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Suppression of immunoglobulin E-mediated allergic responses by regulator of G protein signaling 13.

Nature immunology | Jan 18, 2008

http://www.ncbi.nlm.nih.gov/pubmed/18026105

Mast cells elicit allergic responses through degranulation and release of proinflammatory mediators after antigen crosslinking of the immunoglobulin E receptor FcepsilonRI. Proteins of the 'regulator of G protein signaling' (RGS) family negatively control signaling mediated by G protein-coupled receptors through GTPase-accelerating protein activity. Here we show that RGS13 inhibited allergic responses by physically interacting with the regulatory p85alpha subunit of phosphatidylinositol-3-OH kinase in mast cells and disrupting its association with an FcepsilonRI-activated scaffolding complex. Rgs13-/- mice had enhanced immunoglobulin E-mediated mast cell degranulation and anaphylaxis. Thus, RGS13 inhibits the assembly of immune receptor-induced signalosomes in mast cells. Abnormal RGS13 expression or function may contribute to disorders of amplified mast cell activity, such as idiopathic anaphylaxis.

Pubmed ID: 18026105 RIS Download

Mesh terms: Anaphylaxis | Animals | Cell Degranulation | Cells, Cultured | Enzyme Activation | Immunoglobulin E | Mast Cells | Mice | Mice, Knockout | Phosphatidylinositol 3-Kinases | RGS Proteins | Receptors, IgE | Signal Transduction

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Associated grants

  • Agency: Intramural NIH HHS, Id: Z01 AI000746-10

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