Kroppen, Benjamin

[["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.firstpage","2355"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Cellular and Molecular Life Sciences"],["dc.bibliographiccitation.lastpage","2370"],["dc.bibliographiccitation.volume","78"],["dc.contributor.author","Kroppen, Benjamin"],["dc.contributor.author","Teske, Nelli"],["dc.contributor.author","Yambire, King F."],["dc.contributor.author","Denkert, Niels"],["dc.contributor.author","Mukherjee, Indrani"],["dc.contributor.author","Tarasenko, Daryna"],["dc.contributor.author","Jaipuria, Garima"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Milosevic, Ira"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Meinecke, Michael"],["dc.date.accessioned","2021-04-14T08:23:40Z"],["dc.date.available","2021-04-14T08:23:40Z"],["dc.date.issued","2020"],["dc.description.abstract","Membrane remodeling is a critical process for many membrane trafficking events, including clathrin-mediated endocytosis. Several molecular mechanisms for protein-induced membrane curvature have been described in some detail. Contrary, the effect that the physico-chemical properties of the membrane have on these processes is far less well understood. Here, we show that the membrane binding and curvature-inducing ENTH domain of epsin1 is regulated by phosphatidylserine (PS). ENTH binds to membranes in a PI(4,5)P2-dependent manner but only induces curvature in the presence of PS. On PS-containing membranes, the ENTH domain forms rigid homo-oligomers and assembles into clusters. Membrane binding and membrane remodeling can be separated by structure-to-function mutants. Such oligomerization mutants bind to membranes but do not show membrane remodeling activity. In vivo, they are not able to rescue defects in epidermal growth factor receptor (EGFR) endocytosis in epsin knock-down cells. Together, these data show that the membrane lipid composition is important for the regulation of protein-dependent membrane deformation during clathrin-mediated endocytosis."],["dc.identifier.doi","10.1007/s00018-020-03647-z"],["dc.identifier.pmid","32997199"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81004"],["dc.identifier.url","https://for2848.gwdguser.de/literature/publications/21"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","FOR 2848: Architektur und Heterogenität der inneren mitochondrialen Membran auf der Nanoskala"],["dc.relation","FOR 2848 | P05: Molekulare Charakterisierung der MICOS abhängigen mitochondrialen Innenmembran-Biogenese."],["dc.relation.eissn","1420-9071"],["dc.relation.issn","1420-682X"],["dc.relation.orgunit","Institut für Zellbiochemie"],["dc.relation.workinggroup","RG Meinecke (Molecular Membrane Biology)"],["dc.rights","CC BY 4.0"],["dc.title","Cooperativity of membrane-protein and protein–protein interactions control membrane remodeling by epsin 1 and affects clathrin-mediated endocytosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]