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    Cyclic nucleotide dependent dephosphorylation of regulator of G-protein signaling 18 in human platelets.

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    Authors
    Gegenbauer, Kristina
    Nagy, Zoltan
    Smolenski, Albert
    Issue Date
    2013-11
    Keywords
    CELL BIOLOGY
    PROTEINS
    Local subject classification
    NUCLEOTIDES
    MeSH
    14-3-3 Proteins
    Cell Line
    Cyclic AMP-Dependent Protein Kinases
    Cyclic GMP-Dependent Protein Kinases
    Humans
    Immunoprecipitation
    Phosphorylation
    RGS Proteins
    Signal Transduction
    
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    Citation
    Cyclic nucleotide dependent dephosphorylation of regulator of G-protein signaling 18 in human platelets. 2013, 8 (11):e80251 PLoS ONE
    Journal
    PloS one
    URI
    http://hdl.handle.net/10147/567106
    DOI
    10.1371/journal.pone.0080251
    PubMed ID
    24244663
    Additional Links
    http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0080251
    Abstract
    Regulator of G-protein signaling 18 (RGS18) is a GTPase-activating protein that turns off Gq signaling in platelets. RGS18 is regulated by binding to the adaptor protein 14-3-3 via phosphorylated serine residues S49 and S218 on RGS18. In this study we confirm that thrombin, thromboxane A2, or ADP stimulate the interaction of RGS18 and 14-3-3 by increasing the phosphorylation of S49. Cyclic AMP- and cyclic GMP-dependent kinases (PKA, PKG) inhibit the interaction of RGS18 and 14-3-3 by phosphorylating S216. To understand the effect of S216 phosphorylation we studied the phosphorylation kinetics of S49, S216, and S218 using Phos-tag gels and phosphorylation site-specific antibodies in transfected cells and in platelets. Cyclic nucleotide-induced detachment of 14-3-3 from RGS18 coincides initially with double phosphorylation of S216 and S218. This is followed by dephosphorylation of S49 and S218. Dephosphorylation of S49 and S218 might be mediated by protein phosphatase 1 (PP1) which is linked to RGS18 by the regulatory subunit PPP1R9B (spinophilin). We conclude that PKA and PKG induced S216 phosphorylation triggers the dephosphorylation of the 14-3-3 binding sites of RGS18 in platelets.
    Item Type
    Article
    Language
    en
    ISSN
    1932-6203
    ae974a485f413a2113503eed53cd6c53
    10.1371/journal.pone.0080251
    Scopus Count
    Collections
    St. James's Hospital

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