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TitleMolecular mechanism of IgE-mediated FcεRI activation.
Journal, issue, pagesNature, Vol. 637, Issue 8045, Page 453-460, Year 2025
Publish dateOct 23, 2024
AuthorsMengying Chen / Qiang Su / Yigong Shi /
PubMed AbstractAllergic diseases affect more than a quarter of individuals in industrialized countries, and are a major public health concern. The high-affinity Fc receptor for immunoglobulin E (FcεRI), which is ...Allergic diseases affect more than a quarter of individuals in industrialized countries, and are a major public health concern. The high-affinity Fc receptor for immunoglobulin E (FcεRI), which is mainly present on mast cells and basophils, has a crucial role in allergic diseases. Monomeric immunoglobulin E (IgE) binding to FcεRI regulates mast cell survival, differentiation and maturation. However, the underlying molecular mechanism remains unclear. Here we demonstrate that prior to IgE binding, FcεRI exists mostly as a homodimer on human mast cell membranes. The structure of human FcεRI confirms the dimeric organization, with each promoter comprising one α subunit, one β subunit and two γ subunits. The transmembrane helices of the α subunits form a layered arrangement with those of the γ and β subunits. The dimeric interface is mediated by a four-helix bundle of the α and γ subunits at the intracellular juxtamembrane region. Cholesterol-like molecules embedded within the transmembrane domain may stabilize the dimeric assembly. Upon IgE binding, the dimeric FcεRI dissociates into two protomers, each of which binds to an IgE molecule. This process elicits transcriptional activation of Egr1, Egr3 and Ccl2 in rat basophils, which can be attenuated by inhibiting the FcεRI dimer-to-monomer transition. Collectively, our study reveals the mechanism of antigen-independent, IgE-mediated FcεRI activation.
External linksNature / PubMed:39442557
MethodsEM (single particle)
Resolution3.14 - 3.9 Å
Structure data

39614

8yvu

EMDB-39614, PDB-8yvu:
structure of Ige receptor
Method: EM (single particle) / Resolution: 3.9 Å

39627

8ywa

EMDB-39627, PDB-8ywa:
The structure of IgE receptor binding to IgE
Method: EM (single particle) / Resolution: 3.14 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / immunology / Ige receptor / allergy / MEMBRANE PROTEIN/IMMUNE SYSTEM / MEMBRANE PROTEIN-IMMUNE SYSTEM complex

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