Long-range and directional allostery of actin filaments plays important roles in various cellular activities

Kiyotaka Tokuraku*, Masahiro Kuragano, Taro Q.P. Uyeda

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

11 Citations (Scopus)


A wide variety of uniquely localized actin-binding proteins (ABPs) are involved in various cellular activities, such as cytokinesis, migration, adhesion, morphogenesis, and intracellular transport. In a micrometer-scale space such as the inside of cells, protein molecules diffuse throughout the cell interior within seconds. In this condition, how can ABPs selectively bind to particular actin filaments when there is an abundance of actin filaments in the cytoplasm? In recent years, several ABPs have been reported to induce cooperative conformational changes to actin filaments allowing structural changes to propagate along the filament cables uni-or bidirectionally, thereby regulating the subsequent binding of ABPs. Such propagation of ABP-induced cooperative conformational changes in actin filaments may be advantageous for the elaborate regulation of cellular activities driven by actin-based machineries in the intracellular space, which is dominated by diffusion. In this review, we focus on long-range allosteric regulation driven by cooperative conformational changes of actin filaments that are evoked by binding of ABPs, and discuss roles of allostery of actin filaments in narrow intracellular spaces.

Original languageEnglish
Article number3209
JournalInternational journal of molecular sciences
Issue number9
Publication statusPublished - 2020 May 2


  • Actin
  • Actin-binding protein
  • Cofilin
  • Cooperativity
  • Drebrin
  • Filamin
  • Fimbrin
  • Gelsolin
  • Long-range allostery
  • Myosin
  • Tropomyosin

ASJC Scopus subject areas

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry


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