Schäfer, Jonas

[["dc.bibliographiccitation.firstpage","18604"],["dc.bibliographiccitation.issue","52"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","18613"],["dc.bibliographiccitation.volume","295"],["dc.contributor.author","Schäfer, Jonas"],["dc.contributor.author","Förster, Lucas"],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Papadopoulos, Theofilos"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2021-04-14T08:25:50Z"],["dc.date.available","2021-04-14T08:25:50Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1074/jbc.RA120.015347"],["dc.identifier.pmid","33127642"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81745"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/62"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | A09: SUMOylation und Neddylation in Synapsen"],["dc.relation","SFB 1286 | B04: In vitro Rekonstitution von inhibitorischen GABAergen Postsynapsen"],["dc.relation.issn","0021-9258"],["dc.relation.workinggroup","RG Brose"],["dc.relation.workinggroup","RG Steinem (Biomolecular Chemistry)"],["dc.rights","CC BY 4.0"],["dc.title","Neuroligin-2 dependent conformational activation of collybistin reconstituted in supported hybrid membranes"],["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","1320"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Langmuir"],["dc.bibliographiccitation.lastpage","1328"],["dc.bibliographiccitation.volume","36"],["dc.contributor.author","Schäfer, Jonas"],["dc.contributor.author","Nehls, Jessica"],["dc.contributor.author","Schön, Markus"],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2020-12-10T15:22:49Z"],["dc.date.available","2020-12-10T15:22:49Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1021/acs.langmuir.9b03793"],["dc.identifier.pmid","31951413"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73545"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/44"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | B04: In vitro Rekonstitution von inhibitorischen GABAergen Postsynapsen"],["dc.relation.workinggroup","RG Steinem (Biomolecular Chemistry)"],["dc.title","Leaflet-Dependent Distribution of PtdIns[4,5]P 2 in Supported Model Membranes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2710"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","2719"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Shabardina, Victoria"],["dc.contributor.author","Kramer, Corinna"],["dc.contributor.author","Gerdes, Benjamin"],["dc.contributor.author","Braunger, Julia A."],["dc.contributor.author","Cordes, Andrea"],["dc.contributor.author","Schäfer, Jonas"],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Grill, David"],["dc.contributor.author","Gerke, Volker"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2017-09-07T11:44:51Z"],["dc.date.available","2017-09-07T11:44:51Z"],["dc.date.issued","2016"],["dc.description.abstract","Ezrin, a protein of the ezrin, radixin, moesin (ERM) family, provides a regulated linkage between the plasma membrane and the cytoskeleton. The hallmark of this linkage is the activation of ezrin by phosphatidylinositol-4,5-bisphosphate (PIP2) binding and a threonine phosphorylation at position 567. To analyze the influence of these activating factors on the organization of ezrin on lipid membranes and the proposed concomitant oligomer-monomer transition, we made use of supported lipid bilayers in conjunction with atomic force microscopy and fluorescence microscopy. Bilayers doped with either PIP2 as the natural receptor lipid of ezrin or a Ni-nitrilotriacetic acid-equipped lipid to bind the proteins via their His6-tags to the lipid membrane were used to bind two different ezrin variants: ezrin wild-type and ezrin T567D mimicking the phosphorylated state. Using a combination of reflectometric interference spectroscopy, atomic force microscopy, and Forster resonance energy transfer experiments, we show that only the ezrin T567D mutant, upon binding to PIP2-containing bilayers, undergoes a remarkable conformational change, which we attribute to an opening of the conformation resulting in monomeric protein on the lipid bilayer."],["dc.identifier.doi","10.1016/j.bpj.2016.05.009"],["dc.identifier.gro","3141663"],["dc.identifier.isi","000378383300018"],["dc.identifier.pmid","27332129"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6786"],["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","1542-0086"],["dc.relation.issn","0006-3495"],["dc.title","Mode of Ezrin-Membrane Interaction as a Function of PIP2 Binding and Pseudophosphorylation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]