Ubiquitination and endocytosis of the high affinity receptor for IgE

Abstract

The high affinity receptor for IgE (Fce{open}RI) is constitutivelly expressed on the surface of mast cells and basophils as a multimeric complex. Upon antigen ligation to Fce{open}RI-bound IgE molecules, the receptor complex transduces intracellular signals leading to the release of preformed and newly synthesised pro-inflammatory mediators.Fce{open}RI engagement also generates negative intracellular signals involving the coordinated action of adapters, phosphatases and ubiquitin ligases that limits the intensity and duration of positive signals. Relevant to this, antigen-induced Fce{open}RI ubiquitination has become recognized as an important signal for the internalization and delivery of engaged receptor complexes to lysosomes for degradation.In this article, we review recent advances in our understanding of molecular mechanisms that guarantee the clearance of antigen-stimulated Fce{open}RI complexes from the cell surface.A particular emphasis will be given on how lipid rafts and the ubiquitin pathway cooperate to ensure receptor internalization and sorting along the endocytic compartments.A brief discussion regarding how ubiquitination regulates the endocytosis of Fc receptors other than Fce{open}RI will be included. © 2010 Elsevier Ltd.