Brückner, Bastian Rouven

[["dc.bibliographiccitation.firstpage","6329"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Nano Letters"],["dc.bibliographiccitation.lastpage","6335"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Hubrich, Hanna"],["dc.contributor.author","Mey, Ingo P."],["dc.contributor.author","Brückner, Bastian R."],["dc.contributor.author","Mühlenbrock, Peter"],["dc.contributor.author","Nehls, Stefan"],["dc.contributor.author","Grabenhorst, Lennart"],["dc.contributor.author","Oswald, Tabea"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2020-11-05T15:08:07Z"],["dc.date.available","2020-11-05T15:08:07Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1021/acs.nanolett.0c01769"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/68468"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-352.7"],["dc.relation.eissn","1530-6992"],["dc.relation.issn","1530-6984"],["dc.title","Viscoelasticity of Native and Artificial Actin Cortices Assessed by Nanoindentation Experiments"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["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"]]

[["dc.bibliographiccitation.firstpage","623a"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Brueckner, Bastian"],["dc.contributor.author","Nehls, Stefan"],["dc.date.accessioned","2020-12-10T14:22:42Z"],["dc.date.available","2020-12-10T14:22:42Z"],["dc.date.issued","2016"],["dc.format.extent","623A"],["dc.identifier.doi","10.1016/j.bpj.2015.11.3341"],["dc.identifier.isi","000375143200139"],["dc.identifier.issn","0006-3495"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71702"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.publisher.place","Cambridge"],["dc.relation.eventlocation","Los Angeles, CA"],["dc.relation.issn","1542-0086"],["dc.relation.issn","0006-3495"],["dc.title","Homeostasis of Plasma Membrane Tension Through Surface Area Regulation in Epithelial Cells"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","14700"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Brueckner, Bastian Rouven"],["dc.contributor.author","Pietuch, Anna"],["dc.contributor.author","Nehls, Stefan"],["dc.contributor.author","Rother, Jan"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2018-11-07T09:50:22Z"],["dc.date.available","2018-11-07T09:50:22Z"],["dc.date.issued","2015"],["dc.description.abstract","Plasma membrane tension is responsible for a variety of cellular functions such as motility, cell division, and endocytosis. Since membrane tension is dominated by the attachment of the actin cortex to the inner leaflet of the plasma membrane, we investigated the importance of ezrin, a major cross-linker of the membrane-cytoskeleton interface, for cellular mechanics of confluent MDCK II cells. For this purpose, we carried out ezrin depletion experiments and also enhanced the number of active ezrin molecules at the interface. Mechanical properties were assessed by force indentation experiments followed by membrane tether extraction. PIP2 micelles were injected into individual living cells to reinforce the linkage between plasma membrane and actin-cortex, while weakening of this connection was reached by ezrin siRNA and administration of the inhibitors neomycin and NSC 668394, respectively. We observed substantial stiffening of cells and an increase in membrane tension after addition of PIP2 micelles. In contrast, reduction of active ezrin led to a decrease of membrane tension accompanied by loss of excess surface area, increase in cortical tension, remodelling of actin cytoskeleton, and reduction of cell height. The data confirm the importance of the ezrin-mediated connection between plasma membrane and cortex for cellular mechanics and cell morphology."],["dc.description.sponsorship","Open-Access Publikationsfonds 2015"],["dc.identifier.doi","10.1038/srep14700"],["dc.identifier.isi","000362173300001"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12274"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35692"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","2045-2322"],["dc.rights.access","openAccess"],["dc.title","Ezrin is a Major Regulator of Membrane Tension in Epithelial Cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]