Köster, Sarah

[["dc.bibliographiccitation.artnumber","188102"],["dc.bibliographiccitation.issue","18"],["dc.bibliographiccitation.journal","Physical Review Letters"],["dc.bibliographiccitation.volume","123"],["dc.contributor.author","Lorenz, Charlotta"],["dc.contributor.author","Forsting, Johanna"],["dc.contributor.author","Schepers, Anna V."],["dc.contributor.author","Kraxner, Julia"],["dc.contributor.author","Bauch, Susanne"],["dc.contributor.author","Witt, Hannes"],["dc.contributor.author","Klumpp, Stefan"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2020-12-10T18:25:50Z"],["dc.date.available","2020-12-10T18:25:50Z"],["dc.date.issued","2019"],["dc.description.abstract","The cytoskeleton is a composite network of three types of protein filaments, among which intermediate filaments (IFs) are the most extensible ones. Two very important IFs are keratin and vimentin, which have similar molecular architectures but different mechanical behaviors. Here we compare the mechanical response of single keratin and vimentin filaments using optical tweezers. We show that the mechanics of vimentin strongly depends on the ionic strength of the buffer and that its force-strain curve suggests a high degree of cooperativity between subunits. Indeed, a computational model indicates that in contrast to keratin, vimentin is characterized by strong lateral subunit coupling of its charged monomers during unfolding of α helices. We conclude that cells can tune their mechanics by differential use of keratin versus vimentin."],["dc.identifier.doi","10.1103/PhysRevLett.123.188102"],["dc.identifier.eissn","1079-7114"],["dc.identifier.issn","0031-9007"],["dc.identifier.pmid","31763918"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75854"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation","info:eu-repo/grantAgreement/EC/H2020/724932/EU//MECHANICS"],["dc.relation.eissn","1079-7114"],["dc.relation.issn","0031-9007"],["dc.relation.orgunit","Fakultät für Physik"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.access","openAccess"],["dc.rights.uri","http://creativecommons.org/licenses/by-nc-nd/4.0/"],["dc.subject","intermediate filaments; optical tweezers; atomic force microscopy; cytoskeleton; biomechanics; Monte Carlo simulation"],["dc.subject.ddc","530"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","cellular biophysics"],["dc.title","Lateral Subunit Coupling Determines Intermediate Filament Mechanics"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dc.type.version","submitted_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","735"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Lab on a Chip"],["dc.bibliographiccitation.lastpage","745"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Perego, Eleonora"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2021-04-14T08:28:33Z"],["dc.date.available","2021-04-14T08:28:33Z"],["dc.date.issued","2021"],["dc.description.abstract","Despite the importance for cellular processes, the dynamics of molecular assembly, especially on fast time scales, is not yet fully understood. To this end, we present a multi-layer microfluidic device and combine it with fluorescence fluctuation spectroscopy. We apply this innovative combination of methods to investigate the early steps in assembly of vimentin intermediate filaments (IFs). These filaments, together with actin filaments and microtubules, constitute the cytoskeleton of cells of mesenchymal origin and greatly influence their mechanical properties. We are able to directly follow the two-step assembly process of vimentin IFs and quantify the time scale of the first lateral step to tens of ms with a lag time of below 3 ms. Although demonstrated for a specific biomolecular system here, our method may potentially be employed for a wide range of fast molecular reactions in biological or, more generally, soft matter systems, as it allows for a precise quantification of the kinetics underlying the aggregation and assembly."],["dc.identifier.doi","10.1039/d0lc00985g"],["dc.identifier.pmid","33491697"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82646"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/116"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/89"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | B02: Ein in vitro-Verfahren zum Verständnis der struktur-organisierenden Rolle des Vesikel-Clusters"],["dc.relation.eissn","1473-0189"],["dc.relation.issn","1473-0197"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.rights","CC BY 3.0"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","molecular biophysics"],["dc.subject.gro","microfluidics"],["dc.title","Exploring early time points of vimentin assembly in flow by fluorescence fluctuation spectroscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","eaat1161"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Science Advances"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Block, Johanna"],["dc.contributor.author","Witt, Hannes"],["dc.contributor.author","Candelli, Andrea"],["dc.contributor.author","Danes, Jordi Cabanas"],["dc.contributor.author","Peterman, Erwin J. G."],["dc.contributor.author","Wuite, Gijs J. L."],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2019-07-09T11:45:54Z"],["dc.date.available","2019-07-09T11:45:54Z"],["dc.date.issued","2018"],["dc.description.abstract","Structure and dynamics of living matter rely on design principles fundamentally different from concepts of traditional material science. Specialized intracellular filaments in the cytoskeleton permit living systems to divide, migrate, and growwith a high degree of variability and durability. Among the three filament systems,microfilaments,microtubules, and intermediate filaments (IFs), the physical properties of IFs and their role in cellular mechanics are the least well understood. We use optical trapping of individual vimentin filaments to investigate energy dissipation, strain history dependence, and creep behavior of stretched filaments. By stochastic and numerical modeling, we link our experimental observations to the peculiar molecular architecture of IFs. We find that individual vimentin filaments display tensile memory and are able to dissipate more than 70% of the input energy.We attribute these phenomena to distinct nonequilibrium folding and unfolding of a helices in the vimentin monomers constituting the filaments."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2018"],["dc.identifier.doi","10.1126/sciadv.aat1161"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15341"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59334"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","2375-2548"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.orgunit","Fakultät für Physik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.rights","CC BY-NC 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","530"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","cellular biophysics"],["dc.title","Viscoelastic properties of vimentin originate from nonequilibrium conformational changes"],["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","2693"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","2699"],["dc.bibliographiccitation.volume","107"],["dc.contributor.author","Nolting, Jens-Friedrich"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2017-09-07T11:45:22Z"],["dc.date.available","2017-09-07T11:45:22Z"],["dc.date.issued","2014"],["dc.description.abstract","Along with microtubules and microfilaments, intermediate filaments are a major component of the eukaryotic cytoskeleton and play a key role in cell mechanics. In cells, keratin intermediate filaments form networks of bundles that are sparser in structure and have lower connectivity than, for example, actin networks. Because of this, bending and buckling play an important role in these networks. Buckling events, which occur due to compressive intracellular forces and cross-talk between the keratin network and other cytoskeletal components, are measured here in situ. By applying a mechanical model for the bundled filaments, we can access the mechanical properties of both the keratin bundles themselves and the surrounding cytosol. Bundling is characterized by a coupling parameter that describes the strength of the linkage between the individual filaments within a bundle. Our findings suggest that coupling between the filaments is mostly complete, although it becomes weaker for thicker bundles, with some relative movement allowed."],["dc.identifier.doi","10.1016/j.bpj.2014.10.039"],["dc.identifier.gro","3142001"],["dc.identifier.isi","000345859500029"],["dc.identifier.pmid","25468348"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3445"],["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.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.rights","CC BY-NC-ND 3.0"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","cellular biophysics"],["dc.title","Mechanics of Individual Keratin Bundles in Living Cells"],["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.artnumber","048101"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Physical Review Letters"],["dc.bibliographiccitation.lastpage","5"],["dc.bibliographiccitation.volume","118"],["dc.contributor.author","Block, Johanna"],["dc.contributor.author","Witt, Hannes"],["dc.contributor.author","Candelli, Andrea"],["dc.contributor.author","Peterman, Erwin J. G."],["dc.contributor.author","Wuite, Gijs J. L."],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2020-12-10T18:25:42Z"],["dc.date.available","2020-12-10T18:25:42Z"],["dc.date.issued","2017"],["dc.description.abstract","The mechanical properties of eukaryotic cells are to a great extent determined by the cytoskeleton, a composite network of different filamentous proteins. Among these, intermediate filaments (IFs) are exceptional in their molecular architecture and mechanical properties. Here we directly record stress-strain curves of individual vimentin IFs using optical traps and atomic force microscopy. We find a strong loading rate dependence of the mechanical response, supporting the hypothesis that IFs could serve to protect eukaryotic cells from fast, large deformations. Our experimental results show different unfolding regimes, which we can quantitatively reproduce by an elastically coupled system of multiple two-state elements."],["dc.identifier.doi","10.1103/PhysRevLett.118.048101"],["dc.identifier.eissn","1079-7114"],["dc.identifier.fs","623737"],["dc.identifier.issn","0031-9007"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17056"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75797"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.eissn","1079-7114"],["dc.relation.issn","0031-9007"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0/"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","cellular biophysics"],["dc.title","Nonlinear Loading-Rate-Dependent Force Response of Individual Vimentin Intermediate Filaments to Applied Strain"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","unknown"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2681"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","Lab on a Chip"],["dc.bibliographiccitation.lastpage","2687"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Dammann, Christian"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2017-09-07T11:45:39Z"],["dc.date.available","2017-09-07T11:45:39Z"],["dc.date.issued","2014"],["dc.description.abstract","Intermediate filaments (IFs) are fiber-forming proteins and part of the cytoskeleton of eukaryotes. In vitro the network formation of purified IF systems is mediated, for example, by the interaction with multivalent ions. The understanding of these interaction mechanisms increases the knowledge of the cytoskeleton on a fundamental level. Here, we employ time-lapse fluorescence microscopy to directly image the evolution of network formation of vimentin IFs upon addition of divalent ions. We are thus able to follow the process starting a few seconds after the first encounter of free filaments and ions up to several minutes when the networks are in equilibrium. The local protein density in the compacted networks can reach a factor of 45 higher than the original solution concentration. The competition between mono- and divalent ion condensation onto the protein explains our observations and reveals the polyelectrolyte nature of vimentin as a reason for the protein attraction in the presence of small cations. The method for time-lapse studies in microfluidic drops presented here can be generalized to other dynamic systems."],["dc.identifier.doi","10.1039/c3lc51418h"],["dc.identifier.fs","606787"],["dc.identifier.gro","3142079"],["dc.identifier.isi","000339306700012"],["dc.identifier.pmid","24834442"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11108"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4311"],["dc.language.iso","en"],["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.relation.eissn","1473-0189"],["dc.relation.issn","1473-0197"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.orgunit","Fakultät für Physik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.rights","CC BY 3.0"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","molecular biophysics"],["dc.subject.gro","microfluidics"],["dc.title","Dynamics of counterion-induced attraction between vimentin filaments followed in microfluidic drops"],["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.artnumber","085013"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.journal","New Journal of Physics"],["dc.bibliographiccitation.lastpage","16"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Weinhausen, Britta"],["dc.contributor.author","Nolting, Jens-Friedrich"],["dc.contributor.author","Olendrowitz, Christian"],["dc.contributor.author","Langfahl-Klabes, Jannick"],["dc.contributor.author","Reynolds, Michael"],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2017-09-07T11:48:27Z"],["dc.date.available","2017-09-07T11:48:27Z"],["dc.date.issued","2012"],["dc.description.abstract","The nano-scale structure of cytoskeletal biopolymers as well as sophisticated superstructures determine the versatile cellular shapes and specific mechanical properties. One example is keratin intermediate filaments in epithelial cells, which form thick bundles that can further organize in a cross-linked network. To study the native structure of keratin bundles in whole cells, high-resolution techniques are required, which do at the same time achieve high penetration depths. We employ scanning x-ray diffraction using a nano-focused x-ray beam to study the structure of keratin in freeze-dried eukaryotic cells. By scanning the sample through the beam we obtain x-ray dark-field images with a resolution of the order of the beam size, which clearly show the keratin network. Each individual diffraction pattern is further analyzed to yield insight into the local sample structure, which allows us to determine the local structure orientation. Due to the small beam size we access the structure in a small sample volume without performing the ensemble average over one complete cell."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2012"],["dc.identifier.doi","10.1088/1367-2630/14/8/085013"],["dc.identifier.gro","3142479"],["dc.identifier.isi","000307837200004"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8388"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8740"],["dc.language.iso","en"],["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.relation.issn","1367-2630"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.orgunit","Fakultät für Physik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.subject.gro","x-ray imaging"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","cellular biophysics"],["dc.title","X-Ray Nano-Diffraction on Cytoskeletal Networks"],["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","380"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nanoscale"],["dc.bibliographiccitation.lastpage","387"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Kraxner, Julia"],["dc.contributor.author","Lorenz, Charlotta"],["dc.contributor.author","Menzel, Julia"],["dc.contributor.author","Parfentev, Iwan"],["dc.contributor.author","Silbern, Ivan"],["dc.contributor.author","Denz, Manuela"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2021-09-01T06:42:51Z"],["dc.date.available","2021-09-01T06:42:51Z"],["dc.date.issued","2021"],["dc.description.abstract","The mechanical properties of biological cells are determined by the cytoskeleton, a composite biopolymer network consisting of microtubules, actin filaments and intermediate filaments (IFs). By differential expression of cytoskeletal proteins, modulation of the network architecture and interactions between the filaments, cell mechanics may be adapted to varying requirements on the cell. Here, we focus on the intermediate filament protein vimentin and introduce post-translational modifications as an additional, much faster mechanism for mechanical modulation. We study the impact of phosphorylation on filament mechanics by recording force-strain curves using optical traps. Partial phosphorylation softens the filaments. We show that binding of the protein 14-3-3 to phosphorylated vimentin IFs further enhances this effect and speculate that in the cell 14-3-3 may serve to preserve the softening and thereby the altered cell mechanics. We explain our observation by the additional charges introduced during phosphorylation."],["dc.identifier.doi","10.1039/D0NR07322A"],["dc.identifier.pmid","33351020"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/89158"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/132"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/91"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-455"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | A08: Die Rolle post-translational modifizierter Proteine in der synaptischen Übertragung"],["dc.relation.eissn","2040-3372"],["dc.relation.issn","2040-3364"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.rights","CC BY 3.0"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","cellular biophysics"],["dc.title","Post-translational modifications soften vimentin intermediate filaments"],["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","708"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Lab on a Chip"],["dc.bibliographiccitation.lastpage","716"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Brennich, Martha Elisabeth"],["dc.contributor.author","Nolting, Jens-Friedrich"],["dc.contributor.author","Dammann, Christian"],["dc.contributor.author","Noeding, Bernd"],["dc.contributor.author","Bauch, Susanne"],["dc.contributor.author","Herrmann, Harald"],["dc.contributor.author","Pfohl, Thomas"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2017-09-07T11:45:07Z"],["dc.date.available","2017-09-07T11:45:07Z"],["dc.date.issued","2011"],["dc.description.abstract","The assembly of intermediate filaments (IFs) is a complex process that can be recapitulated through a series of distinct steps in vitro. The combination of microfluidics and small angle X-ray scattering (SAXS) provides a powerful tool to investigate the kinetics of this process on the relevant timescales. Microfluidic mixers based on the principle of hydrodynamic focusing allow for precise control of the mixing of proteins and smaller reagents like ions. Here, we present a multi-layer device that prevents proteins from adsorbing to the channel walls by engulfing the protein jet with a fluid layer of buffer. To ensure compatibility with SAXS, the device is fabricated from UV-curable adhesive (NOA 81). To demonstrate the successful prevention of contact between the protein jet and the channel walls we measure the distribution of a fluorescent dye in the device by confocal microscopy at various flow speeds and compare the results to finite element method (FEM) simulations. The prevention of contact enables the investigation of the assembly of IFs in flow by gradually increasing the salt concentration in the protein jet. The diffusion of salt into the jet can be determined by FEM simulations. SAXS data are collected at different positions in the jet, corresponding to different salt concentrations, and they reveal distinct differences between the earliest assembly states. We find that the mean square radius of gyration perpendicular to the filament axis increases from 13 nm(2) to 58 nm(2) upon assembly. Thereby we provide dynamic structural data of a complex assembly process that was amenable up to now only by microscopic techniques."],["dc.identifier.doi","10.1039/c0lc00319k"],["dc.identifier.gro","3142804"],["dc.identifier.isi","000286765700019"],["dc.identifier.pmid","21212871"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10269"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/249"],["dc.language.iso","en"],["dc.notes","This publication is with permission of the rights owner freely accessible due to an Alliance licence and a national licence (funded by the DFG, German Research Foundation) respectively."],["dc.notes.intern","WoS Import 2017-03-10 / Funder: German Research Foundation (DFG) [SFB 755]; European Commission [226716]"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/226716/EU//ELISA"],["dc.relation.issn","1473-0197"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.orgunit","Fakultät für Physik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","molecular biophysics"],["dc.subject.gro","microfluidics"],["dc.subject.mesh","Adhesives"],["dc.subject.mesh","Adsorption"],["dc.subject.mesh","Finite Element Analysis"],["dc.subject.mesh","Fluorescein"],["dc.subject.mesh","Humans"],["dc.subject.mesh","Microfluidic Analytical Techniques"],["dc.subject.mesh","Recombinant Proteins"],["dc.subject.mesh","Scattering, Small Angle"],["dc.subject.mesh","Vimentin"],["dc.subject.mesh","X-Ray Diffraction"],["dc.title","Dynamics of intermediate filament assembly followed in micro-flow by small angle X-ray scattering"],["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.artnumber","3799"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Schaedel, Laura"],["dc.contributor.author","Lorenz, Charlotta"],["dc.contributor.author","Schepers, Anna V."],["dc.contributor.author","Klumpp, Stefan"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2021-06-21T06:06:57Z"],["dc.date.available","2021-06-21T06:06:57Z"],["dc.date.issued","2021"],["dc.description.abstract","The cytoskeleton determines cell mechanics and lies at the heart of important cellular functions. Growing evidence suggests that the manifold tasks of the cytoskeleton rely on the interactions between its filamentous components—actin filaments, intermediate filaments, and microtubules. However, the nature of these interactions and their impact on cytoskeletal dynamics are largely unknown. Here, we show in a reconstituted in vitro system that vimentin intermediate filaments stabilize microtubules against depolymerization and support microtubule rescue. To understand these stabilizing effects, we directly measure the interaction forces between individual microtubules and vimentin filaments. Combined with numerical simulations, our observations provide detailed insight into the physical nature of the interactions and how they affect microtubule dynamics. Thus, we describe an additional, direct mechanism by which cells establish the fundamental cross talk of cytoskeletal components alongside linker proteins. Moreover, we suggest a strategy to estimate the binding energy of tubulin dimers within the microtubule lattice."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.1038/s41467-021-23523-z"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87261"],["dc.relation.issn","2041-1723"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.rights","CC BY 4.0"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","cellular biophysics"],["dc.title","Vimentin intermediate filaments stabilize dynamic microtubules by direct interactions"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]