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    Protein kinase A regulates Rac and is required for the growth factor-stimulated migration of carcinoma cells

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    Authors
    O'Connor, Kathleen L.
    Mercurio, Arthur M.
    UMass Chan Affiliations
    Department of Cancer Biology
    Document Type
    Journal Article
    Publication Date
    2001-10-19
    Keywords
    Antigens, CD29
    Breast Neoplasms
    Chemotaxis
    Cyclic AMP-Dependent Protein Kinases
    Epidermal Growth Factor
    Humans
    Lysophospholipids
    Signal Transduction
    Tumor Cells, Cultured
    rac GTP-Binding Proteins
    rhoA GTP-Binding Protein
    Cancer Biology
    Neoplasms
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    Link to Full Text
    http://dx.doi.org/10.1074/jbc.M107235200
    Abstract
    Members of the Rho family of small GTPases, such as Rho and Rac, are required for actin cytoskeletal reorganization during the migration of carcinoma cells. Phosphodiesterases are necessary for this migration because they alleviate cAMP-dependent protein kinase (PKA)-mediated inhibition of RhoA (O'Connor, K. L., Shaw, L. M., and Mercurio, A. M. (1998) J. Cell Biol. 143, 1749-1760; O'Connor K. L., Nguyen, B.-K., and Mercurio, A. M. (2000), J. Cell Biol. 148, 253-258). In this study, we report that the migration of breast and squamous carcinoma cells toward either lysophosphatidic acid or epidermal growth factor involves not only phosphodiesterase activity but also cooperative signaling from PKA. Furthermore, we demonstrate that Rac1 activation in response to chemoattractant or beta(1) integrin clustering is regulated by PKA and that Rac1 is required for this migration. Also, we find that beta(1) integrin signaling stimulates the rapid and transient activation of PKA. A novel implication of these findings is that carcinoma cell migration is controlled by cAMP-dependent as well as cAMP inhibitory signaling mechanisms.
    Source
    J Biol Chem. 2001 Dec 21;276(51):47895-900. Epub 2001 Oct 17. Link to article on publisher's site
    DOI
    10.1074/jbc.M107235200
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/26284
    PubMed ID
    11606581
    Related Resources
    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1074/jbc.M107235200
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