TY - JOUR
T1 - The gene and cDNA for the human high affinity immunoglobulin E receptor β chain and expression of the complete human receptor
AU - Kuster, H.
AU - Zhang, L.
AU - Brini, A. T.
AU - MacGlashan, D. W.J.
AU - Kinet, J. P.
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1992
Y1 - 1992
N2 - The high affinity IgE receptor (FcεRI) is a tetrameric hetero-oligomer composed of an α chain, a β chain, and two disulfide-linked γ chains. The β chain contains four transmembrane (TM) segments and long cytoplasmic domains that are thought to play an important role in intracellular signaling. We now report the structural characterization and the sequence of the complete human β gene and cDNA. The gene spans ~10 kilobases and contains seven exons. There is a single transcription initiation site preceded by a TATA box. The first exon codes for the 5'-untranslated region and a portion of the N-terminal cytoplasmic tail. TM-1 is encoded in exons 2 and 3, TM-2 in exons 3 and 4, TM-3 in exon 5, and TM-4 in exon 6. The seventh and final exon encodes the end of the C-terminal cytoplasmic tail and the 3'- untranslated sequence. The human β gene appears to be a single copy gene. Two corresponding transcripts, detected as a doublet around 3.9 kilobases, are present in cells of mast cell and basophil lineage from different individuals, but not in the other hematopoietic cells tested here. The human β protein is homologous to rodent β. The consensus amino acid sequences of human, mouse, and rat β show 69% identical residues. Analysis of the surface expression of transfected receptors indicates that human αγ and αβγ complexes are expressed with comparable efficiency. Human β interacts with human α more efficiently than does rat β, and both rat and mouse β interact with their corresponding α more efficiently than does human β, demonstrating a species specificity of the α/β interaction.
AB - The high affinity IgE receptor (FcεRI) is a tetrameric hetero-oligomer composed of an α chain, a β chain, and two disulfide-linked γ chains. The β chain contains four transmembrane (TM) segments and long cytoplasmic domains that are thought to play an important role in intracellular signaling. We now report the structural characterization and the sequence of the complete human β gene and cDNA. The gene spans ~10 kilobases and contains seven exons. There is a single transcription initiation site preceded by a TATA box. The first exon codes for the 5'-untranslated region and a portion of the N-terminal cytoplasmic tail. TM-1 is encoded in exons 2 and 3, TM-2 in exons 3 and 4, TM-3 in exon 5, and TM-4 in exon 6. The seventh and final exon encodes the end of the C-terminal cytoplasmic tail and the 3'- untranslated sequence. The human β gene appears to be a single copy gene. Two corresponding transcripts, detected as a doublet around 3.9 kilobases, are present in cells of mast cell and basophil lineage from different individuals, but not in the other hematopoietic cells tested here. The human β protein is homologous to rodent β. The consensus amino acid sequences of human, mouse, and rat β show 69% identical residues. Analysis of the surface expression of transfected receptors indicates that human αγ and αβγ complexes are expressed with comparable efficiency. Human β interacts with human α more efficiently than does rat β, and both rat and mouse β interact with their corresponding α more efficiently than does human β, demonstrating a species specificity of the α/β interaction.
UR - http://www.scopus.com/inward/record.url?scp=0026680288&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026680288&partnerID=8YFLogxK
M3 - Article
C2 - 1535625
AN - SCOPUS:0026680288
SN - 0021-9258
VL - 267
SP - 12782
EP - 12787
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 18
ER -