The binding of IgE to high-affinity IgE receptors (Fc epsilon RI) expressed on the surface of mast cells and basophils initiates a cascade of signaling events that results in the release of a wide array of proinflammatory mediators. In order to limit the intensity and duration of cell activation, Fc epsilon RI aggregation has been understood to additionally generate negative signals through the coordinated action of adapters, phosphatases, and ubiquitin ligases. Among them, Cbl family proteins negatively regulate Fc epsilon RI-mediated signals mainly by promoting ubiquitination of the activated receptor subunits and associated protein tyrosine kinases. Notably, Fc epsilon RI ubiquitination has become recognized as an important signal for the internalization and delivery of engaged receptor complexes to lysosomes for degradation. The surface expression of activated Fc epsilon RI complexes is further downregulated through a pathway that is functionally separable from Cbl ligase activity and is dependent on the interaction of Cbl proteins with adapters involved in clathrin-dependent endocytosis. In this article, we review recent advances in our understanding of the molecular mechanisms through which Cbl proteins negatively regulate Fc epsilon RI-mediated mast cell and basophil functions. Copyright (C) 2011 S. Karger AG, Basel

Cbl Family Proteins: Balancing Fc epsilon RI-Mediated Mast Cell and Basophil Activation / Gasparrini, Francesca; Molfetta, Rosa; Santoni, Angela; Paolini, Rossella. - In: INTERNATIONAL ARCHIVES OF ALLERGY AND IMMUNOLOGY. - ISSN 1018-2438. - STAMPA. - 156:1(2011), pp. 16-26. [10.1159/000322236]

Cbl Family Proteins: Balancing Fc epsilon RI-Mediated Mast Cell and Basophil Activation

GASPARRINI, FRANCESCA;MOLFETTA, Rosa;SANTONI, Angela;PAOLINI, Rossella
2011

Abstract

The binding of IgE to high-affinity IgE receptors (Fc epsilon RI) expressed on the surface of mast cells and basophils initiates a cascade of signaling events that results in the release of a wide array of proinflammatory mediators. In order to limit the intensity and duration of cell activation, Fc epsilon RI aggregation has been understood to additionally generate negative signals through the coordinated action of adapters, phosphatases, and ubiquitin ligases. Among them, Cbl family proteins negatively regulate Fc epsilon RI-mediated signals mainly by promoting ubiquitination of the activated receptor subunits and associated protein tyrosine kinases. Notably, Fc epsilon RI ubiquitination has become recognized as an important signal for the internalization and delivery of engaged receptor complexes to lysosomes for degradation. The surface expression of activated Fc epsilon RI complexes is further downregulated through a pathway that is functionally separable from Cbl ligase activity and is dependent on the interaction of Cbl proteins with adapters involved in clathrin-dependent endocytosis. In this article, we review recent advances in our understanding of the molecular mechanisms through which Cbl proteins negatively regulate Fc epsilon RI-mediated mast cell and basophil functions. Copyright (C) 2011 S. Karger AG, Basel
2011
ubiquitination; cbl family proteins; fc epsilon ri; negative regulation; mast cells; basophils
01 Pubblicazione su rivista::01a Articolo in rivista
Cbl Family Proteins: Balancing Fc epsilon RI-Mediated Mast Cell and Basophil Activation / Gasparrini, Francesca; Molfetta, Rosa; Santoni, Angela; Paolini, Rossella. - In: INTERNATIONAL ARCHIVES OF ALLERGY AND IMMUNOLOGY. - ISSN 1018-2438. - STAMPA. - 156:1(2011), pp. 16-26. [10.1159/000322236]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/122331
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