ArticleBiophysical journal2006
ATP hydrolysis stimulates large length fluctuations in single actin filaments.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 76 citations in OpenAlex.
- ATP-dependent actin barbed-end fluctuations at steady state.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Hydrolysis-dependent severing tunes internal monomeric heterogeneity to shape actin length distributions.bioRxiv : the preprint server for biology · 2025Article
- Effects of random hydrolysis on biofilament length distributions in a shared subunit pool.Biophysical journal · 2022Article
- Atomistic molecular dynamics simulations of tubulin heterodimers explain the motion of a microtubule.European biophysics journal : EBJ · 2021Article
- Insights into Actin Polymerization and Nucleation Using a Coarse-Grained Model.Biophysical journal · 2020Article
- A stochastic model for dynamics of FtsZ filaments and the formation of Z -ring.The European physical journal. E, Soft matter · 2020Article
- Triggered disassembly and reassembly of actin networks induces rigidity phase transitions.Soft matter · 2019Article
- Multiscale simulation of actin filaments and actin-associated proteins.Biophysical reviews · 2018Review
- Insights into the Cooperative Nature of ATP Hydrolysis in Actin Filaments.Biophysical journal · 2018Article
- Signatures of a macroscopic switching transition for a dynamic microtubule.Scientific reports · 2017Article
- MEDYAN: Mechanochemical Simulations of Contraction and Polarity Alignment in Actomyosin Networks.PLoS computational biology · 2016Article
- Profilin Interaction with Actin Filament Barbed End Controls Dynamic Instability, Capping, Branching, and Motility.Developmental cell · 2016Article
- Regulation of Microtubule Growth and Catastrophe: Unifying Theory and Experiment.Trends in cell biology · 2015Review
- Force-induced dynamical properties of multiple cytoskeletal filaments are distinct from that of single filaments.PloS one · 2014Article
- Microtubule dynamic instability: a new model with coupled GTP hydrolysis and multistep catastrophe.BioEssays : news and reviews in molecular, cellular and developmental biology · 2013Article
- Quantitative analysis of approaches to measure cooperative phosphate release in polymerized actin.Biophysical journal · 2012Article
- Random hydrolysis controls the dynamic instability of microtubules.Biophysical journal · 2012Article
- A theoretical analysis of filament length fluctuations in actin and other polymers.Journal of mathematical biology · 2011Article
- Individual actin filaments in a microfluidic flow reveal the mechanism of ATP hydrolysis and give insight into the properties of profilin.PLoS biology · 2011Article
- Role of ATP-hydrolysis in the dynamics of a single actin filament.Biophysical journal · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Polymerization dynamics of single actin filaments is investigated theoretically using a stochastic model that takes into account the hydrolysis of ATP-actin subunits, the geometry of actin filament tips, and the lateral interactions between the monomers as well as the processes at both ends of the polymer. Exact analytical expressions are obtained for the mean growth velocity, for the dispersion in the length fluctuations, and the nucleotide composition of the actin filaments. It is found that the ATP hydrolysis has a strong effect on dynamic properties of single actin filaments. At high concentrations of free actin monomers, the mean size of the unhydrolyzed ATP-cap is very large, and the dynamics is governed by association/dissociation of ATP-actin subunits. However, at low concentrations the size of the cap becomes finite, and the dissociation of ADP-actin subunits makes a significant contribution to overall dynamics. Actin filament length fluctuations reach a sharp maximum at the boundary between two dynamic regimes, and this boundary is always larger than the critical concentration for the actin filament's growth at the barbed end, assuming the sequential release of phosphate. Random and sequential mechanisms of hydrolysis are compared, and it is found that they predict qualitatively similar dynamic properties at low and high concentrations of free actin monomers with some deviations near the critical concentration. The possibility of attachment and detachment of oligomers in actin filament's growth is also discussed. Our theoretical approach is successfully applied to analyze the latest experiments on the growth and length fluctuations of individual actin filaments.
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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.