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• W61355124 endingPage "81" @default.
• W61355124 startingPage "71" @default.
• W61355124 abstract "Actin filaments are major dynamic components of the cytoskeleton of eukaryotic cells. Assembly of filaments from monomelic actin occurs with expenditure of energy, the tightly bound ATP being irreversibly hydrolyzed during polymerization. This dissipation of energy perturbs the laws of reversible helical polymerization defined by Oosawa and Asakura (1975), and affects the dynamics of actin filaments. We have shown that ATP hydrolysis destabilizes actin-actin interactions in the filament. The destabilization is linked to the liberation of Pi that follows cleavage of the γ-phosphate. Pi release therefore plays the role of a conformational switch. Because ATP hydrolysis is uncoupled from polymerization, the nucleotide content of the filaments changes during the polymerization process, and filaments grow with a stabilizing “cap” of terminal ADP-Pi subunits. The fact that the dynamic properties of F-actin are affected by ATP hydrolysis results in a non-linear dependence of the rate of filament elongation on monomer concentration." @default.
• W61355124 created "2016-06-24" @default.
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• W61355124 date "1994-01-01" @default.
• W61355124 modified "2023-10-02" @default.
• W61355124 title "Actin Polymerization: Regulation by Divalent Metal Ion and Nucleotide Binding, ATP Hydrolysis and Binding of Myosin" @default.
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• W61355124 doi "https://doi.org/10.1007/978-1-4615-2578-3_7" @default.
• W61355124 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7801813" @default.
• W61355124 hasPublicationYear "1994" @default.
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