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.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Adaptor Proteins, Vesicular Transport, Adenosine Triphosphatases, Animals, Genes, Tumor Suppressor, Humans, Kinetics, Mice, Microfilaments, Movement, Myosin Heavy Chains, Protein Structure, Tertiary, Proteins, Signal Transduction, Two-Hybrid System Techniques, Yeasts
Adaptor Proteins, Signal Transducing, Adaptor Proteins, Vesicular Transport, Adenosine Triphosphatases, Animals, Genes, Tumor Suppressor, Humans, Kinetics, Mice, Microfilaments, Movement, Myosin Heavy Chains, Protein Structure, Tertiary, Proteins, Signal Transduction, Two-Hybrid System Techniques, Yeasts
Biochem. Biophys. Res. Commun.
Date: Mar. 29, 2002
PubMed ID: 11906161
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