ArticleMolecular immunology2009
The first transmembrane region of the beta-chain stabilizes the tetrameric Fc epsilon RI complex.
Article in Molecular immunology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Exon Skipping of FcεRIβ for Allergic Diseases.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Article
- Article
- Regulation of Trafficking and Signaling of the High Affinity IgE Receptor by FcεRIβ and the Potential Impact of FcεRIβ Splicing in Allergic Inflammation.International journal of molecular sciences · 2022Review
- Complement-Activating Anti-HLA Antibodies in Kidney Transplantation: Allograft Gene Expression Profiling and Response to Treatment.Journal of the American Society of Nephrology : JASN · 2018Article
- Exon skipping of FcεRIβ eliminates expression of the high-affinity IgE receptor in mast cells with therapeutic potential for allergy.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Mast cells in airway diseases and interstitial lung disease.European journal of pharmacology · 2016Review
- A truncated splice-variant of the FcεRIβ receptor subunit is critical for microtubule formation and degranulation in mast cells.Immunity · 2013Article
- Development and validation of a standardized ELISA for the detection of soluble Fc-epsilon-RI in human serum.Journal of immunological methods · 2011Article
- A soluble form of the high affinity IgE receptor, Fc-epsilon-RI, circulates in human serum.PloS one · 2011Article
- A novel FcεRIβ-chain truncation regulates human mast cell proliferation and survival.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2010Article
- The SCHOOL of nature: I. Transmembrane signaling.Self/nonself · 2010Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The family of activating immune receptors stabilizes via the 3-helix assembly principle. A charged basic transmembrane residue interacts with two charged acidic transmembrane residues and forms a 3-helix interface to stabilize receptor complexes in the lipid bilayer. One family member, the high affinity receptor for IgE, Fc epsilon RI, is a key regulator of immediate allergic responses. Tetrameric Fc epsilon RI consists of the IgE-binding alpha-chain, the multimembrane-spanning beta-chain and a dimer of the gamma-subunit (Fc epsilon R gamma). Comparative analysis of these seven transmembrane regions indicates that Fc epsilon RI does not meet the charge requirements for the 3-helix assembly mechanism. We performed alanine mutagenesis to show that the only basic amino acid in the transmembrane regions, beta K97, is not involved in Fc epsilon RI stabilization or surface upregulation, a hallmark function of the beta-chain. Even a beta K97E mutant is functional despite four negatively charged acidic amino acids in the transmembrane regions. Using truncation mutants, we demonstrate that the first uncharged transmembrane domain of the beta-chain contains the interface for receptor stabilization. In vitro translation experiments depict the first transmembrane region as the internal signal peptide of the beta-chain. We also show that this beta-chain domain can function as a cleavable signal peptide when used as a leader peptide for a Type I protein. Our results provide evidence that tetrameric Fc epsilon RI does not assemble according to the 3-helix assembly principle. We conclude that receptors formed with multispanning proteins use different mechanisms of shielding transmembrane charged amino acids.
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