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

0346787 - ÚMG 2011 RIV US eng J - Journal Article
Heneberg, Petr - Dráberová, Lubica - Bambousková, Monika - Pompach, Petr - Dráber, Petr
Down-regulation of protein-tyrosine phosphatases activates an immune receptor in the absence of its translocation into lipid rafts.
Journal of Biological Chemistry. Roč. 285, č. 17 (2010), s. 12787-12802. ISSN 0021-9258. E-ISSN 1083-351X
R&D Projects: GA ČR GA301/09/1826; GA ČR GAP302/10/1759; GA MŠMT 1M0506; GA MŠMT 1M0505; GA MŠMT LC545; GA AV ČR KAN200520701
Institutional research plan: CEZ:AV0Z50520514; CEZ:AV0Z50200510
Keywords : mast cell * cell signaling * plasma membrane
Subject RIV: EB - Genetics ; Molecular Biology
Impact factor: 5.328, year: 2010

In 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.
Permanent Link: http://hdl.handle.net/11104/0187716