SOLUBLE AND MEMBRANE-ANCHORED FORMS OF THE HUMAN IFN-ALPHA/BETA RECEPTOR

被引：34

作者：

NOVICK, D ^{[1
]}

COHEN, B ^{[1
]}

TAL, N ^{[1
]}

RUBINSTEIN, M ^{[1
]}

机构：

[1] WEIZMANN INST SCI,DEPT MOLEC GENET & VIROL,IL-76100 REHOVOT,ISRAEL

来源：

JOURNAL OF LEUKOCYTE BIOLOGY | 1995年 / 57卷 / 05期

关键词：

TYROSINE PHOSPHORYLATION; JAK1; TYPE I IFN; CYTOKINE RECEPTOR FAMILY II;

D O I：

10.1002/jlb.57.5.712

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The recently cloned ligand binding component of the type I human interferon-alpha/beta receptor (IFN-alpha/beta R) 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-alpha/beta R. We find that the 51 kDa IFN-alpha/beta R is a disulfide-linked subunit of the 102-kDa IFN-alpha/beta R. Two types of cDNA clones were isolated and sequenced, a 1.5-kb cDNA coding for the transmembrane 51-kDa IFN-alpha/beta R and a 4.5-kb cDNA coding for p40. In addition to ligand binding, IFN-alpha/beta R 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.

引用

页码：712 / 718

页数：7