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Semin Immunol. 1995 Feb;7(1):29-35.

Signal transduction through the conserved motifs of the high affinity IgE receptor Fc epsilon RI.

Author information

1
Molecular Allergy and Immunology Section, NIAID, NIH, Rockville, MD 20852, USA.

Abstract

The high affinity receptor for IgE, Fc epsilon RI, possesses three ARAMs, one in the beta chain (ARAM-beta) and one in each member of the dimer of gamma chains (ARAM-gamma). These two types of ARAM endow the chains in which they are located with distinct properties. The ARAM-containing C-terminal tail of beta binds Lyn, a Src family tyrosine kinase which regulates the phosphorylation of beta, gamma and other substrates including Syk. The tyrosine phosphorylated ARAM-containing C-terminal tail of gamma binds Syk which, when activated, controls later signals such as the rise in intracellular calcium. Therefore, the two ARAM-containing chains of Fc epsilon RI cooperate to realize the full signaling capacity of the receptor.

PMID:
7612892
DOI:
10.1016/1044-5323(95)90005-5
[Indexed for MEDLINE]

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