ArticleBiophysical journal2008
A quantitative analysis of contractility in active cytoskeletal protein networks.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 139 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
139 citing papers in PubMed, 314 citations in OpenAlex.
- Reconstitution of actomyosin networks in cell-sized liposomes dissects distinct mechanisms of membrane blebbing and symmetry breaking.Science advances · 2026Article
- State-dependent energy conversion produces degenerate dissipation in active actomyosin networks.bioRxiv : the preprint server for biology · 2026Article
- Investigating active dynamics of contractile actomyosin gels with micro particle image velocimetry (micro-PIV) analysis.Scientific reports · 2026Article
- Rethinking contractility in active cytoskeletal matter.Biophysical journal · 2026Article
- Crosslinked F-actin networks regulate load-dependent energy conversion.Communications biology · 2026Article
- Engineering filamentous myosins for optical control of contractility.bioRxiv : the preprint server for biology · 2025Article
- Article
- Kinesin-Driven De-Mixing of Cytoskeleton Composites Drives Emergent Mechanical Properties.Macromolecular rapid communications · 2025Article
- Reconstituted systems for studying the architecture and dynamics of actin networks.The Biochemical journal · 2025Review
- Reconstitution of actomyosin networks in cell-sized liposomes reveals distinct mechanical roles of cytoskeletal organization in membrane shape remodeling.bioRxiv : the preprint server for biology · 2025Article
- Filament transport supports contractile steady states of actin networks.bioRxiv : the preprint server for biology · 2025Article
- Article
- Mechanical power is maximized during contractile ring-like formation in a biomimetic dividing cell model.Nature communications · 2024Article
- Myosin-induced F-actin fragmentation facilitates contraction of actin networks.Cytoskeleton (Hoboken, N.J.) · 2024Article
- How cytoskeletal crosstalk makes cells move: Bridging cell-free and cell studies.Biophysics reviews · 2024Review
- F-actin architecture determines the conversion of chemical energy into mechanical work.Nature communications · 2024Article
- Catch bond kinetics are instrumental to cohesion of fire ant rafts under load.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Cofilin-mediated actin filament network flexibility facilitates 2D to 3D actomyosin shape change.European journal of cell biology · 2024Article
- Microscopic interactions control a structural transition in active mixtures of microtubules and molecular motors.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Evidence that tissue recoil in the earlyMolecular biology of the cell · 2023Article
79 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
Abstract
Cells actively produce contractile forces for a variety of processes including cytokinesis and motility. Contractility is known to rely on myosin II motors which convert chemical energy from ATP hydrolysis into forces on actin filaments. However, the basic physical principles of cell contractility remain poorly understood. We reconstitute contractility in a simplified model system of purified F-actin, muscle myosin II motors, and alpha-actinin cross-linkers. We show that contractility occurs above a threshold motor concentration and within a window of cross-linker concentrations. We also quantify the pore size of the bundled networks and find contractility to occur at a critical distance between the bundles. We propose a simple mechanism of contraction based on myosin filaments pulling neighboring bundles together into an aggregated structure. Observations of this reconstituted system in both bulk and low-dimensional geometries show that the contracting gels pull on and deform their surface with a contractile force of approximately 1 microN, or approximately 100 pN per F-actin bundle. Cytoplasmic extracts contracting in identical environments show a similar behavior and dependence on myosin as the reconstituted system. Our results suggest that cellular contractility can be sensitively regulated by tuning the (local) activity of molecular motors and the cross-linker density and binding affinity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.