Actin pp 71-81 | Cite as

Actin Polymerization: Regulation by Divalent Metal Ion and Nucleotide Binding, ATP Hydrolysis and Binding of Myosin

  • Marie-France Carlier
  • Catherine Valentin-Ranc
  • Cecile Combeau
  • Stephane Fievez
  • Dominique Pantoloni
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 358)


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.


Actin Filament Monomer Concentration Actin Polymerization Myosin Head Nucleotide Hydrolysis 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer Science+Business Media New York 1994

Authors and Affiliations

  • Marie-France Carlier
    • 1
  • Catherine Valentin-Ranc
    • 1
  • Cecile Combeau
    • 1
  • Stephane Fievez
    • 1
  • Dominique Pantoloni
    • 1
  1. 1.Laboratoire d’Enzymologoie C.N.R.S.Gif-sur-Yvette CedexFrance

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