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

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    Authors
    Inoue, Akira
    Sato, Osamu
    Homma, Kazuaki
    Ikebe, Mitsuo
    UMass Chan Affiliations
    Department of Physiology
    Graduate School of Biomedical Sciences
    Document Type
    Journal Article
    Publication Date
    2002-03-22
    Keywords
    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
    Life Sciences
    Medicine and Health Sciences
    
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    Link to Full Text
    http://dx.doi.org/10.1006/bbrc.2002.6636
    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.
    Source
    Biochem Biophys Res Commun. 2002 Mar 29;292(2):300-7. Link to article on publisher's site
    DOI
    10.1006/bbrc.2002.6636
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/33905
    PubMed ID
    11906161
    Related Resources
    Link to article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1006/bbrc.2002.6636
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    Morningside GSBS Scholarly Publications

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