FRIP, a hematopoietic cell-specific rasGAP-interacting protein phosphorylated in response to cytokine stimulation

被引：98

作者：

Nelms, K ^{[1
]}

Snow, AL ^{[1
]}

Hu-Li, J ^{[1
]}

Paul, WE ^{[1
]}

机构：

[1] NIAID, Immunol Lab, NIH, Bethesda, MD 20892 USA

来源：

IMMUNITY | 1998年 / 9卷 / 01期

关键词：

D O I：

10.1016/S1074-7613(00)80584-1

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

The human IL-4 receptor contains a sequence (the I4R motif) centered on Y497 that, when phosphorylated, interacts with phosphotyrosine-binding (PTB) domain proteins. Here, we describe a PTB domain protein, FRIP, that is phosphorylated in response to cytokine stimulation. FRIP is related to the rasGAP-associated protein p62(dok) and is bound by the N-terminal SH2 domain of rasGAP. The frip gene maps to the hairless (hr) locus on mouse chromosome 14. hr/hr mice exhibit lymphadenopathy, and their lymph node T cells proliferate more vigorously to anti-CDS with IL-4 or IL-2 stimulation than +/hr T cells. FRIP expression is significantly reduced in T cells from hr/hr mice. FRIP may negatively regulate proliferation by acting as an adapter molecule between rasGAP and receptor complexes.

引用

页码：13 / 24

页数：12

共 64 条

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