Side-binding proteins modulate actin filament dynamics
- Ludwig Maximilian University of Munich, Germany
- Max Planck Institute of Biochemistry, Germany
- Technische Universität München, Germany
- University of Münster, Germany
Abstract
Actin filament dynamics govern many key physiological processes from cell motility to tissue morphogenesis. A central feature of actin dynamics is the capacity of filaments to polymerize and depolymerize at their ends in response to cellular conditions. It is currently thought that filament kinetics can be described by a single rate constant for each end. Here, using direct visualization of single actin filament elongation, we show that actin polymerization kinetics at both filament ends are strongly influenced by the binding of proteins to the lateral filament surface. We also show that the pointed-end has a non-elongating state that dominates the observed filament kinetic asymmetry. Estimates of flexibility as well as effects on fragmentation and growth suggest that the observed kinetic diversity arises from structural alteration. Tuning elongation kinetics by exploiting the malleability of the filament structure may be a ubiquitous mechanism to generate a rich variety of cellular actin dynamics.
Article and author information
Author details
Reviewing Editor
- Anthony A Hyman, Max Planck Institute of Molecular Cell Biology and Genetics, Germany
Version history
- Received: September 3, 2014
- Accepted: February 20, 2015
- Accepted Manuscript published: February 23, 2015 (version 1)
- Version of Record published: March 27, 2015 (version 2)
- Version of Record updated: May 11, 2017 (version 3)
Copyright
© 2015, Crevenna et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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Side-binding proteins modulate actin filament dynamics
eLife 4:e04599.
https://doi.org/10.7554/eLife.04599
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