Rehling, Peter

[["dc.bibliographiccitation.firstpage","2642"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","2649"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Hutu, Dana P."],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Chacinska, Agnieszka"],["dc.contributor.author","Becker, Dorothea"],["dc.contributor.author","Pfanner, Nikolaus"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","van der Laan, Martin"],["dc.date.accessioned","2017-09-07T11:48:16Z"],["dc.date.available","2017-09-07T11:48:16Z"],["dc.date.issued","2008"],["dc.description.abstract","The presequence translocase of the mitochondrial inner membrane (TIM23 complex) mediates the import of preproteins with amino-terminal presequences. To drive matrix translocation the TIM23 complex recruits the presequence translocase-associated motor (PAM) with the matrix heat shock protein 70 (mtHsp70) as central subunit. Activity and localization of mtHsp70 are regulated by four membrane-associated cochaperones: the adaptor protein Tim44, the stimulatory J-complex Pam18/Pam16, and Pam17. It has been proposed that Tim44 serves as molecular platform to localize mtHsp70 and the J-complex at the TIM23 complex, but it is unknown how Pam17 interacts with the translocase. We generated conditional tim44 yeast mutants and selected a mutant allele, which differentially affects the association of PAM modules with TIM23. In tim44-804 mitochondria, the interaction of the J-complex with the TIM23 complex is impaired, whereas unexpectedly the binding of Pam17 is increased. Pam17 interacts with the channel protein Tim23, revealing a new interaction site between TIM23 and PAM. Thus, the motor PAM is composed of functional modules that bind to different sites of the translocase. We suggest that Tim44 is not simply a scaffold for binding of motor subunits but plays a differential role in the recruitment of PAM modules to the inner membrane translocase."],["dc.identifier.doi","10.1091/mbc.E07-12-1226"],["dc.identifier.gro","3143286"],["dc.identifier.isi","000259155200028"],["dc.identifier.pmid","18400944"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/783"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1939-4586"],["dc.relation.issn","1059-1524"],["dc.title","Mitochondrial protein import motor: Differential role of Tim44 in the recruitment of Pam17 and J-complex to the presequence translocase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1694"],["dc.bibliographiccitation.issue","21"],["dc.bibliographiccitation.journal","Circulation"],["dc.bibliographiccitation.lastpage","1713"],["dc.bibliographiccitation.volume","144"],["dc.contributor.author","Bertero, Edoardo"],["dc.contributor.author","Nickel, Alexander"],["dc.contributor.author","Kohlhaas, Michael"],["dc.contributor.author","Hohl, Mathias"],["dc.contributor.author","Sequeira, Vasco"],["dc.contributor.author","Brune, Carolin"],["dc.contributor.author","Schwemmlein, Julia"],["dc.contributor.author","Abeßer, Marco"],["dc.contributor.author","Schuh, Kai"],["dc.contributor.author","Kutschka, Ilona"],["dc.contributor.author","Carlein, Christopher"],["dc.contributor.author","Münker, Kai"],["dc.contributor.author","Atighetchi, Sarah"],["dc.contributor.author","Müller, Andreas"],["dc.contributor.author","Kazakov, Andrey"],["dc.contributor.author","Kappl, Reinhard"],["dc.contributor.author","von der Malsburg, Karina"],["dc.contributor.author","van der Laan, Martin"],["dc.contributor.author","Schiuma, Anna-Florentine"],["dc.contributor.author","Böhm, Michael"],["dc.contributor.author","Laufs, Ulrich"],["dc.contributor.author","Hoth, Markus"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Kuhn, Michaela"],["dc.contributor.author","Dudek, Jan"],["dc.contributor.author","von der Malsburg, Alexander"],["dc.contributor.author","Prates Roma, Leticia"],["dc.contributor.author","Maack, Christoph"],["dc.date.accessioned","2022-02-22T13:45:03Z"],["dc.date.available","2022-02-22T13:45:03Z"],["dc.date.issued","2021"],["dc.description.abstract","Barth syndrome (BTHS) is caused by mutations of the gene encoding tafazzin, which catalyzes maturation of mitochondrial cardiolipin and often manifests with systolic dysfunction during early infancy. Beyond the first months of life, BTHS cardiomyopathy typically transitions to a phenotype of diastolic dysfunction with preserved ejection fraction, blunted contractile reserve during exercise, and arrhythmic vulnerability. Previous studies traced BTHS cardiomyopathy to mitochondrial formation of reactive oxygen species (ROS). Because mitochondrial function and ROS formation are regulated by excitation-contraction coupling, integrated analysis of mechano-energetic coupling is required to delineate the pathomechanisms of BTHS cardiomyopathy."],["dc.identifier.doi","10.1161/CIRCULATIONAHA.121.053755"],["dc.identifier.pmid","34648376"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/100184"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/410"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/357"],["dc.language.iso","en"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A06: Molekulare Grundlagen mitochondrialer Kardiomyopathien"],["dc.relation.eissn","1524-4539"],["dc.relation.issn","0009-7322"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.title","Loss of Mitochondrial Ca2+ Uniporter Limits Inotropic Reserve and Provides Trigger and Substrate for Arrhythmias in Barth Syndrome Cardiomyopathy"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["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","7449"],["dc.bibliographiccitation.issue","17"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","7458"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","van der Laan, Martin"],["dc.contributor.author","Chacinska, Agnieszka"],["dc.contributor.author","Lind, Maria"],["dc.contributor.author","Perschil, Inge"],["dc.contributor.author","Sickmann, Albert"],["dc.contributor.author","Meyer, Helmut E."],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Meisinger, Chris"],["dc.contributor.author","Pfanner, Nikolaus"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:54:18Z"],["dc.date.available","2017-09-07T11:54:18Z"],["dc.date.issued","2005"],["dc.description.abstract","Import of mitochondrial matrix proteins involves the general translocase of the outer membrane and the presequence translocase of the inner membrane. The presequence translocase-associated motor (PAM) drives the completion of preprotein translocation into the matrix. Five subunits of PAM are known: the preprotein-binding matrix heat shock protein 70 (mtHsp70), the nucleotide exchange factor Mge1, Tim44 that directs mtHsp70 to the inner membrane, and the membrane-bound complex of Pam16-Pam18 that regulates the ATPase activity of mtHsp70. We have identified a sixth motor subunit. Pam17 (encoded by the open reading frame YKR065c) is anchored in the inner membrane and exposed to the matrix. Mitochondria lacking Pam17 are selectively impaired in the import of matrix proteins and the generation of an import-driving activity of PAM. Pam17 is required for formation of a stable complex between the cochaperones Pam16 and Pam18 and promotes the association of Pam16-Pam18 with the presequence translocase. Our findings suggest that Pam17 is required for the correct organization of the Pam16-Pam18 complex and thus contributes to regulation of mtHsp70 activity at the inner membrane translocation site."],["dc.identifier.doi","10.1128/MCB.25.17.7449-7458.2005"],["dc.identifier.gro","3143811"],["dc.identifier.isi","000231329300006"],["dc.identifier.pmid","16107694"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1366"],["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","Pam17 is required for architecture and translocation activity of 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","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","33314"],["dc.bibliographiccitation.issue","40"],["dc.bibliographiccitation.journal","Journal of biological chemistry"],["dc.bibliographiccitation.lastpage","33326"],["dc.bibliographiccitation.volume","287"],["dc.contributor.author","Krüger, Vivien"],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Hildenbeutel, Markus"],["dc.contributor.author","van der Laan, Martin"],["dc.contributor.author","Hellmers, Maike"],["dc.contributor.author","Dreker, Christina"],["dc.contributor.author","Preuss, Marc"],["dc.contributor.author","Herrmann, Johannes M."],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Wagner, Richard"],["dc.contributor.author","Meinecke, Michael"],["dc.date.accessioned","2017-09-07T11:48:24Z"],["dc.date.available","2017-09-07T11:48:24Z"],["dc.date.issued","2012"],["dc.description.abstract","The inner membrane of mitochondria is especially protein-rich. To direct proteins into the inner membrane, translocases mediate transport and membrane insertion of precursor proteins. Although the majority of mitochondrial proteins are imported from the cytoplasm, core subunits of respiratory chain complexes are inserted into the inner membrane from the matrix. Oxa1, a conserved membrane protein, mediates the insertion of mitochondrion-encoded precursors into the inner mitochondrial membrane. The molecular mechanism by which Oxa1 mediates insertion of membrane spans, entailing the translocation of hydrophilic domains across the inner membrane, is still unknown. We investigated if Oxa1 could act as a protein-conducting channel for precursor transport. Using a biophysical approach, we show that Oxa1 can form a pore capable of accommodating a translocating protein segment. After purification and reconstitution, Oxa1 acts as a cation-selective channel that specifically responds to mitochondrial export signals. The aqueous pore formed by Oxa1 displays highly dynamic characteristics with a restriction zone diameter between 0.6 and 2 nm, which would suffice for polypeptide translocation across the membrane. Single channel analyses revealed four discrete channels per active unit, suggesting that the Oxa1 complex forms several cooperative hydrophilic pores in the inner membrane. Hence, Oxa1 behaves as a pore-forming translocase that is regulated in a membrane potential and substrate-dependent manner."],["dc.identifier.doi","10.1074/jbc.M112.387563"],["dc.identifier.gro","3142462"],["dc.identifier.isi","000309602100020"],["dc.identifier.pmid","22829595"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8551"],["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 Mitochondrial Oxidase Assembly Protein1 (Oxa1) Insertase Forms a Membrane Pore in Lipid Bilayers"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4347"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","4358"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Wagner, Karina"],["dc.contributor.author","van der Laan, Martin"],["dc.contributor.author","Frazier, Ann E."],["dc.contributor.author","Perschil, Inge"],["dc.contributor.author","Pawlas, Magdalena"],["dc.contributor.author","Meyer, Helmut E."],["dc.contributor.author","Warscheid, Bettina"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:49:24Z"],["dc.date.available","2017-09-07T11:49:24Z"],["dc.date.issued","2007"],["dc.description.abstract","Cytochrome c oxidase ( complex IV) of the respiratory chain is assembled from nuclear and mitochondrially-encoded subunits. Defects in the assembly process lead to severe human disorders such as Leigh syndrome. Shy1 is an assembly factor for complex IV in Saccharomyces cerevisiae and mutations of its human homolog, SURF1, are the most frequent cause for Leigh syndrome. We report that Shy1 promotes complex IV biogenesis through association with different protein modules; Shy1 interacts with Mss51 and Cox14, translational regulators of Cox1. Additionally, Shy1 associates with the subcomplexes of complex IV that are potential assembly intermediates. Formation of these subcomplexes depends on Coal (YIL157c), a novel assembly factor that cooperates with Shy1. Moreover, partially assembled forms of complex IV bound to Shy1 and Cox14 can associate with the bc1 complex to form transitional supercomplexes. We suggest that Shy1 links Cox1 translational regulation to complex IV assembly and supercomplex formation."],["dc.identifier.doi","10.1038/sj.emboj.7601862"],["dc.identifier.gro","3143423"],["dc.identifier.isi","000250467100006"],["dc.identifier.pmid","17882259"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/936"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-blackwell"],["dc.relation.eissn","1460-2075"],["dc.relation.issn","0261-4189"],["dc.title","Shy1 couples Cox1 translational regulation to cytochrome c oxidase assembly"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1624"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","1727"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Naumenko, Nataliia"],["dc.contributor.author","Oeljeklaus, Silke"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","von der Malsburg, Karina"],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Warscheid, Bettina"],["dc.contributor.author","van der Laan, Martin"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:45:41Z"],["dc.date.available","2017-09-07T11:45:41Z"],["dc.date.issued","2014"],["dc.description.abstract","Mitochondrial F1Fo-ATP synthase generates the bulk of cellular ATP. This molecular machine assembles from nuclear- and mitochondria-encoded subunits. Whereas chaperones for formation of the matrix-exposed hexameric F-1-ATPase core domain have been identified, insight into how the nuclear-encoded F-1-domain assembles with the membrane-embedded F-o-region is lacking. Here we identified the INA complex (INAC) in the inner membrane of mitochondria as an assembly factor involved in this process. Ina22 and Ina17 are INAC constituents that physically associate with the F-1-module and peripheral stalk, but not with the assembled F1Fo-ATP synthase. Our analyses show that loss of Ina22 and Ina17 specifically impairs formation of the peripheral stalk that connects the catalytic F-1-module to the membrane embedded F-o-domain. We conclude that INAC represents a matrix-exposed inner membrane protein complex that facilitates peripheral stalk assembly and thus promotes a key step in the biogenesis of mitochondrial F1Fo-ATP synthase."],["dc.identifier.doi","10.15252/embj.201488076"],["dc.identifier.gro","3142082"],["dc.identifier.isi","000339917000005"],["dc.identifier.pmid","24942160"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4345"],["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","1460-2075"],["dc.relation.issn","0261-4189"],["dc.title","The INA complex facilitates assembly of the peripheral stalk of the mitochondrial F1Fo-ATP synthase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1115"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","1122"],["dc.bibliographiccitation.volume","179"],["dc.contributor.author","Wiedemann, Nils"],["dc.contributor.author","van der Laan, Martin"],["dc.contributor.author","Hutu, Dana P."],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Pfanner, Nikolaus"],["dc.date.accessioned","2017-09-07T11:49:22Z"],["dc.date.available","2017-09-07T11:49:22Z"],["dc.date.issued","2007"],["dc.description.abstract","The mitochondrial presequence translocase transports preproteins to either matrix or inner membrane. Two different translocase forms have been identified: the matrix transport form, which binds the heat-shock protein 70 (Hsp70) motor, and the inner membrane sorting form, which lacks the motor but contains translocase of inner mitochondrial membrane 21 (Tim21). The sorting form interacts with the respiratory chain in a Tim21-dependent manner. It is unknown whether the respiratory chain-bound translocase transports preproteins and how the switch between sorting form and motor form occurs. We report that the respiratory chain-bound translocase contains preproteins in transit and, surprisingly, not only sorted but also matrix-targeted preproteins. Presequence translocase-associated motor (Pam) 16 and 18, two regulatory components of the six-subunit motor, interact with the respiratory chain independently of Tim21. Thus, the respiratory chain-bound presequence translocase is not only active in preprotein sorting to the inner membrane but also in an early stage of matrix translocation. The motor does not assemble en bloc with the translocase but apparently in a step-wise manner with the Pam16/18 module before the Hsp70 core."],["dc.identifier.doi","10.1083/jcb.200709087"],["dc.identifier.gro","3143395"],["dc.identifier.isi","000251697300006"],["dc.identifier.pmid","18070913"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/905"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0021-9525"],["dc.title","Sorting switch of mitochondrial presequence translocase involves coupling of motor module to respiratory chain"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","694"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Developmental Cell"],["dc.bibliographiccitation.lastpage","707"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","von der Malsburg, Karina"],["dc.contributor.author","Müller, Judith M."],["dc.contributor.author","Bohnert, Maria"],["dc.contributor.author","Oeljeklaus, Silke"],["dc.contributor.author","Kwiatkowska, Paulina"],["dc.contributor.author","Becker, Thomas"],["dc.contributor.author","Loniewska-Lwowska, Adrianna"],["dc.contributor.author","Wiese, Sebastian"],["dc.contributor.author","Rao, Sanjana"],["dc.contributor.author","Milenkovic, Dusanka"],["dc.contributor.author","Hutu, Dana P."],["dc.contributor.author","Zerbes, Ralf M."],["dc.contributor.author","Schulze-Specking, Agnes"],["dc.contributor.author","Meyer, Helmut E."],["dc.contributor.author","Martinou, Jean-Claude"],["dc.contributor.author","Rospert, Sabine"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Meisinger, Chris"],["dc.contributor.author","Veenhuis, Marten"],["dc.contributor.author","Warscheid, Bettina"],["dc.contributor.author","van der Klei, Ida J."],["dc.contributor.author","Pfanner, Nikolaus"],["dc.contributor.author","Chacinska, Agnieszka"],["dc.contributor.author","van der Laan, Martin"],["dc.date.accessioned","2017-09-07T11:43:21Z"],["dc.date.available","2017-09-07T11:43:21Z"],["dc.date.issued","2011"],["dc.description.abstract","The mitochondrial inner membrane consists of two domains, inner boundary membrane and cristae membrane that are connected by crista junctions. Mitofilin/Fcj1 was reported to be involved in formation of crista junctions, however, different views exist on its function and possible partner proteins. We report that mitofilin plays a dual role. Mitofilin is part of a large inner membrane complex, and we identify five partner proteins as constituents of the mitochondrial inner membrane organizing system (MINOS) that is required for keeping cristae membranes connected to the inner boundary membrane. Additionally, mitofilin is coupled to the outer membrane and promotes protein import via the mitochondrial intermembrane space assembly pathway. Our findings indicate that mitofilin is a central component of MINOS and functions as a multifunctional regulator of mitochondrial architecture and protein biogenesis."],["dc.identifier.doi","10.1016/j.devcel.2011.08.026"],["dc.identifier.gro","3142642"],["dc.identifier.isi","000296366000013"],["dc.identifier.pmid","21944719"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/68"],["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","1878-1551"],["dc.relation.issn","1534-5807"],["dc.title","Dual Role of Mitofilin in Mitochondrial Membrane Organization and Protein Biogenesis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]