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Actomyosin II interaction modulates cell cortex stability.

Wolfgang H Goldmann1, Horacio F Cantiello, Bernard Chasan

  • 1Zentralinstitut für Biomedizinische Technik, Friedrich-Alexander-Universität, Erlangen-Nürnberg, D-91052 Erlangen, Germany. wgoldmann@biomed.uni-erlangen.de

Cell Biology International
|May 24, 2005
PubMed
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Myosin II significantly stiffens actin filaments by cross-linking them, rather than sliding. This change in viscoelastic behavior is energy-dependent, observed when adenosine triphosphate is replaced by adenosine diphosphate.

Area of Science:

  • Biophysics
  • Cell Biology
  • Biochemistry

Background:

  • Actin filaments form the cell's cytoskeleton, providing structure and enabling movement.
  • Myosin II is a motor protein that interacts with actin filaments.
  • The mechanical properties of actin-myosin networks are crucial for cellular functions.

Purpose of the Study:

  • To investigate the effect of Myosin II on the viscoelastic properties of actin filaments.
  • To understand the role of ATP hydrolysis in actomyosin interactions.
  • To characterize the transition from sliding to cross-linking in actin-myosin networks.

Main Methods:

  • Rheological measurements were performed on actin filaments.
  • Atomic force microscopy was used to visualize myosin head binding.

Related Experiment Videos

  • Adenosine triphosphate (ATP) was replaced with adenosine diphosphate (ADP) to alter myosin activity.

    • Main Results:

    • Myosin II increased the elastic modulus (G') of actin filaments by 3-4 fold at a molar ratio of 1:200.
    • Replacing ATP with ADP shifted the actomyosin interaction from sliding to cross-linking.
    • Atomic force microscopy confirmed the presence of inactive myosin heads bound to actin filaments.

    Conclusions:

    • Myosin II acts as a cross-linker for actin filaments in an ATP-independent manner.
    • The transition to cross-linking significantly enhances the elasticity of actin networks.
    • Understanding these mechanics is vital for comprehending cellular structural organization and force generation.