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Endocytic myosin-1 is a force-insensitive, power-generating motor.

Ross T A Pedersen1, Aaron Snoberger2, Serapion Pyrpassopoulos2

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Myosin type I (Myo5) in yeast endocytosis is activated by phosphorylation. Its force-insensitive kinetics suggest it augments actin forces during cell entry.

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Area of Science:

  • Cell biology
  • Biophysics
  • Molecular motor function

Background:

  • Myosins are crucial for clathrin-mediated endocytosis, but their specific roles remain unclear due to limited biophysical data.
  • Myosins exhibit varied mechanochemical properties, influencing their function in cellular processes.

Purpose of the Study:

  • To investigate the in vitro force-dependent kinetics of Saccharomyces cerevisiae endocytic type I myosin (Myo5).
  • To elucidate the molecular contribution of Myo5 to clathrin-mediated endocytosis.

Main Methods:

  • In vitro analysis of Myo5's force-dependent kinetics.
  • Characterization of Myo5's mechanochemical activity and response to phosphorylation.

Main Results:

  • Myo5 functions as a low-duty-ratio motor, with its activity increasing approximately 10-fold upon phosphorylation.
  • The motor's working stroke and actin-detachment kinetics are largely insensitive to force.
  • Myo5's in vitro mechanochemistry resembles cardiac myosin more than slow anchoring myosins.

Conclusions:

  • Myo5's properties suggest it generates power to enhance actin assembly-based forces during endocytosis.
  • Phosphorylation significantly modulates Myo5's motor activity, highlighting its regulatory mechanism.