Denkert, Niels

[["dc.bibliographiccitation.firstpage","389"],["dc.bibliographiccitation.journal","FEBS Journal"],["dc.bibliographiccitation.lastpage","390"],["dc.bibliographiccitation.volume","282"],["dc.contributor.author","Barbot, M."],["dc.contributor.author","Jans, D. C."],["dc.contributor.author","Schulz, C."],["dc.contributor.author","Denkert, N."],["dc.contributor.author","Kroppen, B."],["dc.contributor.author","Hoppert, M."],["dc.contributor.author","Jakobs, Sebastian"],["dc.contributor.author","Meinecke, Michael"],["dc.date.accessioned","2018-11-07T09:54:51Z"],["dc.date.available","2018-11-07T09:54:51Z"],["dc.date.issued","2015"],["dc.identifier.isi","000362570607078"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36626"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.eventlocation","Berlin, GERMANY"],["dc.relation.issn","1742-4658"],["dc.relation.issn","1742-464X"],["dc.relation.orgunit","Institut für Zellbiochemie"],["dc.title","Mic10 oligomerizes to bend mitochondrial inner membranes at cristae junctions"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","756"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Cell Metabolism"],["dc.bibliographiccitation.lastpage","763"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Barbot, Mariam"],["dc.contributor.author","Jans, Daniel C."],["dc.contributor.author","Schulz, Christian"],["dc.contributor.author","Denkert, Niels"],["dc.contributor.author","Kroppen, Benjamin"],["dc.contributor.author","Hoppert, Michael"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Meinecke, Michael"],["dc.date.accessioned","2017-09-07T11:44:24Z"],["dc.date.available","2017-09-07T11:44:24Z"],["dc.date.issued","2015"],["dc.description.abstract","The mitochondrial inner membrane is highly folded and displays a complex molecular architecture. Cristae junctions are highly curved tubular openings that separate cristae membrane invaginations from the surrounding boundary membrane. Despite their central role in many vital cellular processes like apoptosis, the details of cristae junction formation remain elusive. Here we identify Mic10, a core subunit of the recently discovered MICOS complex, as an inner mitochondrial membrane protein with the ability to change membrane morphology in vitro and in vivo. We show that Mic10 spans the inner membrane in a hairpin topology and that its ability to sculpt membranes depends on oligomerization through a glycine-rich motif. Oligomerization mutants fail to induce curvature in model membranes, and when expressed in yeast, mitochondria display an altered inner membrane architecture characterized by drastically decreased numbers of cristae junctions. Thus, we demonstrate that membrane sculpting by Mic10 is essential for cristae junction formation."],["dc.identifier.doi","10.1016/j.cmet.2015.04.006"],["dc.identifier.gro","3141906"],["dc.identifier.isi","000353978700017"],["dc.identifier.pmid","25955211"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2389"],["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","1932-7420"],["dc.relation.issn","1550-4131"],["dc.relation.orgunit","Institut für Zellbiochemie"],["dc.title","Mic10 Oligomerizes to Bend Mitochondrial Inner Membranes at Cristae Junctions"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e28324"],["dc.bibliographiccitation.journal","eLife"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Denkert, Niels"],["dc.contributor.author","Schendzielorz, Alexander Benjamin"],["dc.contributor.author","Barbot, Mariam"],["dc.contributor.author","Versemann, Lennart"],["dc.contributor.author","Richter, Frank"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Meinecke, Michael"],["dc.date.accessioned","2020-12-10T18:48:05Z"],["dc.date.available","2020-12-10T18:48:05Z"],["dc.date.issued","2017"],["dc.description.abstract","Virtually all mitochondrial matrix proteins and a considerable number of inner membrane proteins carry a positively charged, N-terminal presequence and are imported by the TIM23 complex (presequence translocase) located in the inner mitochondrial membrane. The voltage-regulated Tim23 channel constitutes the actual protein-import pore wide enough to allow the passage of polypeptides with a secondary structure. In this study, we identify amino acids important for the cation selectivity of Tim23. Structure based mutants show that selectivity is provided by highly conserved, pore-lining amino acids. Mutations of these amino acid residues lead to reduced selectivity properties, reduced protein import capacity and they render the Tim23 channel insensitive to substrates. We thus show that the cation selectivity of the Tim23 channel is a key feature for substrate recognition and efficient protein import."],["dc.format.extent","1"],["dc.identifier.doi","10.7554/eLife.28324"],["dc.identifier.pmid","28857742"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16499"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/79012"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/12"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P12: Funktionelle Regulation der mitochondrialen Präsequenz-Translokase"],["dc.relation.eissn","2050-084X"],["dc.relation.orgunit","Institut für Zellbiochemie"],["dc.relation.workinggroup","RG Meinecke (Molecular Membrane Biology)"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject","S. cerevisiae; Tim23; biochemistry; biophysics; electrophysiology; membrane channels; mitochondria; mitochondrial biogenesis; protein trafficking; structural biology"],["dc.title","Cation selectivity of the presequence translocase channel Tim23 is crucial for efficient protein import"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]