Regulation of dynamin-mediated membrane fission by the N-BAR protein endophilin
| Autor: | Hohendahl, Annika |
|---|---|
| Přispěvatelé: | Roux, Aurélien |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
Cell biology
BIN1 N-BAR Amphiphysin Genetic disease Transport Clathrine Fission membranaire Vps34 In vitro Dynamine AP180 CME Endophiline Endophilin Endocytose médiée par la clathrine Centronuclear myopathy Membrane Membrane fission MCN BAR Clathrin Clathrin-mediated endocytosis Dynamin ddc:540 Myopathie centronucléaire Amphiphysine CNM Mutations Nanotube pulling assay |
| DOI: | 10.13097/archive-ouverte/unige:91833 |
| Popis: | Eukaryotic cells are composed of different compartments with defined biological functions. Transport of molecules from one compartment to another, as well as from and to the plasma membrane, occurs via membrane vesicles. Clathrin-mediated endocytosis is the most studied pathway for the formation of such a vesicle. The GTPase dynamin mediates the final membrane fission step in this process. This thesis describes the experimental work to clarify how a specific class of crescent-shaped proteins called N-BAR proteins regulate dynamin-mediated membrane fission. Endophilin, one of the N-BAR proteins, was taken as an example. The major experimental technique is the nanotube pulling assay, an in-vitro essay using purified proteins. Other chapters of this thesis explore curvature-inducing properties of the clathrin adapter AP180 and the curvature-dependent activity of yeast Vps34 complex I. Additionally, this thesis analyses structural consequences of mutations in dynamin and another N-BAR protein, BIN1/amphiphysin 2, which cause the hereditary muscle disease CNM (centronuclear myopathy). |
| Databáze: | OpenAIRE |
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