Barbot, Mariam

[["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.journal","European Biophysics Journal"],["dc.bibliographiccitation.volume","44"],["dc.contributor.author","Gleisner, M."],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Barbot, M."],["dc.contributor.author","Dreker, C."],["dc.contributor.author","Meinecke, Michael"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2018-11-07T09:55:32Z"],["dc.date.available","2018-11-07T09:55:32Z"],["dc.date.issued","2015"],["dc.format.extent","S78"],["dc.identifier.isi","000380001400135"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36765"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New York"],["dc.relation.eventlocation","Dresden"],["dc.relation.issn","1432-1017"],["dc.relation.issn","0175-7571"],["dc.relation.orgunit","Institut für Zellbiochemie"],["dc.title","Impact of the ENTH domain on protruded pore spanning membranes"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","20"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Structural Biology"],["dc.bibliographiccitation.lastpage","28"],["dc.bibliographiccitation.volume","196"],["dc.contributor.author","Barbot, Mariam"],["dc.contributor.author","Meinecke, Michael"],["dc.date.accessioned","2018-11-07T10:08:00Z"],["dc.date.available","2018-11-07T10:08:00Z"],["dc.date.issued","2016"],["dc.description.abstract","Biological membranes exhibit function-related shapes, leading to a plethora of complex and beautiful cell and cell organellar morphologies. Most if not all of these structures have evolved for a particular physiological reason. The shapes of these structures are formed by physical forces that operate on membranes. To create particular shaped cells and cell organelles, membranes must undergo deformations which are determined by the structure and elasticity of the membrane and this process is most probable driven by proteins, lipids and/or interplay of both Zimmerberg and Kozlov (2006). Therefore, an important question of current cell biology in conjunction with physics and mathematics is to elucidate the functional cause for these different membrane morphologies as well as how they are formed. One of the most peculiar membrane shapes is observed in mitochondria. These organelles are surrounded by two membranes and especially the convoluted inner membrane displays a complex ultra structure. A molecular understanding of how this membrane is shaped is missing to a large extent. Unlike membrane remodeling in classical curvature-dependent processes like clathrin-mediated endocytosis, mitochondria are most likely shaped by integral membrane proteins. Following, we will review the current knowledge of inner mitochondrial membrane architecture and discuss recent findings and advances in understanding the factors that shape this membrane. We will address pending questions especially with regard to the experimentally challenging nature of investigating membrane bending by hydrophobic integral membrane proteins. (C) 2016 Elsevier Inc. All rights reserved."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [SFB803, FOR1905, SFB1190]"],["dc.identifier.doi","10.1016/j.jsb.2016.07.014"],["dc.identifier.isi","000384275700004"],["dc.identifier.pmid","27456366"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39390"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/2"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P12: Funktionelle Regulation der mitochondrialen Präsequenz-Translokase"],["dc.relation.issn","1095-8657"],["dc.relation.issn","1047-8477"],["dc.relation.orgunit","Institut für Zellbiochemie"],["dc.relation.workinggroup","RG Meinecke (Molecular Membrane Biology)"],["dc.title","Reconstitutions of mitochondrial inner membrane remodeling"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","overview_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Tarasenko, D."],["dc.contributor.author","Barbot, M."],["dc.contributor.author","Jans, D. C."],["dc.contributor.author","Kroppen, B."],["dc.contributor.author","Heim, Gudrun"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Jakobs, Sebastian"],["dc.contributor.author","Meinecke, Michael"],["dc.date.accessioned","2018-11-07T10:19:35Z"],["dc.date.available","2018-11-07T10:19:35Z"],["dc.date.issued","2016"],["dc.identifier.isi","000396046900520"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41694"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Cell Biology"],["dc.publisher.place","Bethesda"],["dc.relation.conference","Annual Meeting of the American-Society-for-Cell-Biology (ASCB)"],["dc.relation.eventlocation","San Francisco, CA"],["dc.relation.issn","1939-4586"],["dc.relation.issn","1059-1524"],["dc.relation.orgunit","Institut für Zellbiochemie"],["dc.title","A conserved membrane bending activity of Mic60 is necessary for cristae formation."],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]