DOC-2/DAB2 is the binding partner of myosin VI

Akira Inoue, Osamu Sato, Kazuaki Homma, Mitsuo Ikebe*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

57 Scopus citations

Abstract

Myosin VI is a molecular motor that moves processively along actin filaments and is believed to play a role in cargo movement in cells. Here we found that DOC-2/DAB2, a signaling molecule inhibiting the Ras cascade, binds to myosin VI at the globular tail domain. DOC-2/DAB2 binds stoichiometrically to myosin VI with one molecule per one myosin VI heavy chain. The C-terminal 122 amino acid residues of DOC-2/DAB2, containing the Grb2 binding site, is identified to be critical for the binding to myosin VI. Actin gliding assay revealed that the binding of DOC-2/DAB2 to myosin VI can support the actin filament gliding by myosin VI, suggesting that it can function as a myosin VI anchoring molecule. The C-terminal domain but not the N-terminal domain of DOC-2/DAB2 functions as a myosin VI anchoring site. The present findings suggest that myosin VI plays a role in transporting DOC-2/DAB2, a Ras cascade signaling molecule, thus involved in Ras signaling pathways.

Original languageEnglish (US)
Pages (from-to)300-307
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume292
Issue number2
DOIs
StatePublished - Jan 1 2002

Keywords

  • ATPase
  • Actin
  • DOC-2/DAB2
  • Molecular motor
  • Myosin VI
  • Rab2
  • Ras
  • Trafficking
  • Vesicle transport

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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