Blood · 2009 · 119 citations · 32 references
Life SciencesCell BiologyMolecular BiologyCell SignalingCytoskeletonSignal TransductionCalcium SignalingCyclic Nucleotide SignalingCytoskeletal SignalingIntracellular Calcium SignalingMast Cell ActivationProtein Kinase CascadesCalcium-induced Calcium ReleaseDegranulation MechanismsMast Cell Calcium SignalingMast Cell Degranulation InhibitionMast Cell Degranulation PathwaysMast Cell Membrane DynamicsMast Cell Signal TransductionMast Cell Signaling Pathways
Mast cells are key participants in allergic diseases via activation of high-affinity IgE receptors (FcepsilonRI) resulting in release of proinflammatory mediators. The biochemical pathways linking IgE activation to calcium influx and cytoskeletal changes required for intracellular granule release are incompletely understood. We demonstrate, genetically, that Pak1 is required for this process. In a passive cutaneous anaphylaxis experiment, W(sh)/W(sh) mast cell-deficient mice locally reconstituted with Pak1(-/-) bone marrow-derived mast cells (BMMCs) experienced strikingly decreased allergen-induced vascular permeability compared with controls. Consistent with the in vivo phenotype, Pak1(-/-) BMMCs exhibited a reduction in FcepsilonRI-induced degranulation. Further, Pak1(-/-) BMMCs demonstrated diminished calcium mobilization and altered depolymerization of cortical filamentous actin (F-actin) in response to FcepsilonRI stimulation. These data implicate Pak1 as an essential molecular target for modulating acute mast cell responses that contribute to allergic diseases.
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Human p21-activated kinase (Pak1) regulates actin organization in mammalian cells
Mary Ann Sells, Ulla G. Knaus, Shubha Bagrodia et al. · Current Biology · 1997 · 696 citations · Full text
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