Mey, Ingo P.

[["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"]]

[["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.volume","40"],["dc.contributor.author","Braunger, Julia A."],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2018-11-07T08:53:34Z"],["dc.date.available","2018-11-07T08:53:34Z"],["dc.date.issued","2011"],["dc.format.extent","40"],["dc.identifier.isi","000293637300018"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22440"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New York"],["dc.relation.eventlocation","Budapest, Hungary"],["dc.relation.issn","0175-7571"],["dc.title","Force spectroscopy at the membrane-cytoskeleton interface: interactions between ezrin and filamentous actin"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","9833"],["dc.bibliographiccitation.issue","14"],["dc.bibliographiccitation.journal","Journal of biological chemistry"],["dc.bibliographiccitation.lastpage","9843"],["dc.bibliographiccitation.volume","289"],["dc.contributor.author","Braunger, Julia A."],["dc.contributor.author","Brückner, Bastian R."],["dc.contributor.author","Nehls, Stefan"],["dc.contributor.author","Pietuch, Anna"],["dc.contributor.author","Gerke, Volker"],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2017-09-07T11:46:19Z"],["dc.date.available","2017-09-07T11:46:19Z"],["dc.date.issued","2014"],["dc.description.abstract","Background: Ezrin can establish a dynamic linkage between plasma membrane and cytoskeleton. Results: The individual bond strength between ezrin and F-actin is small, but the number of attachment sites is significantly altered by phosphatidylinositol 4,5-bisphosphate (PIP2). Conclusion: PIP2 activates ezrin to establish multiple weak ezrin/F-actin interactions. Significance: Plasma membrane tension is maintained by ezrin/F-actin interactions. Direct linkage between the plasma membrane and the actin cytoskeleton is controlled by the protein ezrin, a member of the ezrin-radixin-moesin protein family. To function as a membrane-cytoskeleton linker, ezrin needs to be activated in a process that involves binding of ezrin to phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphorylation of a conserved threonine residue. Here, we used colloidal probe microscopy to quantitatively analyze the interaction between ezrin and F-actin as a function of these activating factors. We show that the measured individual unbinding forces between ezrin and F-actin are independent of the activating parameters, in the range of approximately 50 piconewtons. However, the cumulative adhesion energy greatly increases in the presence of PIP2 demonstrating that a larger number of bonds between ezrin and F-actin has formed. In contrast, the phosphorylation state, represented by phosphor-mimetic mutants of ezrin, only plays a minor role in the activation process. These results are in line with in vivo experiments demonstrating that an increase in PIP2 concentration recruits more ezrin to the apical plasma membrane of polarized cells and significantly increases the membrane tension serving as a measure of the adhesion sites between the plasma membrane and the F-actin network."],["dc.identifier.doi","10.1074/jbc.M113.530659"],["dc.identifier.gro","3142143"],["dc.identifier.isi","000333807000033"],["dc.identifier.pmid","24500715"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5022"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [STE 884/11-1, GE 514/8-1, GE 514/9-1]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1083-351X"],["dc.relation.issn","0021-9258"],["dc.title","Phosphatidylinositol 4,5-Bisphosphate Alters the Number of Attachment Sites between Ezrin and Actin Filaments A COLLOIDAL PROBE STUDY "],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]