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    Lemur tyrosine kinase-2 signalling regulates kinesin-1 light chain-2 phosphorylation and binding of Smad2 cargo.

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    Authors
    Manser, C
    Guillot, F
    Vagnoni, A
    Davies, J
    Lau, K-F
    McLoughlin, D M
    De Vos, K J
    Miller, C C J
    Affiliation
    Department of Neuroscience P037, MRC Centre for Neurodegeneration Research, Institute of Psychiatry, King's College London, London, UK.
    Issue Date
    2012-05-31
    MeSH
    Blotting, Western
    Cell Nucleus
    Cell Proliferation
    Fluorescent Antibody Technique
    Glycogen Synthase Kinase 3
    HeLa Cells
    Humans
    Immunoenzyme Techniques
    Immunoprecipitation
    Membrane Proteins
    Microtubule-Associated Proteins
    Phosphorylation
    Protein Phosphatase 1
    Protein-Serine-Threonine Kinases
    RNA, Messenger
    RNA, Small Interfering
    Real-Time Polymerase Chain Reaction
    Receptors, Transforming Growth Factor beta
    Signal Transduction
    Smad2 Protein
    Transforming Growth Factor beta
    Two-Hybrid System Techniques
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    Citation
    Lemur tyrosine kinase-2 signalling regulates kinesin-1 light chain-2 phosphorylation and binding of Smad2 cargo. 2012, 31 (22):2773-82 Oncogene
    Journal
    Oncogene
    URI
    http://hdl.handle.net/10147/244217
    DOI
    10.1038/onc.2011.437
    PubMed ID
    21996745
    Abstract
    A recent genome-wide association study identified the gene encoding lemur tyrosine kinase-2 (LMTK2) as a susceptibility gene for prostate cancer. The identified genetic alteration is within intron 9, but the mechanisms by which LMTK2 may impact upon prostate cancer are not clear because the functions of LMTK2 are poorly understood. Here, we show that LMTK2 regulates a known pathway that controls phosphorylation of kinesin-1 light chain-2 (KLC2) by glycogen synthase kinase-3β (GSK3β). KLC2 phosphorylation by GSK3β induces the release of cargo from KLC2. LMTK2 signals via protein phosphatase-1C (PP1C) to increase inhibitory phosphorylation of GSK3β on serine-9 that reduces KLC2 phosphorylation and promotes binding of the known KLC2 cargo Smad2. Smad2 signals to the nucleus in response to transforming growth factor-β (TGFβ) receptor stimulation and transport of Smad2 by kinesin-1 is required for this signalling. We show that small interfering RNA loss of LMTK2 not only reduces binding of Smad2 to KLC2, but also inhibits TGFβ-induced Smad2 signalling. Thus, LMTK2 may regulate the activity of kinesin-1 motor function and Smad2 signalling.
    Item Type
    Article
    Language
    en
    ISSN
    1476-5594
    ae974a485f413a2113503eed53cd6c53
    10.1038/onc.2011.437
    Scopus Count
    Collections
    St. Patrick's University Hospital

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