Class VI myosin moves processively along actin filaments backward with large steps

So Nishikawa, Kazuaki Homma, Yasunori Komori, Mitsuhiro Iwaki, Tetsuichi Wazawa, Atsuko Hikikoshi Iwone, Junya Saito, Reiko Ikebe, Eisaku Katayama, Toshio Yanagida, Mitsuo Ikebe*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

153 Scopus citations


Among a superfamily of myosin, class VI myosin moves actin filaments backwards. Here we show that myosin VI moves processively on actin filaments backwards with large (∼36 nm) steps, nevertheless it has an extremely short neck domain. Myosin V also moves processively with large (∼36 nm) steps and it is believed that myosin V strides along the actin helical repeat with its elongated neck domain that is critical for its processive movement with large steps. Myosin VI having a short neck cannot take this scenario. We found by electron microscopy that myosin VI cooperatively binds to an actin filament at ∼36 nm intervals in the presence of ATP, raising a hypothesis that the binding of myosin VI evokes "hot spots" on actin filaments that attract myosin heads. Myosin VI may step on these "hot spots" on actin filaments in every helical pitch, thus producing processive movement with 36 nm steps.

Original languageEnglish (US)
Pages (from-to)311-317
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - 2002


  • Actin
  • Brownian motion
  • GFP
  • Molecular motor
  • Myosin VI
  • Nanotechnology
  • Optical trap
  • Single molecule imaging
  • Vesicle transport

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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