Side-binding proteins modulate actin filament dynamics

Abstract
Article and author information
Metrics

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

Alvaro H Crevenna

Physical Chemistry, Department of Chemistry and Center for Nanoscience, Ludwig Maximilian University of Munich, Munich, Germany

For correspondence
alvaro.crevenna@cup.uni-muenchen.de

Competing interests
The authors declare that no competing interests exist.
Marcelino Arciniega

Max Planck Institute of Biochemistry, Martinsried, Germany

Competing interests
The authors declare that no competing interests exist.
Aurélie Dupont

Physical Chemistry, Department of Chemistry and Center for Nanoscience, Ludwig Maximilian University of Munich, Munich, Germany

Competing interests
The authors declare that no competing interests exist.
Naoko Mizuno

Cellular and Membrane Trafficking, Max Planck Institute of Biochemistry, Martinsried, Germany

Competing interests
The authors declare that no competing interests exist.
Kaja Kowalska

Cellular Dynamics and Cell Patterning, Max Planck Institute of Biochemistry, Martinsried, Germany

Competing interests
The authors declare that no competing interests exist.
Oliver F Lange

Department of Chemistry, Technische Universität München, Garching, Germany

Competing interests
The authors declare that no competing interests exist.
Roland Wedlich-Söldner

Institute of Cell Dynamics and Imaging, University of Münster, Münster, Germany

Competing interests
The authors declare that no competing interests exist.
Don C Lamb

Physical Chemistry, Department for Chemistry and Center for Nanoscience, Ludwig Maximilian University of Munich, Munich, Germany

Competing interests
The authors declare that no competing interests exist.

Copyright

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.