ArticleJournal of molecular biology2008
Effects of solution crowding on actin polymerization reveal the energetic basis for nucleotide-dependent filament stability.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 35 citations in OpenAlex.
- Using Cryogenic Electron Tomography (cryoET) to Determine Rubisco Polymerization Constants in α-Carboxysomes.bioRxiv : the preprint server for biology · 2026Article
- Cooperative and divergent properties of bacterial actin isoforms inBiophysics and physicobiology · 2026Article
- Article
- Molecular Basis for Actin Polymerization Kinetics Modulated by Solution Crowding.Biomolecules · 2023Article
- Graphene Enhances Actin Filament Assembly Kinetics and Modulates NIH-3T3 Fibroblast Cell Spreading.International journal of molecular sciences · 2022Article
- Regulation of Actin Bundle Mechanics and Structure by Intracellular Environmental Factors.Frontiers in physics · 2021Article
- Crowding tunes the organization and mechanics of actin bundles formed by crosslinking proteins.FEBS letters · 2021Article
- Partitioning and Enhanced Self-Assembly of Actin in Polypeptide Coacervates.Biophysical journal · 2018Article
- Charged Molecules Modulate the Volume Exclusion Effects Exerted by Crowders on FtsZ Polymerization.PloS one · 2016Article
- Heterogeneous preferential solvation of water and trifluoroethanol in homologous lysozymes.The journal of physical chemistry. B · 2014Article
- Sucrose increases the activation energy barrier for actin-myosin strong binding.Archives of biochemistry and biophysics · 2014Article
- Biophysics of actin filament severing by cofilin.FEBS letters · 2013Review
- ATP and ADP actin states.Biopolymers · 2013Article
- Emergent complexity of the cytoskeleton: from single filaments to tissue.Advances in physics · 2013Review
- Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Endocytic response of type I alveolar epithelial cells to hypertonic stress.American journal of physiology. Lung cellular and molecular physiology · 2011Article
- Kinetic analysis of the guanine nucleotide exchange activity of TRAPP, a multimeric Ypt1p exchange factor.Journal of molecular biology · 2009Article
- How cofilin severs an actin filament.Biophysical reviews · 2009Article
- Cofilin increases the bending flexibility of actin filaments: implications for severing and cell mechanics.Journal of molecular biology · 2008Article
- A regulatable switch mediates self-association in an immunoglobulin fold.Nature structural & molecular biology · 2008Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Actin polymerization is a fundamental cellular process involved in cell structure maintenance, force generation, and motility. Phosphate release from filament subunits following ATP hydrolysis destabilizes the filament lattice and increases the critical concentration (C(c)) for assembly. The structural differences between ATP- and ADP-actin are still debated, as well as the energetic factors that underlie nucleotide-dependent filament stability, particularly under crowded intracellular conditions. Here, we investigate the effect of crowding agents on ATP- and ADP-actin polymerization and find that ATP-actin polymerization is largely unaffected by solution crowding, while crowding agents lower the C(c) of ADP-actin in a concentration-dependent manner. The stabilities of ATP- and ADP-actin filaments are comparable in the presence of physiological amounts (approximately 30% w/v) and types (sorbitol) of low molecular weight crowding agents. Crowding agents act to stabilize ADP-F-actin by slowing subunit dissociation. These observations suggest that nucleotide hydrolysis and phosphate release per se do not introduce intrinsic differences in the in vivo filament stability. Rather, the preferential disassembly of ADP-actin filaments in cells is driven through interactions with regulatory proteins. Interpretation of the experimental data according to osmotic stress theory implicates water as an allosteric regulator of actin activity and hydration as the molecular basis for nucleotide-dependent filament stability.
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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.