Vink, Richard L. C.

[["dc.bibliographiccitation.firstpage","634a"],["dc.bibliographiccitation.issue","2, Supplement 1"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","634a"],["dc.bibliographiccitation.volume","106"],["dc.contributor.author","Honigmann, Alf"],["dc.contributor.author","Sadeghi, Sina"],["dc.contributor.author","Jan, Keller"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Vink, Richard"],["dc.date.accessioned","2017-09-07T11:53:03Z"],["dc.date.available","2017-09-07T11:53:03Z"],["dc.date.issued","2014"],["dc.description.abstract","The cytoplasmic side of eukaryotic cell membranes is covered by a dense actin rich cortex. We present FCS and STED experiments showing that a dense membrane bound actin network has severe influence on temperature dependent lipid phase separation. A minimal actin cortex was bound to a supported lipid bilayer via biotinylated lipid streptavidin complexes (pinning sites). In general, actin binding to ternary membranes prevented macroscopic liquid-ordered (Lo) and liquid-disordered (Ld) domain formation in these systems, even at low temperature. For pinning sites that strongly attract Ld domains, an actin correlated multi-domain pattern was observed, consisting of Ld “channels” along the actin fibers, with Lo “islands” in the voids. FCS measurements revealed enhanced diffusion of unsaturated lipids along the channels, and hindered diffusion of these lipids in directions perpendicular. For pinning sites strongly attractive to Lo domains, an “inverse” domain structure was observed. These findings are in good agreement with a number of recently proposed simulation models. However, to fully capture our experimental observations, an extended simulation model is proposed, in which the lipid domains also couple to the local membrane curvature. Our results provide a mechanism how cells may prevent macroscopic de-mixing of membrane components and at the same time regulate the local membrane compositions."],["dc.identifier.doi","10.1016/j.bpj.2013.11.3506"],["dc.identifier.gro","3145018"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2708"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","0006-3495"],["dc.title","A Lipid Bound Actin Meshwork Organizes Liquid Phase Separation in Model Membranes"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e01671"],["dc.bibliographiccitation.journal","eLife"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Honigmann, Alf"],["dc.contributor.author","Sadeghi, Sina"],["dc.contributor.author","Keller, Jan"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Vink, Richard"],["dc.date.accessioned","2017-09-07T11:46:25Z"],["dc.date.available","2017-09-07T11:46:25Z"],["dc.date.issued","2014"],["dc.description.abstract","The eukaryotic cell membrane is connected to a dense actin rich cortex. We present FCS and STED experiments showing that dense membrane bound actin networks have severe influence on lipid phase separation. A minimal actin cortex was bound to a supported lipid bilayer via biotinylated lipid streptavidin complexes (pinning sites). In general, actin binding to ternary membranes prevented macroscopic liquid-ordered and liquid-disordered domain formation, even at low temperature. Instead, depending on the type of pinning lipid, an actin correlated multi-domain pattern was observed. FCS measurements revealed hindered diffusion of lipids in the presence of an actin network. To explain our experimental findings, a new simulation model is proposed, in which the membrane composition, the membrane curvature, and the actin pinning sites are all coupled. Our results reveal a mechanism how cells may prevent macroscopic demixing of their membrane components, while at the same time regulate the local membrane composition."],["dc.identifier.doi","10.7554/eLife.01671"],["dc.identifier.fs","605546"],["dc.identifier.gro","3142167"],["dc.identifier.isi","000333192500001"],["dc.identifier.pmid","24642407"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10516"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5277"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Elife Sciences Publications Ltd"],["dc.relation.issn","2050-084X"],["dc.relation.orgunit","Fakultät für Physik"],["dc.rights","CC BY 3.0"],["dc.title","A lipid bound actin meshwork organizes liquid phase separation in model membranes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]