Meinecke, Michael

[["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.volume","42"],["dc.contributor.author","Gleisner, M."],["dc.contributor.author","Dreker, C."],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Meinecke, Michael"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2018-11-07T09:22:32Z"],["dc.date.available","2018-11-07T09:22:32Z"],["dc.date.issued","2013"],["dc.format.extent","S122"],["dc.identifier.isi","000330215300334"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29365"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.relation.eventlocation","Lisbon, PORTUGAL"],["dc.relation.issn","1432-1017"],["dc.relation.issn","0175-7571"],["dc.relation.orgunit","Institut für Zellbiochemie"],["dc.title","Pore spanning membranes as a model system for the selective generation of membrane curvature"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","6228"],["dc.bibliographiccitation.issue","33"],["dc.bibliographiccitation.journal","Soft Matter"],["dc.bibliographiccitation.lastpage","6236"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Gleisner, Martin"],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Barbot, Mariam"],["dc.contributor.author","Dreker, Christina"],["dc.contributor.author","Meinecke, Michael"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2017-09-07T11:46:54Z"],["dc.date.available","2017-09-07T11:46:54Z"],["dc.date.issued","2014"],["dc.description.abstract","The generation of a regular array of micrometre-sized pore-spanning membranes that protrude from the underlying surface as a function of osmotic pressure is reported. Giant unilamellar vesicles are spread onto non-functionalized Si/SiO2 substrates containing a highly ordered array of cavities with pore diameters of 850 nm, an interpore distance of 4 mm and a pore depth of 10 mm. The shape of the resulting pore-spanning membranes is controlled by applying an osmotic pressure difference between the bulk solution and the femtoliter-sized cavity underneath each membrane. By applying Young-Laplace's law assuming moderate lateral membrane tensions, the response of the membranes to the osmotic pressure difference can be theoretically well described. Protruded pore-spanning membranes containing the receptor lipid PIP2 specifically bind the ENTH domain of epsin resulting in an enlargement of the protrusions and disappearance as a result of ENTH-domain induced defects in the membranes. These results are discussed in the context of an ENTH-domain induced reduction of lateral membrane tension and formation of defects as a result of helix insertion of the protein in the bilayer."],["dc.identifier.doi","10.1039/c4sm00702f"],["dc.identifier.fs","606035"],["dc.identifier.gro","3142206"],["dc.identifier.isi","000340438600011"],["dc.identifier.pmid","25012509"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11470"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5710"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: DFG [SFB 803]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1744-6848"],["dc.relation.issn","1744-683X"],["dc.relation.orgunit","Institut für Zellbiochemie"],["dc.rights.access","openAccess"],["dc.title","Driving a planar model system into the 3rd dimension: generation and control of curved pore-spanning membrane arrays"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","233"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Soft Matter"],["dc.bibliographiccitation.lastpage","240"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Meinecke, Michael"],["dc.date.accessioned","2021-04-14T08:30:16Z"],["dc.date.available","2021-04-14T08:30:16Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1039/c9sm02437a"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83172"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1744-6848"],["dc.relation.issn","1744-683X"],["dc.relation.orgunit","Institut für Zellbiochemie"],["dc.title","ENTH domain-dependent membrane remodelling"],["dc.type","journal_article"],["dc.type.internalPublication","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","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","19953"],["dc.bibliographiccitation.issue","38"],["dc.bibliographiccitation.journal","The Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","19961"],["dc.bibliographiccitation.volume","291"],["dc.contributor.author","Gleisner, Martin"],["dc.contributor.author","Kroppen, Benjamin"],["dc.contributor.author","Fricke, Christian"],["dc.contributor.author","Teske, Nelli"],["dc.contributor.author","Kliesch, Torben-Tobias"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Meinecke, Michael"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2020-12-10T18:12:56Z"],["dc.date.available","2020-12-10T18:12:56Z"],["dc.date.issued","2016"],["dc.description.abstract","The epsin N-terminal homology domain (ENTH) is a major player in clathrin-mediated endocytosis. To investigate the influence of initial membrane tension on ENTH binding and activity, we established a bilayer system based on adhered giant unilamellar vesicles (GUVs) to be able to control and adjust the membrane tension sigma covering a broad regime. The shape of each individual adhered GUV as well as its adhesion area was monitored by spinning disc confocal laser microscopy. Control of sigma in a range of 0.08-1.02 mN/m was achieved by altering the Mg2+ concentration in solution, which changes the surface adhesion energy per unit area of the GUVs. Specific binding of ENTH to phosphatidylinositol 4,5-bisphosphate leads to a substantial increase in adhesion area of the sessile GUV. At low tension (<0.1 mN/m) binding of ENTH can induce tubular structures, whereas at higher membrane tension the ENTH interaction deflates the sessile GUV and thereby increases the adhesion area. The increase in adhesion area is mainly attributed to a decrease in the area compressibility modulus K-A. We propose that the insertion of the ENTH helix-0 into the membrane is largely responsible for the observed decrease in K-A, which is supported by the observation that the mutant ENTH L6E shows a reduced increase in adhesion area. These results demonstrate that even in the absence of tubule formation, the area compressibility modulus and, as such, the bending rigidity of the membrane is considerably reduced upon ENTH binding. This renders membrane bending and tubule formation energetically less costly."],["dc.identifier.doi","10.1074/jbc.M116.731612"],["dc.identifier.eissn","1083-351X"],["dc.identifier.gro","3141621"],["dc.identifier.isi","000383243100019"],["dc.identifier.issn","0021-9258"],["dc.identifier.pmid","27466364"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74538"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1083-351X"],["dc.relation.issn","0021-9258"],["dc.relation.orgunit","Institut für Zellbiochemie"],["dc.title","Epsin N-terminal Homology Domain (ENTH) Activity as a Function of Membrane Tension"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]