Dudek, Jan

[["dc.bibliographiccitation.artnumber","479"],["dc.bibliographiccitation.journal","Frontiers in Physiology"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Can, Karolina"],["dc.contributor.author","Menzfeld, Christiane"],["dc.contributor.author","Rinne, Lena"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Kügler, Sebastian"],["dc.contributor.author","Golubiani, Gocha"],["dc.contributor.author","Dudek, Jan"],["dc.contributor.author","Müller, Michael"],["dc.date.accessioned","2019-07-09T11:51:15Z"],["dc.date.available","2019-07-09T11:51:15Z"],["dc.date.issued","2019"],["dc.description.abstract","Rett syndrome (RTT), an X chromosome-linked neurodevelopmental disorder affecting almost exclusively females, is associated with various mitochondrial alterations. Mitochondria are swollen, show altered respiratory rates, and their inner membrane is leaking protons. To advance the understanding of these disturbances and clarify their link to redox impairment and oxidative stress, we assessed mitochondrial respiration in defined brain regions and cardiac tissue of male wildtype (WT) and MeCP2-deficient (Mecp2-/y) mice. Also, we quantified for the first time neuronal redox-balance with subcellular resolution in cytosol and mitochondrial matrix. Quantitative roGFP1 redox imaging revealed more oxidized conditions in the cytosol of Mecp2-/y hippocampal neurons than in WT neurons. Furthermore, cytosol and mitochondria of Mecp2-/y neurons showed exaggerated redox-responses to hypoxia and cell-endogenous reactive oxygen species (ROS) formation. Biochemical analyzes exclude disease-related increases in mitochondrial mass in Mecp2-/y hippocampus and cortex. Protein levels of complex I core constituents were slightly lower in Mecp2-/y hippocampus and cortex than in WT; those of complex V were lower in Mecp2-/y cortex. Respiratory supercomplex-formation did not differ among genotypes. Yet, supplied with the complex II substrate succinate, mitochondria of Mecp2-/y cortex and hippocampus consumed more O2 than WT. Furthermore, mitochondria from Mecp2-/y hippocampus and cortex mediated an enhanced oxidative burden. In conclusion, we further advanced the molecular understanding of mitochondrial dysfunction in RTT. Intensified mitochondrial O2 consumption, increased mitochondrial ROS generation and disturbed redox balance in mitochondria and cytosol may represent a causal chain, which provokes dysregulated proteins, oxidative tissue damage, and contributes to neuronal network dysfunction in RTT."],["dc.identifier.doi","10.3389/fphys.2019.00479"],["dc.identifier.pmid","31114506"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16085"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59907"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/12"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | A06: Mitochondrienfunktion und -umsatz in Synapsen"],["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","573"],["dc.subject.ddc","612"],["dc.title","Neuronal Redox-Imbalance in Rett Syndrome Affects Mitochondria as Well as Cytosol, and Is Accompanied by Intensified Mitochondrial O2 Consumption and ROS Release"],["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.firstpage","38047"],["dc.bibliographiccitation.issue","36"],["dc.bibliographiccitation.journal","Journal of biological chemistry"],["dc.bibliographiccitation.lastpage","38054"],["dc.bibliographiccitation.volume","279"],["dc.contributor.author","Li, Yanfeng"],["dc.contributor.author","Dudek, Jan"],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Pfanner, Nikolaus"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Voos, Wolfgang"],["dc.date.accessioned","2017-09-07T11:43:13Z"],["dc.date.available","2017-09-07T11:43:13Z"],["dc.date.issued","2004"],["dc.description.abstract","Transport of preproteins into the mitochondrial matrix requires the presequence translocase of the inner membrane (TIM23 complex) and the presequence translocase-associated motor (PAM). The motor consists of five essential subunits, the mitochondrial heat shock protein 70 (mtHsp70) and four cochaperones, the nucleotide exchange-factor Mge1, the translocase-associated fulcrum Tim44, the J-protein Pam18, and Pam16. Pam16 forms a complex with Pam18 and displays similarity to J-proteins but lacks the canonical tripeptide motif His-Pro-Asp (HPD). We report that Pam16 does not function as a typical J-domain protein but, rather, antagonizes the function of Pam18. Pam16 specifically inhibits the Pam18-mediated stimulation of the ATPase activity of mtHsp70. The inclusion of the HPD motif in Pam16 does not confer the ability to stimulate mtHsp70 activity. Pam16-HPD fully substitutes for wild-type Pam16 in vitro and in vivo but is not able to replace Pam18. Pam16 represents a new type of cochaperone that controls the stimulatory effect of the J-protein Pam18 and regulates the interaction of mtHsp70 with precursor proteins during import into mitochondria."],["dc.identifier.doi","10.1074/jbc.M404319200"],["dc.identifier.gro","3143946"],["dc.identifier.isi","000223554600099"],["dc.identifier.pmid","15218029"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1516"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0021-9258"],["dc.title","The presequence translocase-associated protein import motor of mitochondria"],["dc.title.subtitle","Pam16 functions in an antagonistic manner to Pam18"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","817"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","829"],["dc.bibliographiccitation.volume","120"],["dc.contributor.author","Chacinska, Agnieszka"],["dc.contributor.author","Lind, Maria"],["dc.contributor.author","Frazier, Ann E."],["dc.contributor.author","Dudek, Jan"],["dc.contributor.author","Meisinger, Chris"],["dc.contributor.author","Geissler, Andreas"],["dc.contributor.author","Sickmann, Albert"],["dc.contributor.author","Meyer, Helmut E."],["dc.contributor.author","Truscott, Kaye N."],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Pfanner, Nikolaus"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:54:31Z"],["dc.date.available","2017-09-07T11:54:31Z"],["dc.date.issued","2005"],["dc.description.abstract","The presequence translocase of the inner mitochondrial membrane (TIM23 complex) operates at a central junction of protein import. It accepts preproteins from the outer membrane TOM complex and directs them to inner membrane insertion or, in cooperation with the presequence translocase-associated motor (PAM), to the matrix. Little is known of how the TIM23 complex coordinates these tasks. We have identified Tim21 (YGR033c) that interacts with the TOM complex. Tim21 is specific for a TIM23 form that cooperates with TOM and promotes inner membrane insertion. Protein translocation into the matrix requires a switch to a Tim21-free, PAM bound presequence translocase. Tim17 is crucial for the switch by performing two separable functions: promotion of inner membrane insertion and binding of Pam18 to form the functional TIM-PAM complex. Thus, the presequence translocase is not a static complex but switches between TOM tethering and PAM binding in a reaction cycle involving Tim21 and Tim17."],["dc.identifier.doi","10.1016/j.cell.2005.01.011"],["dc.identifier.gro","3143878"],["dc.identifier.isi","000228067500011"],["dc.identifier.pmid","15797382"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1440"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0092-8674"],["dc.title","Mitochondrial presequence translocase: Switching between TOM tethering and motor recruitment involves Tim21 and Tim17"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","226"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","233"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Frazier, Ann E."],["dc.contributor.author","Dudek, Jan"],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Voos, W."],["dc.contributor.author","Li, Y. F."],["dc.contributor.author","Lind, Maria"],["dc.contributor.author","Meisinger, Chris"],["dc.contributor.author","Geissler, A."],["dc.contributor.author","Sickmann, Albert"],["dc.contributor.author","Meyer, Helmut E."],["dc.contributor.author","Bilanchone, V."],["dc.contributor.author","Cumsky, M. G."],["dc.contributor.author","Truscott, Kaye N."],["dc.contributor.author","Pfanner, Nikolaus"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:43:59Z"],["dc.date.available","2017-09-07T11:43:59Z"],["dc.date.issued","2004"],["dc.description.abstract","Mitochondrial preproteins destined for the matrix are translocated by two channel-forming transport machineries, the translocase of the outer membrane and the presequence translocase of the inner membrane. The presequence translocase-associated protein import motor (PAM) contains four essential subunits: the matrix heat shock protein 70 (mtHsp70) and its three cochaperones Mge1, Tim44 and Pam18. Here we report that the PAM contains a fifth essential subunit, Pam16 ( encoded by Saccharomyces cerevisiae YJL104W), which is selectively required for preprotein translocation into the matrix, but not for protein insertion into the inner membrane. Pam16 interacts with Pam18 and is needed for the association of Pam18 with the presequence translocase and for formation of a mtHsp70 Tim44 complex. Thus, Pam16 is a newly identified type of motor subunit and is required to promote a functional PAM reaction cycle, thereby driving preprotein import into the matrix."],["dc.identifier.doi","10.1038/nsmb735"],["dc.identifier.gro","3144008"],["dc.identifier.isi","000220281100012"],["dc.identifier.pmid","14981507"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1585"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: NIGMS NIH HHS [GM 57017]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1545-9985"],["dc.title","Pam16 has an essential role in the mitochondrial protein import motor"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","274"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],["dc.bibliographiccitation.lastpage","285"],["dc.bibliographiccitation.volume","1833"],["dc.contributor.author","Dudek, Jan"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","van der Laan, Martin"],["dc.date.accessioned","2017-09-07T11:48:18Z"],["dc.date.available","2017-09-07T11:48:18Z"],["dc.date.issued","2013"],["dc.description.abstract","Most mitochondrial proteins are encoded in the nucleus. They are synthesized as precursor forms in the cytosol and must be imported into mitochondria with the help of different protein translocases. Distinct import signals within precursors direct each protein to the mitochondrial surface and subsequently onto specific transport routes to its final destination within these organelles. In this review we highlight common principles of mitochondrial protein import and address different mechanisms of protein integration into mitochondrial membranes. Over the last years it has become clear that mitochondrial protein translocases are not independently operating units, but in fact closely cooperate with each other. We discuss recent studies that indicate how the pathways for mitochondrial protein biogenesis are embedded into a functional network of various other physiological processes, such as energy metabolism, signal transduction, and maintenance of mitochondrial morphology. This article is part of a Special Issue entitled: Protein Import and Quality Control in Mitochondria and Plastids. (C)2012 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.bbamcr.2012.05.028"],["dc.identifier.gro","3142399"],["dc.identifier.isi","000314002000005"],["dc.identifier.pmid","22683763"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7852"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0167-4889"],["dc.title","Mitochondrial protein import: Common principles and physiological networks"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","806"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Stem Cell Research"],["dc.bibliographiccitation.lastpage","819"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Dudek, Jan"],["dc.contributor.author","Cheng, I-Fen"],["dc.contributor.author","Balleininger, Martina"],["dc.contributor.author","Vaz, Frederic M."],["dc.contributor.author","Streckfuss-Bömeke, Katrin"],["dc.contributor.author","Hübscher, Daniela"],["dc.contributor.author","Vukotic, Milena"],["dc.contributor.author","Wanders, Ronald J. A."],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Guan, Kaomei"],["dc.date.accessioned","2017-09-07T11:47:37Z"],["dc.date.available","2017-09-07T11:47:37Z"],["dc.date.issued","2013"],["dc.description.abstract","Barth syndrome (BTHS) patients carrying mutations in tafazzin (TAZ1), which is involved in the final maturation of cardiolipin, present with dilated cardiomyopathy, skeletal myopathy, growth retardation and neutropenia. To study how mitochondrial function is impaired in BTHS patients, we generated induced pluripotent stem cells (iPSCs) to develop a novel and relevant human model system for BTHS. BTHS-iPSCs generated from dermal fibroblasts of three patients with different mutations in TAZ1 expressed pluripotency markers, and were able to differentiate into cells derived from all three germ layers both in vitro and in vivo. We used these cells to study the impact of tafazzin deficiency on mitochondria( oxidative phosphorylation. We found an impaired remodeling of cardiolipin, a dramatic decrease in basal oxygen consumption rate and in the maximal respiratory capacity in BTHS-iPSCs. Simultaneous measurement of extra-cellular acidification rate allowed us a thorough assessment of the metabolic deficiency in BTHS patients. Blue native gel analyses revealed that decreased respiration coincided with dramatic structural changes in respiratory chain supercomplexes leading to a massive increase in generation of reactive oxygen species. Our data demonstrate that BTHS-iPSCs are capable of modeling BTHS by recapitulating the disease phenotype and thus are important tools for studying the disease mechanism. (C) 2013 The Authors. Published by Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.scr.2013.05.005"],["dc.identifier.gro","3142297"],["dc.identifier.isi","000323586600012"],["dc.identifier.pmid","23792436"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11333"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6720"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/12"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A04: Patienten-spezifische induzierte pluripotente Stammzellen zur funktionellen Untersuchung von Ryanodinrezeptor-Mutationen"],["dc.relation","SFB 1002 | A06: Molekulare Grundlagen mitochondrialer Kardiomyopathien"],["dc.relation.issn","1873-5061"],["dc.relation.workinggroup","RG Guan (Application of patient-specific induced pluripotent stem cells in disease modelling)"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Cardiolipin deficiency affects respiratory chain function and organization in an induced pluripotent stem cell model of Barth syndrome"],["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"]]

[["dc.bibliographiccitation.firstpage","5009"],["dc.bibliographiccitation.issue","24"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","5021"],["dc.bibliographiccitation.volume","32"],["dc.contributor.author","Reinhold, Robert"],["dc.contributor.author","Krüger, Vivien"],["dc.contributor.author","Meinecke, Michael"],["dc.contributor.author","Schulz, Christian"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Grunau, Silke D."],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Wiedemann, Nils"],["dc.contributor.author","van der Laan, Martin"],["dc.contributor.author","Wagner, Richard"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Dudek, Jan"],["dc.date.accessioned","2017-09-07T11:48:21Z"],["dc.date.available","2017-09-07T11:48:21Z"],["dc.date.issued","2012"],["dc.description.abstract","The majority of multispanning inner mitochondrial membrane proteins utilize internal targeting signals, which direct them to the carrier translocase (TIM22 complex), for their import. MPV17 and its Saccharomyces cerevisiae orthologue Sym1 are multispanning inner membrane proteins of unknown function with an amino-terminal presequence that suggests they may be targeted to the mitochondria. Mutations affecting MPV17 are associated with mitochondrial DNA depletion syndrome (MDDS). Reconstitution of purified Sym1 into planar lipid bilayers and electrophysiological measurements have demonstrated that Sym1 forms a membrane pore. To address the biogenesis of Sym1, which oligomerizes in the inner mitochondrial membrane, we studied its import and assembly pathway. Sym1 forms a transport intermediate at the translocase of the outer membrane (TOM) complex. Surprisingly, Sym1 was not transported into mitochondria by an amino-terminal signal, and in contrast to what has been observed in carrier proteins, Sym1 transport and assembly into the inner membrane were independent of small translocase of mitochondrial inner membrane (TIM) and TIM22 complexes. Instead, Sym1 required the presequence of translocase for its biogenesis. Our analyses have revealed a novel transport mechanism for a polytopic membrane protein in which internal signals direct the precursor into the inner membrane via the TIM23 complex, indicating a presequence-independent function of this translocase."],["dc.identifier.doi","10.1128/MCB.00843-12"],["dc.identifier.gro","3142435"],["dc.identifier.isi","000311492200011"],["dc.identifier.pmid","23045398"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8252"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0270-7306"],["dc.title","The Channel-Forming Sym1 Protein Is Transported by the TIM23 Complex in a Presequence-Independent Manner"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","139"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","EMBO Molecular Medicine"],["dc.bibliographiccitation.lastpage","154"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Dudek, Jan"],["dc.contributor.author","Cheng, I-Fen"],["dc.contributor.author","Chowdhury, Arpita"],["dc.contributor.author","Wozny, Katharina"],["dc.contributor.author","Balleininger, Martina"],["dc.contributor.author","Reinhold, Robert"],["dc.contributor.author","Grunau, Silke"],["dc.contributor.author","Callegari, Sylvie"],["dc.contributor.author","Toischer, Karl"],["dc.contributor.author","Wanders, Ronald JA"],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Brügger, Britta"],["dc.contributor.author","Guan, Kaomei"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:53:31Z"],["dc.date.available","2017-09-07T11:53:31Z"],["dc.date.issued","2016"],["dc.description.abstract","Barth syndrome (BTHS) is a cardiomyopathy caused by the loss of tafazzin, a mitochondrial acyltransferase involved in the maturation of the glycerophospholipid cardiolipin. It has remained enigmatic as to why a systemic loss of cardiolipin leads to cardiomyopathy. Using a genetic ablation of tafazzin function in the BTHS mouse model, we identified severe structural changes in respiratory chain supercomplexes at a pre‐onset stage of the disease. This reorganization of supercomplexes was specific to cardiac tissue and could be recapitulated in cardiomyocytes derived from BTHS patients. Moreover, our analyses demonstrate a cardiac‐specific loss of succinate dehydrogenase (SDH), an enzyme linking the respiratory chain with the tricarboxylic acid cycle. As a similar defect of SDH is apparent in patient cell‐derived cardiomyocytes, we conclude that these defects represent a molecular basis for the cardiac pathology in Barth syndrome."],["dc.identifier.doi","10.15252/emmm.201505644"],["dc.identifier.fs","615879"],["dc.identifier.gro","3145083"],["dc.identifier.pmid","26697888"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13136"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2780"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/101"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.intern","Merged 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","1757-4676"],["dc.relation.issn","1757-4684"],["dc.relation.workinggroup","RG Guan (Application of patient-specific induced pluripotent stem cells in disease modelling)"],["dc.relation.workinggroup","RG Hasenfuß (Transition zur Herzinsuffizienz)"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.relation.workinggroup","RG Toischer (Kardiales Remodeling)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject","Barth syndrome; Cardiolipin, Mitochondriar; Respiratory chain; Succinate dehydrogenase"],["dc.title","Cardiac-specific succinate dehydrogenase deficiency in Barth syndrome"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4970"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","FEBS Journal"],["dc.bibliographiccitation.lastpage","4982"],["dc.bibliographiccitation.volume","280"],["dc.contributor.author","Welter, Evelyn"],["dc.contributor.author","Montino, Marco"],["dc.contributor.author","Reinhold, Robert"],["dc.contributor.author","Schlotterhose, Petra"],["dc.contributor.author","Krick, Roswitha"],["dc.contributor.author","Dudek, Jan"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Thumm, Michael"],["dc.date.accessioned","2017-09-07T11:47:07Z"],["dc.date.available","2017-09-07T11:47:07Z"],["dc.date.issued","2013"],["dc.description.abstract","Mitochondria are turned over by an autophagic process termed mitophagy. This process is considered to remove damaged, superfluous and aged organelles. However, little is known about how defective organelles are recognized, what types of damage induce turnover, and whether an identical set of factors contributes to degradation under different conditions. Here we systematically compared the mitophagy rate and requirement for mitophagy-specific proteins during post-log-phase and rapamycin-induced mitophagy. To specifically assess mitophagy of damaged mitochondria, we analyzed cells accumulating proteins prone to degradation due to lack of the mitochondrial AAA-protease Yme1. While autophagy 32 (Atg32) was required under all tested conditions, the function of Atg33 could be partially bypassed in post-log-phase and rapamycin-induced mitophagy. Unexpectedly, we found that Uth1 was dispensable for mitophagy. A re-evaluation of its mitochondrial localization revealed that Uth1 is a protein of the inner mitochondrial membrane that is targeted by a cleavable N-terminal pre-sequence. In agreement with our functional analyses, this finding excludes a role of Uth1 as a mitochondrial surface receptor."],["dc.identifier.doi","10.1111/febs.12468"],["dc.identifier.gro","3142274"],["dc.identifier.isi","000327132100006"],["dc.identifier.pmid","23910823"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6465"],["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","1742-4658"],["dc.relation.issn","1742-464X"],["dc.title","Uth1 is a mitochondrial inner membrane protein dispensable for post-log-phase and rapamycin-induced mitophagy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]