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BP: Fachverband Biologische Physik
BP 36: Cytoskeletal Filaments I
BP 36.6: Vortrag
Donnerstag, 19. März 2020, 16:45–17:00, SCH A251
Influence of Phosphorylation on Vimentin Mechanics — •Julia Kraxner1, Julia Menzel2, Henning Urlaub3, Blanche Schwappach2, and Sarah Köster1 — 1Institute for X-Ray Physics, University of Göttingen — 2Department of Molecular Biology, University Medical Center Göttingen — 3Bioanalytical Mass Spectrometry, Max Planck Institute for Biophysical Chemistry, Göttingen
The mechanical properties of biological cells are determined by the cytoskeleton. This composite biopolymer network consists of microtubules and microfilaments, which are conserved throughout all cell types, and different types of intermediate filaments (IFs), which are expressed in a cell-type specific manner. The adaption to specific mechanical requirements may be further achieved by post-translational modifications of the proteins. In this context, phosphorylation which adds negative charges to the modified site, plays an important role. Regarding IFs, phosphorylation heavily affects disassembly of the filaments and provides binding sites for proteins like 14-3-3 which is a regulator for signaling proteins. Here, we study partially phosphorylated single vimentin IFs by analyzing stress-strain curves recorded with an optical tweezer setup which combines microfluidics and fluorescence microscopy. Furthermore, we investigate the influence of bound 14-3-3 on the mechanics and the contribution of single phosphorylation sites by phosphomimetics. Our results show that additional charges within the filament soften the vimentin filaments and the binding of 14-3-3 weakens the filaments even more.