Platen, Mitja

[["dc.bibliographiccitation.firstpage","519"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Traffic"],["dc.bibliographiccitation.lastpage","533"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Dannhauser, Philip N."],["dc.contributor.author","Platen, Mitja"],["dc.contributor.author","Boening, Heike"],["dc.contributor.author","Ungewickell, Huberta"],["dc.contributor.author","Schaap, Iwan Alexander Taco"],["dc.contributor.author","Ungewickell, Ernst J."],["dc.date.accessioned","2018-11-07T09:58:02Z"],["dc.date.available","2018-11-07T09:58:02Z"],["dc.date.issued","2015"],["dc.description.abstract","Clathrin-dependent transport processes require the polymerization of clathrin triskelia into polygonal scaffolds. Together with adapter proteins, clathrin collects cargo and induces membrane bud formation. It is not known to what extent clathrin light chains affect the structural and functional properties of clathrin lattices and the ability of clathrin to deform membranes. To address these issues, we have developed a novel procedure for analyzing clathrin lattice formation on rigid surfaces. We found that lattices can form on adaptor-coated convex-, planar- and even shallow concave surfaces, but the rate of formation and resistance to thermal dissociation of the lattice are greatly enhanced on convex surfaces. Atomic force microscopy on planar clathrin lattices demonstrates that the stiffness of the clathrin lattice is strictly dependent on light chains. The reduced stiffness of the lattice also compromised the ability of clathrin to generate coated buds on the surface of rigid liposomal membranes."],["dc.identifier.doi","10.1111/tra.12263"],["dc.identifier.isi","000353461400006"],["dc.identifier.pmid","25652138"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37289"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1600-0854"],["dc.relation.issn","1398-9219"],["dc.title","Effect of Clathrin Light Chains on the Stiffness of Clathrin Lattices and Membrane Budding"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","954"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Nature Nanotechnology"],["dc.bibliographiccitation.lastpage","U194"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Dannhauser, Philip N."],["dc.contributor.author","Platen, Mitja"],["dc.contributor.author","Boening, Heike"],["dc.contributor.author","Schaap, I. A. T."],["dc.date.accessioned","2018-11-07T09:49:35Z"],["dc.date.available","2018-11-07T09:49:35Z"],["dc.date.issued","2015"],["dc.description.abstract","Biological molecules that self-assemble and interact with other molecules are attractive building blocks for engineering biological devices. DNA has been widely used for the creation of nanomaterials(1), but the use of proteins remains largely unexplored. Here, we show that clathrin can form homogeneous and extended two-dimensional lattices on a variety of substrates, including glass, metal, carbon and plastic. Clathrin is a threelegged protein complex with unique self-assembling properties and is relevant in the formation of membrane transport vesicles in eukaryotic cells(2,3). We used a fragment of the adaptor protein epsin to immobilize clathrin lattices on the substrates. The lattices span multiple square millimetres with a regular periodicity of 30 nm and can be functionalized via modified subunits of clathrin with either inorganic nanoparticles or active enzymes. The lattices can be stored for months after crosslinking and stabilization with uranyl acetate. They could be dehydrated and rehydrated without loss of function, offering potential applications in sensing and as biosynthetic reactors."],["dc.identifier.doi","10.1038/NNANO.2015.206"],["dc.identifier.isi","000364528300012"],["dc.identifier.pmid","26367107"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35538"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1748-3395"],["dc.relation.issn","1748-3387"],["dc.title","Durable protein lattices of clathrin that can be functionalized with nanoparticles and active biomolecules"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]