Richter-Dennerlein, Ricarda

[["dc.bibliographiccitation.journal","Frontiers in Microbiology"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Wesolowska, Maria T."],["dc.contributor.author","Richter-Dennerlein, Ricarda"],["dc.contributor.author","Lightowlers, Robert N."],["dc.contributor.author","Chrzanowska-Lightowlers, Zofia M. A."],["dc.date.accessioned","2022-03-01T11:44:22Z"],["dc.date.available","2022-03-01T11:44:22Z"],["dc.date.issued","2014"],["dc.identifier.doi","10.3389/fmicb.2014.00374"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103008"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1664-302X"],["dc.title","Overcoming stalled translation in human mitochondria"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.contributor.author","Kolanczyk, Mateusz"],["dc.contributor.author","Pech, Markus"],["dc.contributor.author","Zemojtel, Tomasz"],["dc.contributor.author","Yamamoto, Hiroshi"],["dc.contributor.author","Mikula, Ivan"],["dc.contributor.author","Calvaruso, Maria-Antonietta"],["dc.contributor.author","Richter-Dennerlein, Ricarda"],["dc.contributor.author","Fischer-Zirnsak, Björn"],["dc.contributor.author","Ritz, Anita"],["dc.contributor.author","Kossler, Nadine"],["dc.contributor.author","Martasek, Pavel"],["dc.contributor.author","Spoerle, Ralf"],["dc.contributor.author","Smeitink, Jan"],["dc.contributor.author","Kornak, Uwe"],["dc.contributor.author","Vingron, Martin"],["dc.contributor.author","Nijtmans, Leo"],["dc.contributor.author","Nierhaus, Knud"],["dc.contributor.author","Lightowlers, Robert"],["dc.contributor.author","Schuelke, Markus"],["dc.contributor.author","Mundlos, Stefan"],["dc.date.accessioned","2020-06-19T09:54:57Z"],["dc.date.available","2020-06-19T09:54:57Z"],["dc.date.issued","2011"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/66547"],["dc.title","Trophoblast Development Is Compromised By The Mitochondrial Dysfunction"],["dc.type","report"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","284"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Trends in Cell Biology"],["dc.bibliographiccitation.lastpage","297"],["dc.bibliographiccitation.volume","31"],["dc.contributor.author","Maiti, Priyanka"],["dc.contributor.author","Lavdovskaia, Elena"],["dc.contributor.author","Barrientos, Antoni"],["dc.contributor.author","Richter-Dennerlein, Ricarda"],["dc.date.accessioned","2021-04-14T08:28:48Z"],["dc.date.available","2021-04-14T08:28:48Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1016/j.tcb.2020.12.008"],["dc.identifier.pmid","33419649"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82707"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/125"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.issn","0962-8924"],["dc.relation.workinggroup","RG Richter-Dennerlein (Mitoribosome Assembly)"],["dc.title","Role of GTPases in Driving Mitoribosome Assembly"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.contributor.author","Hillen, Hauke S."],["dc.contributor.author","Lavdovskaia, Elena"],["dc.contributor.author","Nadler, Franziska"],["dc.contributor.author","Hanitsch, Elisa"],["dc.contributor.author","Linden, Andreas"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Richter-Dennerlein, Ricarda"],["dc.date.accessioned","2022-02-23T16:35:33Z"],["dc.date.available","2022-02-23T16:35:33Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1101/2021.03.17.435767"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/100377"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/241"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.workinggroup","RG Hillen (Structure and Function of Molecular Machines)"],["dc.relation.workinggroup","RG Richter-Dennerlein (Mitoribosome Assembly)"],["dc.title","Structural basis of GTPase-mediated mitochondrial ribosome biogenesis and recycling"],["dc.type","preprint"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Nadler, Franziska"],["dc.contributor.author","Lavdovskaia, Elena"],["dc.contributor.author","Krempler, Angelique"],["dc.contributor.author","Cruz-Zaragoza, Luis Daniel"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Richter-Dennerlein, Ricarda"],["dc.date.accessioned","2022-12-01T08:30:49Z"],["dc.date.available","2022-12-01T08:30:49Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract\r\n Translation termination requires release factors that read a STOP codon in the decoding center and subsequently facilitate the hydrolysis of the nascent peptide chain from the peptidyl tRNA within the ribosome. In human mitochondria eleven open reading frames terminate in the standard UAA or UAG STOP codon, which can be recognized by mtRF1a, the proposed major mitochondrial release factor. However, two transcripts encoding for COX1 and ND6 terminate in the non-conventional AGA or AGG codon, respectively. How translation termination is achieved in these two cases is not known. We address this long-standing open question by showing that the non-canonical release factor mtRF1 is a specialized release factor that triggers COX1 translation termination, while mtRF1a terminates the majority of other mitochondrial translation events including the non-canonical ND6. Loss of mtRF1 leads to isolated COX deficiency and activates the mitochondrial ribosome-associated quality control accompanied by the degradation of COX1 mRNA to prevent an overload of the ribosome rescue system. Taken together, these results establish the role of mtRF1 in mitochondrial translation, which had been a mystery for decades, and lead to a comprehensive picture of translation termination in human mitochondria."],["dc.identifier.doi","10.1038/s41467-022-34088-w"],["dc.identifier.pii","34088"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/117991"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-621"],["dc.relation.eissn","2041-1723"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Human mtRF1 terminates COX1 translation and its ablation induces mitochondrial ribosome-associated quality control"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","148"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Molecular Cell"],["dc.bibliographiccitation.lastpage","162"],["dc.bibliographiccitation.volume","64"],["dc.contributor.author","Koenig, Tim"],["dc.contributor.author","Troeder, Simon E."],["dc.contributor.author","Bakka, Kavya"],["dc.contributor.author","Korwitz, Anne"],["dc.contributor.author","Richter-Dennerlein, Ricarda"],["dc.contributor.author","Lampe, Philipp A."],["dc.contributor.author","Patron, Maria"],["dc.contributor.author","Muhlmeister, Mareike"],["dc.contributor.author","Guerrero-Castillo, Sergio"],["dc.contributor.author","Brandt, Ulrich"],["dc.contributor.author","Decker, Thorsten"],["dc.contributor.author","Lauria, Ines"],["dc.contributor.author","Paggio, Angela"],["dc.contributor.author","Rizzuto, Rosario"],["dc.contributor.author","Rugarli, Elena I."],["dc.contributor.author","De Stefani, Diego"],["dc.contributor.author","Langer, Thomas"],["dc.date.accessioned","2018-11-07T10:07:10Z"],["dc.date.available","2018-11-07T10:07:10Z"],["dc.date.issued","2016"],["dc.description.abstract","Mutations in subunits of mitochondrialm-AAA proteases in the inner membrane cause neurodegeneration in spinocerebellar ataxia (SCA28) and hereditary spastic paraplegia (HSP7). m-AAA proteases preserve mitochondrial proteostasis, mitochondrial morphology, and efficient OXPHOS activity, but the cause for neuronal loss in disease is unknown. We have determined the neuronal interactome of m-AAA proteases in mice and identified a complex with C2ORF47 (termed MAIP1), which counteracts cell death by regulating the assembly of the mitochondrial Ca2+ uniporter MCU. While MAIP1 assists biogenesis of the MCU subunit EMRE, the m-AAA protease degrades non-assembled EMRE and ensures efficient assembly of gatekeeper subunits with MCU. Loss of the m-AAA protease results in accumulation of constitutively active MCU-EMRE channels lacking gatekeeper subunits in neuronal mitochondria and facilitates mitochondrial Ca2+ overload, mitochondrial permeability transition pore opening, and neuronal death. Together, our results explain neuronal loss in m-AAA protease deficiency by deregulated mitochondrial Ca2+ homeostasis."],["dc.identifier.doi","10.1016/j.molcel.2016.08.020"],["dc.identifier.isi","000389514900016"],["dc.identifier.pmid","27642048"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39230"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","1097-4164"],["dc.relation.issn","1097-2765"],["dc.title","The m-AAA Protease Associated with Neurodegeneration Limits MCU Activity in Mitochondria"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","157"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","166"],["dc.bibliographiccitation.volume","212"],["dc.contributor.author","Korwitz, Anne"],["dc.contributor.author","Merkwirth, Carsten"],["dc.contributor.author","Richter-Dennerlein, Ricarda"],["dc.contributor.author","Tröder, Simon E."],["dc.contributor.author","Sprenger, Hans-Georg"],["dc.contributor.author","Quirós, Pedro M."],["dc.contributor.author","López-Otín, Carlos"],["dc.contributor.author","Rugarli, Elena I."],["dc.contributor.author","Langer, Thomas"],["dc.date.accessioned","2022-03-01T11:46:33Z"],["dc.date.available","2022-03-01T11:46:33Z"],["dc.date.issued","2016"],["dc.description.abstract","Proteolytic cleavage of the dynamin-like guanosine triphosphatase OPA1 in mitochondria is emerging as a central regulatory hub that determines mitochondrial morphology under stress and in disease. Stress-induced OPA1 processing by OMA1 triggersmitochondrial fragmentation, which is associated with mitophagy and apoptosis in vitro. Here, we identify OMA1 as a critical regulator of neuronal survival in vivo and demonstrate that stress-induced OPA1 processing by OMA1 promotes neuronal death and neuroinflammatory responses. Using mice lacking prohibitin membrane scaffolds as a model of neurodegeneration, we demonstrate that additional ablation of Oma1 delays neuronal loss and prolongs lifespan. This is accompanied by the accumulation of fusion-active, long OPA1 forms, which stabilize the mitochondrial genome but do not preserve mitochondrial cristae or respiratory chain supercomplex assembly in prohibitin-depleted neurons. Thus, long OPA1 forms can promote neuronal survival independently of cristae shape, whereas stress-induced OMA1 activation and OPA1 cleavage limit mitochondrial fusion and promote neuronal death."],["dc.description.abstract","Proteolytic cleavage of the dynamin-like guanosine triphosphatase OPA1 in mitochondria is emerging as a central regulatory hub that determines mitochondrial morphology under stress and in disease. Stress-induced OPA1 processing by OMA1 triggersmitochondrial fragmentation, which is associated with mitophagy and apoptosis in vitro. Here, we identify OMA1 as a critical regulator of neuronal survival in vivo and demonstrate that stress-induced OPA1 processing by OMA1 promotes neuronal death and neuroinflammatory responses. Using mice lacking prohibitin membrane scaffolds as a model of neurodegeneration, we demonstrate that additional ablation of Oma1 delays neuronal loss and prolongs lifespan. This is accompanied by the accumulation of fusion-active, long OPA1 forms, which stabilize the mitochondrial genome but do not preserve mitochondrial cristae or respiratory chain supercomplex assembly in prohibitin-depleted neurons. Thus, long OPA1 forms can promote neuronal survival independently of cristae shape, whereas stress-induced OMA1 activation and OPA1 cleavage limit mitochondrial fusion and promote neuronal death."],["dc.identifier.doi","10.1083/jcb.201507022"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103711"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1540-8140"],["dc.relation.issn","0021-9525"],["dc.title","Loss of OMA1 delays neurodegeneration by preventing stress-induced OPA1 processing in mitochondria"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1844"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","EMBO Reports"],["dc.bibliographiccitation.lastpage","1856"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Wai, Timothy"],["dc.contributor.author","Saita, Shotaro"],["dc.contributor.author","Nolte, Hendrik"],["dc.contributor.author","Mueller, Sebastian"],["dc.contributor.author","Koenig, Tim"],["dc.contributor.author","Richter-Dennerlein, Ricarda"],["dc.contributor.author","Sprenger, Hans-Georg"],["dc.contributor.author","Madrenas, Joaquin"],["dc.contributor.author","Muehlmeister, Mareike"],["dc.contributor.author","Brandt, Ulrich"],["dc.contributor.author","Krueger, Marcus"],["dc.contributor.author","Langer, Thomas"],["dc.date.accessioned","2018-11-07T10:05:17Z"],["dc.date.available","2018-11-07T10:05:17Z"],["dc.date.issued","2016"],["dc.description.abstract","The SPFH (stomatin, prohibitin, flotillin, HflC/K) superfamily is composed of scaffold proteins that form ring-like structures and locally specify the protein-lipid composition in a variety of cellular membranes. Stomatin-like protein 2 (SLP2) is a member of this superfamily that localizes to the mitochondrial inner membrane (IM) where it acts as a membrane organizer. Here, we report that SLP2 anchors a large protease complex composed of the rhomboid protease PARL and the i-AAA protease YME1L, which we term the SPY complex (for SLP2-PARL-YME1L). Association with SLP2 in the SPY complex regulates PARL-mediated processing of PTEN-induced kinase PINK1 and the phosphatase PGAM5 in mitochondria. Moreover, SLP2 inhibits the stress-activated peptidase OMA1, which can bind to SLP2 and cleaves PGAM5 in depolarized mitochondria. SLP2 restricts OMA1-mediated processing of the dynamin-like GTPase OPA1 allowing stress-induced mitochondrial hyperfusion under starvation conditions. Together, our results reveal an important role of SLP2 membrane scaffolds for the spatial organization of IM proteases regulating mitochondrial dynamics, quality control, and cell survival."],["dc.identifier.doi","10.15252/embr.201642698"],["dc.identifier.isi","000389329400020"],["dc.identifier.pmid","27737933"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38867"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1469-3178"],["dc.relation.issn","1469-221X"],["dc.title","The membrane scaffold SLP2 anchors a proteolytic hub in mitochondria containing PARL and the i-AAA protease YME1L"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.contributor.author","Nadler, Franziska"],["dc.contributor.author","Lavdovskaia, Elena"],["dc.contributor.author","Krempler, Angelique"],["dc.contributor.author","Cruz-Zaragoza, Luis Daniel"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Richter-Dennerlein, Ricarda"],["dc.date.accessioned","2022-08-24T05:56:01Z"],["dc.date.available","2022-08-24T05:56:01Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1101/2022.07.08.499411"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/113155"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/521"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.workinggroup","RG Richter-Dennerlein (Mitoribosome Assembly)"],["dc.title","Human mtRF1 terminates COX1 translation and its ablation induces mitochondrial ribosome-associated quality control"],["dc.type","preprint"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","158"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Cell Metabolism"],["dc.bibliographiccitation.lastpage","171"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Richter-Dennerlein, Ricarda"],["dc.contributor.author","Korwitz, Anne"],["dc.contributor.author","Haag, Mathias"],["dc.contributor.author","Tatsuta, Takashi"],["dc.contributor.author","Dargazanli, Sascha"],["dc.contributor.author","Baker, Michael"],["dc.contributor.author","Decker, Thorsten"],["dc.contributor.author","Lamkemeyer, Tobias"],["dc.contributor.author","Rugarli, Elena I."],["dc.contributor.author","Langer, Thomas"],["dc.date.accessioned","2022-03-01T11:45:05Z"],["dc.date.available","2022-03-01T11:45:05Z"],["dc.date.issued","2014"],["dc.identifier.doi","10.1016/j.cmet.2014.04.016"],["dc.identifier.pii","S155041311400182X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103208"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","1550-4131"],["dc.rights.uri","https://www.elsevier.com/tdm/userlicense/1.0/"],["dc.title","DNAJC19, a Mitochondrial Cochaperone Associated with Cardiomyopathy, Forms a Complex with Prohibitins to Regulate Cardiolipin Remodeling"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]