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Soluble and membrane‐anchored forms of the human IFN‐α/β receptor
Author(s) -
Novick Daniela,
Cohen Batya,
Tal Natan,
Rubinstein Menachem
Publication year - 1995
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.57.5.712
Subject(s) - biology , complementary dna , transmembrane protein , microbiology and biotechnology , protein subunit , receptor , ligand (biochemistry) , interferon , phosphorylation , tyrosine kinase , tyrosine , transmembrane domain , immunoprecipitation , antibody , biochemistry , gene , genetics
The recently cloned ligand binding component of the type I human interferon‐α/β receptor (IFN‐α/βR) and its soluble analogue (p40) were characterized. p40 is a potent inhibitor of type I IFNs and antibodies directed against p40 completely block the activity of type I IFNs in human cells. These antibodies immunoprecipitate cellular 102‐kDa (major) and 51‐kDa (minor) forms of IFN‐α/βR. We find that the 51‐kDa IFN‐α/βR is a disulfide‐linked subunit of the 102‐kDa IFN‐α/βR. Two types of cDNA clones were isolated and sequenced, a 1.5‐kb cDNA coding for the transmembrane 51‐kDa IFN‐α/βR and a 4.5‐kb cDNA coding for p40. In addition to ligand binding, IFN‐α/βR is directly involved in signaling, because it becomes phosphorylated at Tyr residues on ligand binding and it is physically associated with the cytoplasmic tyrosine kinase JAK1. J. Leukoc. Biol . 57: 712–718; 1995.