Role of the extracellular domain of Fc epsilon RI alpha in intracellular processing and surface expression of the high affinity receptor for IgE Fc epsilon RI

Molecular Immunology
Mor-Li HartmanJ P Kinet

Abstract

The high affinity receptor for immunoglobulin E, Fc epsilon RI, is a critical component of IgE-mediated allergic reactions. It is expressed as a tetramer (alphabetagamma(2)) made of an IgE-binding alpha chain and a signaling module formed by the beta chain and a dimer of gamma chains. It is expressed in humans and rodents on basophils and mast cells at a high level, and, upon activation, it induces the liberation of allergy mediators. In humans a trimeric form lacking the beta chain also exists (alphagamma(2)). This trimeric form is expressed on antigen presenting cells where it acts to facilitate antigen presentation via IgE. Both the expression and the signaling capacity of the trimer are lower than those of the tetramer. The differences between human (tetrameric and trimeric) and murine (tetrameric only) expression is explained in part by the fact that mouse alpha cannot be expressed at the cell surface in the absence of beta, while human alpha can. Here we demonstrate that the capacity of human alpha to be expressed at the cell surface in the absence of beta is encoded entirely in its extracellular domain. These findings show that the extracellular domain of the type I transmembrane protein Fc epsilon RI alpha plays a role ...Continue Reading

Citations

Jul 30, 2011·The Journal of Biological Chemistry·Lawren C Wu
Oct 5, 2011·The Journal of Experimental Medicine·Adeline PorcherieSalaheddine Mécheri
Nov 17, 2009·Immunological Reviews·Taku KambayashiGary A Koretzky
Jan 1, 2010·The Journal of Immunology : Official Journal of the American Association of Immunologists·Asifa K Zaidi, Donald W MacGlashan
Jul 2, 2019·Current Pharmaceutical Biotechnology·Xiangsheng LiZhongcheng Liu
Sep 30, 2008·Current Opinion in Immunology·Donald MacGlashan

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