Molecular to organismal chirality is induced by the conserved myosin 1D

Science. 2018 Nov 23;362(6417):949-952. doi: 10.1126/science.aat8642.


The emergence of asymmetry from an initially symmetrical state is a universal transition in nature. Living organisms show asymmetries at the molecular, cellular, tissular, and organismal level. However, whether and how multilevel asymmetries are related remains unclear. In this study, we show that Drosophila myosin 1D (Myo1D) and myosin 1C (Myo1C) are sufficient to generate de novo directional twisting of cells, single organs, or the whole body in opposite directions. Directionality lies in the myosins' motor domain and is swappable between Myo1D and Myo1C. In addition, Myo1D drives gliding of actin filaments in circular, counterclockwise paths in vitro. Altogether, our results reveal the molecular motor Myo1D as a chiral determinant that is sufficient to break symmetry at all biological scales through chiral interaction with the actin cytoskeleton.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actin Cytoskeleton / chemistry*
  • Animals
  • Drosophila Proteins / antagonists & inhibitors
  • Drosophila Proteins / chemistry*
  • Drosophila melanogaster / growth & development
  • Isomerism
  • Larva
  • Models, Molecular*
  • Myosin Type I / antagonists & inhibitors
  • Myosin Type I / chemistry*
  • Myosin Type V / chemistry
  • Protein Domains


  • Drosophila Proteins
  • Myo31DF protein, Drosophila
  • didum protein, Drosophila
  • Myosin Type I
  • Myosin Type V