Richter-Dennerlein, Ricarda

[["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.journal","eLife"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Poerschke, Sabine"],["dc.contributor.author","Oeljeklaus, Silke"],["dc.contributor.author","Wang, Cong"],["dc.contributor.author","Richter-Dennerlein, Ricarda"],["dc.contributor.author","Sattmann, Johannes"],["dc.contributor.author","Bauermeister, Diana"],["dc.contributor.author","Hanitsch, Elisa"],["dc.contributor.author","Stoldt, Stefan"],["dc.contributor.author","Langer, Thomas"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2022-02-01T10:31:53Z"],["dc.date.available","2022-02-01T10:31:53Z"],["dc.date.issued","2021"],["dc.description.abstract","Human mitochondria express a genome that encodes thirteen core subunits of the oxidative phosphorylation system (OXPHOS). These proteins insert into the inner membrane co-translationally. Therefore, mitochondrial ribosomes engage with the OXA1L-insertase and membrane-associated proteins, which support membrane insertion of translation products and early assembly steps into OXPHOS complexes. To identify ribosome-associated biogenesis factors for the OXPHOS system, we purified ribosomes and associated proteins from mitochondria. We identified TMEM223 as a ribosome-associated protein involved in complex IV biogenesis. TMEM223 stimulates the translation of COX1 mRNA and is a constituent of early COX1 assembly intermediates. Moreover, we show that SMIM4 together with C12ORF73 interacts with newly synthesized cytochrome b to support initial steps of complex III biogenesis in complex with UQCC1 and UQCC2. Our analyses define the interactome of the human mitochondrial ribosome and reveal novel assembly factors for complex III and IV biogenesis that link early assembly stages to the translation machinery."],["dc.identifier.doi","10.7554/eLife.68213"],["dc.identifier.pmid","34969438"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/98968"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/384"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/166"],["dc.identifier.url","https://for2848.gwdguser.de/literature/publications/7"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-517"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P13: Protein Transport über den mitochondrialen Carrier Transportweg"],["dc.relation","FOR 2848: Architektur und Heterogenität der inneren mitochondrialen Membran auf der Nanoskala"],["dc.relation","FOR 2848 | P04: Analyse der räumlichen Organisation der OXPHOS Assemblierung in Säugerzellen"],["dc.relation.eissn","2050-084X"],["dc.relation.workinggroup","RG Jakobs (Structure and Dynamics of Mitochondria)"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.relation.workinggroup","RG Richter-Dennerlein (Mitoribosome Assembly)"],["dc.relation.workinggroup","RG Langer (Mitochondrial Proteostasis)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","http://creativecommons.org/licenses/by/4.0/"],["dc.title","Defining the interactome of the human mitochondrial ribosome identifies SMIM4 and TMEM223 as respiratory chain assembly factors"],["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","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.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"]]