Journal
EUROPEAN JOURNAL OF IMMUNOLOGY
Volume 48, Issue 3, Pages 441-453Publisher
WILEY
DOI: 10.1002/eji.201747196
Keywords
Allergies; B cell antigen receptor (BCR); ER retention; IgE; Signal transduction
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Funding
- Deutsche Forschungsgemeinschaft [EN834/2-1, TRR130]
- Deutsche Forschungsgemeinschaft through Cluster of Excellence Nanoscale Microscopy and Molecular Physiology of the Brain (CNMPB)
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Immunoglobulin E (IgE) antibodies are key mediators of allergic reactions. Due to their potentially harmful anaphylactic properties, their production is tightly regulated. The membrane-bound isoform of IgE (mIgE), which is an integral component of the B cell antigen receptor, has been shown to be critical for the regulation of IgE responses in mice. In primate species including humans, mIgE can be expressed in two isoforms that are produced by alternative splicing of the primary epsilon Ig heavy chain transcript, and differ in the absence or presence of an extracellular membrane-proximal domain (EMPD) consisting of 52 amino acids. However, the function of the EMPD remains unclear. Here, we demonstrate that the EMPD restricts surface expression of mIgE-containing BCRs in human and murine B cells. The EMPD does not interfere with BCR assembly but acts as an autonomous endoplasmic reticulum retention domain. Limited surface expression of EMPD-containing mIgE-BCRs caused impaired activation of intracellular signaling cascades and hence represents a regulatory mechanism that may control the production of potentially anaphylactic IgE antibodies in primate species.
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