Meinecke, Michael

[["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","274"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Nature Cell Biology"],["dc.bibliographiccitation.lastpage","281"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Vasic, Vedran"],["dc.contributor.author","Denkert, Niels"],["dc.contributor.author","Schmidt, Claudia C."],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Stein, Alexander"],["dc.contributor.author","Meinecke, Michael"],["dc.date.accessioned","2021-04-14T08:27:11Z"],["dc.date.available","2021-04-14T08:27:11Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1038/s41556-020-0473-4"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82199"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1476-4679"],["dc.relation.issn","1465-7392"],["dc.relation.orgunit","Institut für Zellbiochemie"],["dc.title","Hrd1 forms the retrotranslocation pore regulated by auto-ubiquitination and binding of misfolded proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["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.issue","0"],["dc.bibliographiccitation.journal","Biological Chemistry"],["dc.bibliographiccitation.volume","0"],["dc.contributor.author","Ghosh, Mausumi"],["dc.contributor.author","Denkert, Niels"],["dc.contributor.author","Reuter, Maren"],["dc.contributor.author","Klümper, Jessica"],["dc.contributor.author","Reglinski, Katharina"],["dc.contributor.author","Peschel, Rebecca"],["dc.contributor.author","Schliebs, Wolfgang"],["dc.contributor.author","Erdmann, Ralf"],["dc.contributor.author","Meinecke, Michael"],["dc.date.accessioned","2022-09-01T09:51:01Z"],["dc.date.available","2022-09-01T09:51:01Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract\n Peroxisomal matrix proteins are synthesized on cytosolic ribosomes and imported in a posttranslational manner. Intricate protein import machineries have evolved that catalyze the different stages of translocation. In humans, PEX5L was found to be an essential component of the peroxisomal translocon. PEX5L is the main receptor for substrate proteins carrying a peroxisomal targeting signal (PTS). Substrates are bound by soluble PEX5L in the cytosol after which the cargo-receptor complex is recruited to peroxisomal membranes. Here, PEX5L interacts with the docking protein PEX14 and becomes part of an integral membrane protein complex that facilitates substrate translocation into the peroxisomal lumen in a still unknown process. In this study, we show that PEX5L containing complexes purified from human peroxisomal membranes constitute water-filled pores when reconstituted into planar-lipid membranes. Channel characteristics were highly dynamic in terms of conductance states, selectivity and voltage- and substrate-sensitivity. Our results show that a PEX5L associated pore exists in human peroxisomes, which can be activated by receptor-cargo complexes."],["dc.identifier.doi","10.1515/hsz-2022-0170"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/113861"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-597"],["dc.relation.eissn","1437-4315"],["dc.relation.issn","1431-6730"],["dc.title","Dynamics of the translocation pore of the human peroxisomal protein import machinery"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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"]]

[["dc.bibliographiccitation.firstpage","10568"],["dc.bibliographiccitation.issue","21"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","10575"],["dc.bibliographiccitation.volume","116"],["dc.contributor.author","Guan, Li"],["dc.contributor.author","Denkert, Niels"],["dc.contributor.author","Eisa, Ahmed"],["dc.contributor.author","Lehmann, Martin"],["dc.contributor.author","Sjuts, Inga"],["dc.contributor.author","Weiberg, Arne"],["dc.contributor.author","Soll, Jürgen"],["dc.contributor.author","Meinecke, Michael"],["dc.contributor.author","Schwenkert, Serena"],["dc.date.accessioned","2020-12-10T18:12:53Z"],["dc.date.available","2020-12-10T18:12:53Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1073/pnas.1900482116"],["dc.identifier.pmid","31068459"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74523"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/68"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P12: Funktionelle Regulation der mitochondrialen Präsequenz-Translokase"],["dc.relation.orgunit","Institut für Zellbiochemie"],["dc.relation.workinggroup","RG Meinecke (Molecular Membrane Biology)"],["dc.title","JASSY, a chloroplast outer membrane protein required for jasmonate biosynthesis"],["dc.type","journal_article"],["dc.type.internalPublication","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"]]