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J. Biol. Chem., Vol. 264, Issue 26, 15323-15327, 09, 1989
C Ra, MH Jouvin and JP Kinet
The high affinity receptor for IgE (Fc epsilon RI) found on mast cells and
basophils is a tetrameric complex of a single alpha subunit, a single beta
subunit, and two identical gamma subunits. The genes for the three subunits
of mouse Fc epsilon RI have now been cloned from the mast cell line, PT18.
When compared at the DNA level, the rat and mouse subunits are similarly
conserved. However, at the protein level the homology between mouse and rat
alpha is surprisingly low (71% identities) especially in the cytoplasmic
regions (57% identities) which are of different length (25 and 20 residues,
respectively). By contrast the beta and gamma are homogeneously conserved
between mouse and rat (83 and 93% identities, respectively). The consensus
amino acid sequence of the alpha subunit derived from three species (rat,
mouse, and human) shows that the cytoplasmic tail diverges to the same
extent as the leader peptide. Conversely, the transmembrane domain of the
alpha is highly conserved and contains 10 consecutive residues that are
identical. Comparisons between mouse Fc epsilon RI and other mouse proteins
reveal regions of high homology between the alpha subunit and Fc gamma RIIa
and between the gamma subunit and the zeta chain of the T cell receptor.
Cells transfected with the alpha gene express the alpha subunit on their
surface very inefficiently. Efficient expression is only achieved after
co-transfection of the three rodent genes or of the human alpha gene
together with the rodent gamma without apparent need for beta. The subunits
are completely interchangeable upon transfection so that various chimeric
mouse-rat-human receptors can be expressed.
Complete structure of the mouse mast cell receptor for IgE (Fc epsilon RI) and surface expression of chimeric receptors (rat-mouse-human) on transfected cells
Arthritis and Rheumatism Branch, National Institute of Arthritis and Musculoskeletal and Skin Diseases, Bethesda, Maryland 20892.
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