Mick, David U.

[["dc.bibliographiccitation.firstpage","1523"],["dc.bibliographiccitation.issue","5779"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","1526"],["dc.bibliographiccitation.volume","312"],["dc.contributor.author","Meinecke, Michael"],["dc.contributor.author","Wagner, Richard"],["dc.contributor.author","Kovermann, Peter"],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Hutu, Dana P."],["dc.contributor.author","Voos, Wolfgang"],["dc.contributor.author","Truscott, Kaye N."],["dc.contributor.author","Chacinska, Agnieszka"],["dc.contributor.author","Pfanner, Nikolaus"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:52:41Z"],["dc.date.available","2017-09-07T11:52:41Z"],["dc.date.issued","2006"],["dc.description.abstract","Transport of metabolites across the mitochondrial inner membrane is highly selective, thereby maintaining the electrochemical proton gradient that functions as the main driving force for cellular adenosine triphosphate synthesis. Mitochondria import many preproteins via the presequence translocase of the inner membrane. However, the reconstituted Tim23 protein constitutes a pore remaining mainly in its open form, a state that would be deleterious in organello. We found that the intermembrane space domain of Tim50 induced the Tim23 channel to close. Presequences overcame this effect and activated the channel for translocation. Thus, the hydrophilic cis domain of Tim50 maintains the permeability barrier of mitochondria by closing the translocation pore in a presequence-regulated manner."],["dc.identifier.doi","10.1126/science.1127628"],["dc.identifier.gro","3143677"],["dc.identifier.isi","000238124100048"],["dc.identifier.pmid","16763150"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1217"],["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","0036-8075"],["dc.title","Tim50 maintains the permeability barrier of the mitochondrial inner membrane"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","553"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","564"],["dc.bibliographiccitation.volume","172"],["dc.contributor.author","Frazier, Ann E."],["dc.contributor.author","Taylor, Rebecca D."],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Warscheid, Bettina"],["dc.contributor.author","Stoepel, Nadine"],["dc.contributor.author","Meyer, Helmut E."],["dc.contributor.author","Ryan, Michael T."],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:53:24Z"],["dc.date.available","2017-09-07T11:53:24Z"],["dc.date.issued","2006"],["dc.description.abstract","Saccharomyces cerevisiae Mdm38 and Ylh47 are homologues of human Letm1, a protein implicated in Wolf-Hirschhorn syndrome. We analyzed the function of Mdm38 and Ylh47 in yeast mitochondria to gain insight into the role of Letm1. We find that mdm38 Delta mitochondria have reduced amounts of certain mitochondrially encoded proteins and low levels of complex III and IV and accumulate unassembled Atp6 of complex V of the respiratory chain. Mdm38 is especially required for efficient transport of Atp6 and cytochrome b across the inner membrane, whereas Ylh47 plays a minor role in this process. Both Mdm38 and Ylh47 form stable complexes with mitochondrial ribosomes, similar to what has been reported for Oxa1, a central component of the mitochondrial export machinery. Our results indicate that Mdm38 functions as a component of an Oxa1-independent insertion machinery in the inner membrane and that Mdm38 plays a critical role in the biogenesis of the respiratory chain by coupling ribosome function to protein transport across the inner membrane."],["dc.identifier.doi","10.1083/jcb.200505060"],["dc.identifier.gro","3143739"],["dc.identifier.isi","000235329800024"],["dc.identifier.pmid","16476776"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1286"],["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","0021-9525"],["dc.title","Mdm38 interacts with ribosomes and is a component of the mitochondrial protein export machinery"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2271"],["dc.bibliographiccitation.issue","22"],["dc.bibliographiccitation.journal","Current Biology"],["dc.bibliographiccitation.lastpage","2276"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","van der Laan, Martin"],["dc.contributor.author","Wiedemann, Nils"],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Pfanner, Nikolaus"],["dc.date.accessioned","2017-09-07T11:49:54Z"],["dc.date.available","2017-09-07T11:49:54Z"],["dc.date.issued","2006"],["dc.description.abstract","The mitochondrial inner membrane harbors complexes of the respiratory chain and translocase complexes for preproteins. The membrane potential generated by the respiratory chain is essential for ATP production by the mitochondrial ATP synthase and as a driving force for protein import [1-7]. It is generally believed that the preprotein translocases just use the membrane potential without getting into physical contact with respiratory-chain complexes [3, 6, 7]. Here, we show that the presequence translocase interacts with the respiratory chain. Tim21, a specific subunit of the sorting-active presequence translocase [8, 9], recruits proton-pumping respiratory-chain complexes and stimulates preprotein insertion. Thus, the presequence translocase cooperates with the respiratory chain and promotes membrane-potential-dependent protein sorting into the inner mitochondrial membrane. These findings suggest a new coupling mechanism in an energy-transducing membrane."],["dc.identifier.doi","10.1016/j.cub.2006.10.025"],["dc.identifier.gro","3143586"],["dc.identifier.isi","000242268900031"],["dc.identifier.pmid","17113393"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1116"],["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","0960-9822"],["dc.title","A role for Tim21 in membrane-potential-dependent preprotein sorting in mitochondria"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","307"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","318"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Chacinska, Agnieszka"],["dc.contributor.author","van der Laan, Martin"],["dc.contributor.author","Mehnert, Carola S."],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Hutu, Dana P."],["dc.contributor.author","Truscott, Kaye N."],["dc.contributor.author","Wiedemann, Nils"],["dc.contributor.author","Meisinger, Chris"],["dc.contributor.author","Pfanner, Nikolaus"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:46:43Z"],["dc.date.available","2017-09-07T11:46:43Z"],["dc.date.issued","2010"],["dc.description.abstract","Mitochondrial import of cleavable preproteins occurs at translocation contact sites, where the translocase of the outer membrane (TOM) associates with the presequence translocase of the inner membrane (TIM23) in a supercomplex. Different views exist on the mechanism of how TIM23 mediates preprotein sorting to either the matrix or inner membrane. On the one hand, two TIM23 forms were proposed, a matrix transport form containing the presequence translocase-associated motor (PAM; TIM23-PAM) and a sorting form containing Tim21 (TIM23(SORT)). On the other hand, it was reported that TIM23 and PAM are permanently associated in a single-entity translocase. We have accumulated distinct transport intermediates of preproteins to analyze the translocases in their active, preprotein-carrying state. We identified two different forms of active TOM-TIM23 supercomplexes, TOM-TIM23(SORT) and TOM-TIM23-PAM. These two supercomplexes do not represent separate pathways but are in dynamic exchange during preprotein translocation and sorting. Depending on the signals of the preproteins, switches between the different forms of supercomplex and TIM23 are required for the completion of preprotein import."],["dc.identifier.doi","10.1128/MCB.00749-09"],["dc.identifier.gro","3142998"],["dc.identifier.isi","000272569200025"],["dc.identifier.pmid","19884344"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/464"],["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","Distinct Forms of Mitochondrial TOM-TIM Supercomplexes Define Signal-Dependent States of Preprotein Sorting"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]