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Dynamic Interactions of Fc Receptor IIB with Filamin-Bound SHIP1 Amplify Filamentous Actin-Dependent Negative Regulation of Fc Receptor I Signaling¹

Renaud Lesourne^*,, Wolf H. Fridman^* and Marc Daëron^2,*,

^* Laboratoire d’Immunologie Cellulaire et Clinique, Institut National de la Santé et de la Recherche Médicale, Unité 255, Institut Biomédical des Cordeliers, Paris, France; and Unité d’Allergologie Moléculaire et Cellulaire, Institut Pasteur, Paris, France

The engagement of high affinity receptors for IgE (FcRI) generates both positive and negative signals whose integration determines the intensity of mast cell responses. FcRI-positive signals are also negatively regulated by low affinity receptors for IgG (FcRIIB). Although the constitutive negative regulation of FcRI signaling was shown to depend on the submembranous F-actin skeleton, the role of this compartment in FcRIIB-dependent inhibition is unknown. We show in this study that the F-actin skeleton is essential for FcRIIB-dependent negative regulation. It contains SHIP1, the phosphatase responsible for inhibition, which is constitutively associated with the actin-binding protein, filamin-1. After coaggregation, FcRIIB and FcRI rapidly interact with the F-actin skeleton and engage SHIP1 and filamin-1. Later, filamin-1 and F-actin dissociate from FcR complexes, whereas SHIP1 remains associated with FcRIIB. Based on these results, we propose a dynamic model in which the submembranous F-actin skeleton forms an inhibitory compartment where filamin-1 functions as a donor of SHIP1 for FcRIIB, which concentrate this phosphatase in the vicinity of FcRI and thereby extinguish activation signals.

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