Posttranslational regulation of IRF-4 activity by the immunophilin FKBP52

被引：79

作者：

Mamane, Y

Sharma, S

Petropoulos, L

Lin, RT

Hiscott, J ^{[1
]}

机构：

[1] McGill Univ, Terry Fox Mol Oncol Grp, Lady Davis Inst Med Res, Montreal, PQ H3T 1E2, Canada

[2] McGill Univ, Dept Microbiol & Immunol, Montreal, PQ H3T 1E2, Canada

[3] McGill Univ, Dept Med, Montreal, PQ H3T 1E2, Canada

[4] McGill Univ, Dept Oncol, Montreal, PQ H3T 1E2, Canada

来源：

IMMUNITY | 2000年 / 12卷 / 02期

基金：

英国医学研究理事会;

关键词：

D O I：

10.1016/S1074-7613(00)80166-1

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

Interferon regulatory factor-4 (IRF-4) plays an important role in immunoregulatory gene expression in B and T lymphocytes and is also highly expressed in human T cell leukemia virus type 1 infected cells. In this study, we characterize a novel interaction between IRF-4 and the FK506-binding protein 52 (FKBP52), a 59 kDa member of the immunophilin family with peptidyl-prolyl isomerase activity (PPlase). IRF-4-FKBP52 association inhibited IRF4-PU.1 binding to the immunoglobulin light chain enhancer Elambda 2-4 as well as IRF-4-PU. 1 transactivation, effects that were dependent on functional PPlase activity. FKBP52 association also resulted in a structural modification of IRF-4, detectable by immunoblot analysis and by IRF-4 partial proteolysis. These results demonstrate a novel posttranslational mechanism of transcriptional control, mediated through the interaction of an immunophilin with a transcriptional regulator.

引用

页码：129 / 140

页数：12

共 43 条

[1] Assembly requirements of PU.1-Pip (IRF-4) activator complexes:: inhibiting function in vivo using fused dimers [J].