regulate the assembly process, the availability of Cox1 is under control of a regulatory feedback cycle in which translation of COX1 mRNA is stalled when assembly intermediates of Cox1 accumulate through inactivation of the translational activator Mss51. Here we isolate a cytochrome c oxidase assembly intermediate in preparatory scale from coa1 Delta. mutant cells, using Mss51 as bait. We demonstrate that at this stage of assembly, the complex has not yet incorporated the heme a cofactors. Using quantitative mass spectrometry, we define the protein composition of the assembly intermediate and unexpectedly identify the putative methyltransferase Oms1 as a constituent. Our analyses show that Oms1 participates in cytochrome c oxidase assembly by stabilizing newly synthesized Cox1."],["dc.identifier.doi","10.1091/mbc.E15-12-0811"],["dc.identifier.eissn","1939-4586"],["dc.identifier.gro","3141687"],["dc.identifier.isi","000376456800004"],["dc.identifier.issn","1059-1524"],["dc.identifier.pmid","27030670"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75047"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1939-4586"],["dc.relation.issn","1059-1524"],["dc.title","Oms1 associates with cytochrome c oxidase assembly intermediates to stabilize newly synthesized Cox1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","68"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Immunity"],["dc.bibliographiccitation.lastpage","83.e6"],["dc.bibliographiccitation.volume","54"],["dc.contributor.author","Almeida, Luís"],["dc.contributor.author","Dhillon-LaBrooy, Ayesha"],["dc.contributor.author","Castro, Carla N."],["dc.contributor.author","Adossa, Nigatu"],["dc.contributor.author","Carriche, Guilhermina M."],["dc.contributor.author","Guderian, Melanie"],["dc.contributor.author","Lippens, Saskia"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Hesse, Christina"],["dc.contributor.author","Lambrecht, Bart N."],["dc.contributor.author","Berod, Luciana"],["dc.contributor.author","Schauser, Leif"],["dc.contributor.author","Blazar, Bruce R."],["dc.contributor.author","Kalesse, Markus"],["dc.contributor.author","Müller, Rolf"],["dc.contributor.author","Moita, Luís F."],["dc.contributor.author","Sparwasser, Tim"],["dc.date.accessioned","2021-04-14T08:30:29Z"],["dc.date.available","2021-04-14T08:30:29Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1016/j.immuni.2020.11.001"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83254"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.issn","1074-7613"],["dc.title","Ribosome-Targeting Antibiotics Impair T Cell Effector Function and Ameliorate Autoimmunity by Blocking Mitochondrial Protein Synthesis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4128"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","4137"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Bareth, Bettina"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Nikolov, Miroslav"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:47:07Z"],["dc.date.available","2017-09-07T11:47:07Z"],["dc.date.issued","2013"],["dc.description.abstract","Cox1, the core subunit of the cytochrome c oxidase, receives two heme a cofactors during assembly of the 13-subunit enzyme complex. However, at which step of the assembly process and how heme is inserted into Cox1 have remained an enigma. Shy1, the yeast SURF1 homolog, has been implicated in heme transfer to Cox1, whereas the heme a synthase, Cox15, catalyzes the final step of heme a synthesis. Here we performed a comprehensive analysis of cytochrome c oxidase assembly intermediates containing Shy1. Our analyses suggest that Cox15 displays a role in cytochrome c oxidase assembly, which is independent of its functions as the heme a synthase. Cox15 forms protein complexes with Shy1 and also associates with Cox1-containing complexes independently of Shy1 function. These findings indicate that Shy1 does not serve as a mobile heme carrier between the heme a synthase and maturing Cox1 but rather cooperates with Cox15 for heme transfer and insertion in early assembly intermediates of cytochrome c oxidase."],["dc.identifier.doi","10.1128/MCB.00747-13"],["dc.identifier.gro","3142276"],["dc.identifier.isi","000324912000015"],["dc.identifier.pmid","23979592"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6487"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1098-5549"],["dc.relation.issn","0270-7306"],["dc.title","The Heme a Synthase Cox15 Associates with Cytochrome c Oxidase Assembly Intermediates during Cox1 Maturation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","598"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","614"],["dc.bibliographiccitation.volume","218"],["dc.contributor.author","Richter, Frank"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Nikolov, Miroslav"],["dc.contributor.author","Jans, Daniel C."],["dc.contributor.author","Naumenko, Nataliia"],["dc.contributor.author","Aich, Abhishek"],["dc.contributor.author","MacVicar, Thomas"],["dc.contributor.author","Linden, Andreas"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Langer, Thomas"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2019-07-09T11:50:27Z"],["dc.date.available","2019-07-09T11:50:27Z"],["dc.date.issued","2019"],["dc.description.abstract","The mitochondrial presequence translocation machinery (TIM23 complex) is conserved between the yeast Saccharomyces cerevisiae and humans; however, functional characterization has been mainly performed in yeast. Here, we define the constituents of the human TIM23 complex using mass spectrometry and identified ROMO1 as a new translocase constituent with an exceptionally short half-life. Analyses of a ROMO1 knockout cell line revealed aberrant inner membrane structure and altered processing of the GTPase OPA1. We show that in the absence of ROMO1, mitochondria lose the inner membrane YME1L protease, which participates in OPA1 processing and ROMO1 turnover. While ROMO1 is dispensable for general protein import along the presequence pathway, we show that it participates in the dynamics of TIM21 during respiratory chain biogenesis and is specifically required for import of YME1L. This selective import defect can be linked to charge distribution in the unusually long targeting sequence of YME1L. Our analyses establish an unexpected link between mitochondrial protein import and inner membrane protein quality control."],["dc.identifier.doi","10.1083/jcb.201806093"],["dc.identifier.pmid","30598479"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15943"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59776"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/339580/EU//MITRAC"],["dc.relation.issn","1540-8140"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","ROMO1 is a constituent of the human presequence translocase required for YME1L protease import"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","712"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Trends in Cell Biology"],["dc.bibliographiccitation.lastpage","721"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Wang, Cong"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2018-01-18T11:02:55Z"],["dc.date.available","2018-01-18T11:02:55Z"],["dc.date.issued","2017"],["dc.description.abstract","Mitochondria maintained a genome during evolution to synthesize core subunits of the oxidative phosphorylation system. Expression of the mitochondrial genome requires intraorganellar replication, transcription, and translation. Membrane-associated ribosomes translate mitochondrial-encoded proteins and facilitate co-translational insertion of newly synthesized polypeptides into the inner membrane. Considering that mitochondrial-encoded proteins assemble with imported, nuclear-encoded proteins into enzyme complexes of the oxidative phosphorylation system, it is expected that expression of mitochondrial genes should adapt to the availability of their nuclear-encoded partners. Recent work shows that mitochondrial translation is influenced by the cellular environment. We discuss how mitochondrial translation is affected by the cellular environment and propose models of translational plasticity that modulate mitochondrial translation in response to the availability of imported proteins."],["dc.identifier.doi","10.1016/j.tcb.2017.05.004"],["dc.identifier.pmid","28606446"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11744"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1879-3088"],["dc.subject","OXPHOS assembly; mitochondria; mitochondrial ribosome; respiratory chain; translation regulation"],["dc.title","Plasticity of Mitochondrial Translation"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["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.artnumber","e32572"],["dc.bibliographiccitation.journal","eLife"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Aich, Abhishek"],["dc.contributor.author","Wang, Cong"],["dc.contributor.author","Chowdhury, Arpita"],["dc.contributor.author","Ronsör, Christin"],["dc.contributor.author","Pacheu-Grau, David"],["dc.contributor.author","Richter-Dennerlein, Ricarda"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2018-05-03T09:03:52Z"],["dc.date.accessioned","2021-10-27T13:21:07Z"],["dc.date.available","2018-05-03T09:03:52Z"],["dc.date.available","2021-10-27T13:21:07Z"],["dc.date.issued","2018"],["dc.description.abstract","Cytochrome c oxidase of the mitochondrial oxidative phosphorylation system reduces molecular oxygen with redox equivalent-derived electrons. The conserved mitochondrial-encoded COX1- and COX2-subunits are the heme- and copper-center containing core subunits that catalyze water formation. COX1 and COX2 initially follow independent biogenesis pathways creating assembly modules with subunit-specific, chaperone-like assembly factors that assist in redox centers formation. Here, we find that COX16, a protein required for cytochrome c oxidase assembly, interacts specifically with newly synthesized COX2 and its copper center-forming metallochaperones SCO1, SCO2, and COA6. The recruitment of SCO1 to the COX2-module is COX16- dependent and patient-mimicking mutations in SCO1 affect interaction with COX16. These findings implicate COX16 in CuA-site formation. Surprisingly, COX16 is also found in COX1-containing assembly intermediates and COX2 recruitment to COX1. We conclude that COX16 participates in merging the COX1 and COX2 assembly lines."],["dc.identifier.doi","10.7554/eLife.32572"],["dc.identifier.gro","3142446"],["dc.identifier.pmid","29381136"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15212"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/91995"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/200"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.notes.status","final"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A06: Molekulare Grundlagen mitochondrialer Kardiomyopathien"],["dc.relation.issn","2050-084X"],["dc.relation.orgunit","Universitätsmedizin Göttingen"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","COX16 promotes COX2 metallation and assembly during respiratory complex IV biogenesis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]