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    In vivo movement of the type V myosin Myo52 requires dimerisation but is independent of the neck domain.

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    Authors
    Grallert, Agnes
    Martín-García, Rebeca
    Bagley, Steven
    Mulvihill, Daniel P
    Affiliation
    Cancer Research UK Cell Division Group, CR-UK Paterson Institute for Cancer Research, Manchester, M20 4BX, UK.
    Issue Date
    2007-12-01
    
    Metadata
    Show full item record
    Abstract
    Intracellular movement is a fundamental property of all cell types. Many organelles and molecules are actively transported throughout the cytoplasm by molecular motors, such as the dimeric type V myosins. These possess a long neck, which contains an IQ motif, that allow it to make 36-nm steps along the actin polymer. Live cell imaging of the fission yeast type V myosin Myo52 reveals that the protein moves rapidly throughout the cytoplasm. Here, we describe analysis of this movement and have established that Myo52 moves long distances on actin filaments in an ATP-dependent manner at approximately 0.5 mum/second. Myo51 and the microtubule cytoskeleton have no discernable role in modulating Myo52 movements, whereas rigour mutations in Myo52 abrogated its movement. We go on to show that, although dimerisation is required for Myo52 movement, deleting its neck has no discernable affect on Myo52 function or velocity in vivo.
    Citation
    In vivo movement of the type V myosin Myo52 requires dimerisation but is independent of the neck domain. 2007, 120 (Pt 23):4093-8 J. Cell. Sci.
    Journal
    Journal of Cell Science
    URI
    http://hdl.handle.net/10541/71364
    DOI
    10.1242/jcs.012468
    PubMed ID
    18003699
    Type
    Article
    Language
    en
    ISSN
    0021-9533
    ae974a485f413a2113503eed53cd6c53
    10.1242/jcs.012468
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

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