Assembly Kinetics of Vimentin Tetramers to Unit-Length Filaments: A Stopped-Flow Study

Biophysical Journal
Norbert MückeH Herrmann

Abstract

Intermediate filaments (IFs) are principal components of the cytoskeleton, a dynamic integrated system of structural proteins that provides the functional architecture of metazoan cells. They are major contributors to the elasticity of cells and tissues due to their high mechanical stability and intrinsic flexibility. The basic building block for the assembly of IFs is a rod-like, 60-nm-long tetrameric complex made from two antiparallel, half-staggered coiled coils. In low ionic strength, tetramers form stable complexes that rapidly assemble into filaments upon raising the ionic strength. The first assembly products, "frozen" by instantaneous chemical fixation and viewed by electron microscopy, are 60-nm-long "unit-length" filaments (ULFs) that apparently form by lateral in-register association of tetramers. ULFs are the active elements of IF growth, undergoing longitudinal end-to-end annealing with one another and with growing filaments. Originally, we have employed quantitative time-lapse atomic force and electron microscopy to analyze the kinetics of vimentin-filament assembly starting from a few seconds to several hours. To obtain detailed quantitative insight into the productive reactions that drive ULF formation, we now i...Continue Reading

Citations

Jul 10, 2020·Nanoscale·Anna V SchepersSarah Köster
Apr 15, 2020·International Journal of Molecular Sciences·Marcos GouveiaMirjana Liovic
Sep 30, 2020·Physical Biology·Alison E PattesonPaul A Janmey
Nov 16, 2020·Current Opinion in Cell Biology·Sherif A EldiranyChristopher G Bunick
May 26, 2021·Current Biology : CB·Gaëlle Dutour-Provenzano, Sandrine Etienne-Manneville
Jun 20, 2021·Nature Communications·Laura SchaedelSarah Köster

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