title: Fragmentation is crucial for the steady-state dynamics of actin filaments.
abstract: Despite the recognition that actin filaments are important for numerous cellular processes, and decades of investigation, the dynamics of in vitro actin filaments are still not completely understood. Here, we follow the time evolution of the length distribution of labeled actin reporter filaments in an unlabeled F-actin solution via fluorescence microscopy. Whereas treadmilling and diffusive length fluctuations cannot account for the observed dynamics, our results suggest that at low salt conditions, spontaneous fragmentation is crucial.
authors.affiliation: Lehrstuhl für Biophysik E27, Technische Universität München, Garching, Germany.
authors.forename: Kurt M
authors.initials: KM
authors.lastname: Schmoller
authors.forename: Thomas
authors.initials: T
authors.lastname: Niedermayer
authors.forename: Carla
authors.initials: C
authors.lastname: Zensen
authors.forename: Christine
authors.initials: C
authors.lastname: Wurm
authors.forename: Andreas R
authors.initials: AR
authors.lastname: Bausch
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism*; D000199:Actins / Q000378:metabolism; D000818:Animals; D007700:Kinetics; D008856:Microscopy, Fluorescence; D010710:Phosphates / Q000378:metabolism; D058105:Polymerization; D011817:Rabbits; D013997:Time Factors
chemical_list: D000199:Actins; D010710:Phosphates