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    hShroom1 links a membrane bound protein to the actin cytoskeleton

    Access Status
    Fulltext not available
    Authors
    Dye, Danielle
    Karlen, S.
    Rohrbach, B.
    Staub, O.
    Braathen, L.
    Eidne, K.
    Coombe, Deirdre
    Date
    2009
    Type
    Journal Article
    
    Metadata
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    Citation
    Dye, D. and Karlen, S. and Rohrbach, B. and Staub, O. and Braathen, L. and Eidne, K. and Coombe, D. 2009. hShroom1 links a membrane bound protein to the actin cytoskeleton. Cellular and Molecular Life Sciences. 66 (4): pp. 681-696.
    Source Title
    Cellular and Molecular Life Sciences
    DOI
    10.1007/s00018-009-8645-1
    ISSN
    1420-682X
    Faculty
    Faculty of Health Sciences
    School of Biomedical Sciences
    School
    Molecular Immunology / Bio Sciences
    URI
    http://hdl.handle.net/20.500.11937/15471
    Collection
    • Curtin Research Publications
    Abstract

    hShroom1 (hShrm1) is a member of the Apx/Shroom (Shrm) protein family and was identified from a yeast two-hybrid screen as a protein that interacts with the cytoplasmic domain of melanoma cell adhesion molecule (MCAM). The characteristic signature of the Shrm family is the presence of a unique domain, ASD2 (Apx/Shroom domain 2). mRNA analysis suggests that hShrm1 is expressed in brain, heart, skeletal muscle, colon, small intestine, kidney, placenta and lung tissue, as well a variety of melanoma and other cell lines. Co-immunoprecipitation and bioluminescence resonance energy transfer (BRET) experiments indicate that hShrm1 and MCAM interact in vivo and by immunofluorescence microscopy some co-localization of these proteins is observed. hShrm1 partly co-localises with β-actin and is found in the Triton X-100 insoluble fraction of melanoma cell extracts. We propose that hShrm1 is involved in linking MCAM to the cytoskeleton.

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