Entropic forces drive contraction of cytoskeletal networks
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
Grant support
242933
European Research Council - International
- Keywords
- cytoskeleton, depletion forces, entropic forces, entropy, filament crosslinkers, force generation, molecular motors,
- MeSH
- Biomechanical Phenomena MeSH
- Cell Division MeSH
- Cytoskeleton metabolism ultrastructure MeSH
- Entropy MeSH
- Eukaryotic Cells metabolism ultrastructure MeSH
- Humans MeSH
- Microtubules metabolism ultrastructure MeSH
- Molecular Motor Proteins metabolism MeSH
- Cell Movement MeSH
- Microtubule-Associated Proteins metabolism MeSH
- Saccharomyces cerevisiae Proteins metabolism MeSH
- Saccharomyces cerevisiae metabolism ultrastructure MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Ase1 protein, S cerevisiae MeSH Browser
- Molecular Motor Proteins MeSH
- Microtubule-Associated Proteins MeSH
- Saccharomyces cerevisiae Proteins MeSH
The cytoskeleton is a network of interconnected protein filaments, which provide a three-dimensional scaffold for cells. Remodeling of the cytoskeleton is important for key cellular processes, such as cell motility, division, or morphogenesis. This remodeling is traditionally considered to be driven exclusively by processes consuming chemical energy, such as the dynamics of the filaments or the action of molecular motors. Here, we review two mechanisms of cytoskeletal network remodeling that are independent of the consumption of chemical energy. In both cases directed motion of overlapping filaments is driven by entropic forces, which arise from harnessing thermal energy present in solution. Entropic forces are induced either by macromolecular crowding agents or by diffusible crosslinkers confined to the regions where filaments overlap. Both mechanisms increase filament overlap length and lead to the contraction of filament networks. These force-generating mechanisms, together with the chemical energy-dependent mechanisms, need to be considered for the comprehensive quantitative picture of the remodeling of cytoskeletal networks in cells.
B CUBE Center for Molecular Bioengineering Technische Universität Dresden Dresden Germany
Institute of Biotechnology CAS BIOCEV Center Vestec Czech Republic
Martin Fisher School of Physics Brandeis University Waltham MA USA
Max Planck Institute of Molecular Cell Biology and Genetics Dresden Germany
References provided by Crossref.org
Anillin propels myosin-independent constriction of actin rings