Rucktäschel, Robert

[["dc.bibliographiccitation.artnumber","1237"],["dc.bibliographiccitation.firstpage","1237"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.lastpage","1"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Naumenko, Nataliia"],["dc.contributor.author","Morgenstern, Marcel"],["dc.contributor.author","Rucktäschel, Robert"],["dc.contributor.author","Warscheid, Bettina"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2018-01-09T14:08:26Z"],["dc.date.available","2018-01-09T14:08:26Z"],["dc.date.issued","2017"],["dc.description.abstract","The F1F0-ATP synthase translates a proton flux across the inner mitochondrial membrane into a mechanical rotation, driving anhydride bond formation in the catalytic portion. The complex's membrane-embedded motor forms a proteinaceous channel at the interface between Atp9 ring and Atp6. To prevent unrestricted proton flow dissipating the H+-gradient, channel formation is a critical and tightly controlled step during ATP synthase assembly. Here we show that the INA complex (INAC) acts at this decisive step promoting Atp9-ring association with Atp6. INAC binds to newly synthesized mitochondrial-encoded Atp6 and Atp8 in complex with maturation factors. INAC association is retained until the F1-portion is built on Atp6/8 and loss of INAC causes accumulation of the free F1. An independent complex is formed between INAC and the Atp9 ring. We conclude that INAC maintains assembly intermediates of the F1 F0-ATP synthase in a primed state for the terminal assembly step-motor module formation."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2017"],["dc.format.extent","1"],["dc.identifier.doi","10.1038/s41467-017-01437-z"],["dc.identifier.pmid","29093463"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14823"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11598"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.eissn","2041-1723"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","INA complex liaises the F1Fo-ATP synthase membrane motor modules"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","947"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Traffic"],["dc.bibliographiccitation.lastpage","959"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Otzen, Marleen"],["dc.contributor.author","Rucktäschel, Robert"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Emmrich, Kerstin"],["dc.contributor.author","Krikken, Arjen M."],["dc.contributor.author","Erdmann, Ralf"],["dc.contributor.author","van der Klei, Ida J."],["dc.date.accessioned","2020-08-10T05:14:16Z"],["dc.date.available","2020-08-10T05:14:16Z"],["dc.date.issued","2012"],["dc.description.abstract","During budding of yeast cells peroxisomes are distributed over mother cell and bud, a process that involves the myosin motor protein Myo2p and the peroxisomal membrane protein Inp2p. Here, we show that Pex19p, a peroxin implicated in targeting and complex formation of peroxisomal membrane proteins, also plays a role in peroxisome partitioning. Binding studies revealed that Pex19p interacts with the cargo-binding domain of Myo2p. We identified mutations in Myo2p that specifically reduced binding to Pex19p, but not to Inp2p. The interaction between Myo2p and Pex19p was also reduced by a mutation that blocked Pex19p farnesylation. Microscopy revealed that the Pex19p-Myo2p interaction is important for peroxisome inheritance, because mutations that affect this interaction hamper peroxisome inheritance in vivo. Together these data suggest that both Inp2p and Pex19p are required for proper association of peroxisomes to Myo2p."],["dc.identifier.doi","10.1111/j.1600-0854.2012.01364.x"],["dc.identifier.pmid","22486971"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67537"],["dc.language.iso","en"],["dc.relation.eissn","1600-0854"],["dc.relation.issn","1398-9219"],["dc.title","Pex19p contributes to peroxisome inheritance in the association of peroxisomes to Myo2p"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","20885"],["dc.bibliographiccitation.issue","31"],["dc.bibliographiccitation.journal","The Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","20896"],["dc.bibliographiccitation.volume","284"],["dc.contributor.author","Rucktäschel, Robert"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Sidorovitch, Vadim"],["dc.contributor.author","Halbach, Andre"],["dc.contributor.author","Pechlivanis, Markos"],["dc.contributor.author","Volkmer, Rudolf"],["dc.contributor.author","Alexandrov, Kirill"],["dc.contributor.author","Kuhlmann, Jürgen"],["dc.contributor.author","Rottensteiner, Hanspeter"],["dc.contributor.author","Erdmann, Ralf"],["dc.date.accessioned","2020-08-10T05:20:25Z"],["dc.date.available","2020-08-10T05:20:25Z"],["dc.date.issued","2009"],["dc.description.abstract","The conserved CaaX box peroxin Pex19p is known to be modified by farnesylation. The possible involvement of this lipid modification in peroxisome biogenesis, the degree to which Pex19p is farnesylated, and its molecular function are unknown or controversial. We resolve these issues by first showing that the complete pool of Pex19p is processed by farnesyltransferase in vivo and that this modification is independent of peroxisome induction or the Pex19p membrane anchor Pex3p. Furthermore, genomic mutations of PEX19 prove that farnesylation is essential for proper matrix protein import into peroxisomes, which is supposed to be caused indirectly by a defect in peroxisomal membrane protein (PMP) targeting or stability. This assumption is corroborated by the observation that mutants defective in Pex19p farnesylation are characterized by a significantly reduced steady-state concentration of prominent PMPs (Pex11p, Ant1p) but also of essential components of the peroxisomal import machinery, especially the RING peroxins, which were almost depleted from the importomer. In vivo and in vitro, PMP recognition is only efficient when Pex19p is farnesylated with affinities differing by a factor of 10 between the non-modified and wild-type forms of Pex19p. Farnesylation is likely to induce a conformational change in Pex19p. Thus, isoprenylation of Pex19p contributes to substrate membrane protein recognition for the topogenesis of PMPs, and our results highlight the importance of lipid modifications in protein-protein interactions."],["dc.identifier.doi","10.1074/jbc.M109.016584"],["dc.identifier.pmid","19451657"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67540"],["dc.language.iso","en"],["dc.relation.eissn","1083-351X"],["dc.relation.issn","0021-9258"],["dc.title","Farnesylation of pex19p is required for its structural integrity and function in peroxisome biogenesis"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]