Number of the records: 1  

Down-regulation of protein-tyrosine phosphatases activates an immune receptor in the absence of its translocation into lipid rafts

  1. 1.
    SYSNO ASEP0346787
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleDown-regulation of protein-tyrosine phosphatases activates an immune receptor in the absence of its translocation into lipid rafts
    Author(s) Heneberg, Petr (UMG-J)
    Dráberová, Lubica (UMG-J) RID
    Bambousková, Monika (UMG-J)
    Pompach, Petr (MBU-M) RID, ORCID
    Dráber, Petr (UMG-J) RID
    Source TitleJournal of Biological Chemistry. - : Elsevier - ISSN 0021-9258
    Roč. 285, č. 17 (2010), s. 12787-12802
    Number of pages16 s.
    Languageeng - English
    CountryUS - United States
    Keywordsmast cell ; cell signaling ; plasma membrane
    Subject RIVEB - Genetics ; Molecular Biology
    R&D ProjectsGA301/09/1826 GA ČR - Czech Science Foundation (CSF)
    GAP302/10/1759 GA ČR - Czech Science Foundation (CSF)
    1M0506 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    1M0505 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    LC545 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    KAN200520701 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR)
    CEZAV0Z50520514 - UMG-J (2005-2011)
    AV0Z50200510 - MBU-M (2005-2011)
    UT WOS000276787800037
    DOI10.1074/jbc.M109.052555
    AnnotationIn mast cells and basophils activated by multivalent antigen-IgE complexes, tyrosine phosphorylation of the high affinity IgE receptor (FcepsilonRI) is mediated by Src family protein tyrosine (PTK) kinase Lyn. However, the exact molecular mechanism of this phosphorylation step is incompletely understood. In this study, we tested the hypothesis that changes in activity and/or topography of protein-tyrosine phosphatases (PTPs) could play a major role in the FcepsilonRI triggering. We found that exposure of rat basophilic leukemia cells or mouse bone marrow-derived mast cells to PTP inhibitors, H2O2 or pervanadate, induced phosphorylation of the FcepsilonRI subunits, similarly as FcepsilonRI triggering. Interestingly, and in sharp contrast to antigen-induced activation, neither H2O2 nor pervanadate induced any changes in the association of FcepsilonRI with detergent-resistant membranes on isolated plasma membrane sheets.
    WorkplaceInstitute of Molecular Genetics
    ContactNikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217
    Year of Publishing2011
Number of the records: 1  

  This site uses cookies to make them easier to browse. Learn more about how we use cookies.