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

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.

Pubmed ID: 11906161


  • Inoue A
  • Sato O
  • Homma K
  • Ikebe M


Biochemical and biophysical research communications

Publication Data

March 29, 2002

Associated Grants

  • Agency: NIAMS NIH HHS, Id: AR 41653
  • Agency: NIGMS NIH HHS, Id: GM 55834

Mesh Terms

  • Actin Cytoskeleton
  • Adaptor Proteins, Signal Transducing
  • Adaptor Proteins, Vesicular Transport
  • Adenosine Triphosphatases
  • Animals
  • Genes, Tumor Suppressor
  • Humans
  • Kinetics
  • Mice
  • Movement
  • Myosin Heavy Chains
  • Protein Structure, Tertiary
  • Proteins
  • Signal Transduction
  • Tumor Suppressor Proteins
  • Two-Hybrid System Techniques
  • Yeasts