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    Translocation of telokin by cGMP signaling in smooth muscle cells

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    Authors
    Komatsu, Satoshi
    Miyazaki, Koji
    Tuft, Richard A.
    Ikebe, Mitsuo
    UMass Chan Affiliations
    Department of Physiology
    Document Type
    Journal Article
    Publication Date
    2002-08-15
    Keywords
    Animals
    Binding Sites
    COS Cells
    Cell Membrane
    Cells, Cultured
    Cyclic GMP
    Cyclic GMP-Dependent Protein Kinases
    Enzyme Inhibitors
    Green Fluorescent Proteins
    Luminescent Proteins
    Muscle Proteins
    Muscle, Smooth
    Mutagenesis, Site-Directed
    Myosin-Light-Chain Kinase
    Myosins
    Nitric Oxide Donors
    Peptides
    Phosphorylation
    Protein Binding
    Protein Transport
    Recombinant Fusion Proteins
    Signal Transduction
    Swine
    Trachea
    Transfection
    Life Sciences
    Medicine and Health Sciences
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    Link to Full Text
    http://dx.doi.org/10.1152/ajpcell.00501.2001
    Abstract
    Telokin is an acidic protein with a sequence identical to the COOH-terminal domain of myosin light chain kinase (MLCK) produced by an alternate promoter of the MLCK gene. Although it is abundantly expressed in smooth muscle, its physiological function is not understood. In the present study, we attempted to clarify the function of telokin by analyzing its spatial and temporal localization in living single smooth muscle cells. Primary cultured smooth muscle cells were transfected with green fluorescent protein (GFP)-tagged telokin. The telokin-GFP localized mostly diffusely in cytosol. Stimulation with both sodium nitroprusside (SNP) and 8-bromo-cyclic GMP induced translocation of GFP-tagged telokin to near plasma membrane in living single smooth muscle cells. The translocation was slow, and it took more than 10 min at room temperature. Mutation of the phosphorylation sites of telokin (S13A, S19A, and S13A/S19A) significantly attenuated SNP-induced translocation. Both KT-5823 (cGMP-dependent protein kinase inhibitor) and PD-98059 (mitogen-activated protein kinase inhibitor) diminished the telokin-GFP translocation. These results suggest that telokin changes its intracellular localization because of phosphorylation at Ser13 and/or Ser19 via the cGMP-signaling pathway.
    Source
    Am J Physiol Cell Physiol. 2002 Sep;283(3):C752-61. Link to article on publisher's site
    DOI
    10.1152/ajpcell.00501.2001
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/38277
    PubMed ID
    12176732
    Related Resources
    Link to article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1152/ajpcell.00501.2001
    Scopus Count
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