SPI-C和STAT6可以协同刺激IgE种系转录。

SPI-C and STAT6 can cooperate to stimulate IgE germline transcription.

作者信息

Carlsson Robert, Thorell Kaisa, Liberg David, Leanderson Tomas

机构信息

Immunology Group, Lund University, BMC I:13, 22184 Lund, Sweden.

出版信息

Biochem Biophys Res Commun. 2006 Jun 16;344(4):1155-60. doi: 10.1016/j.bbrc.2006.04.026. Epub 2006 May 2.

DOI:10.1016/j.bbrc.2006.04.026

PMID:16647686

Abstract

SPI-C is a novel ETS protein that is expressed in B lymphocytes. No target gene for SPI-C has so far been defined. We have performed a yeast two-hybrid screen using SPI-C as bait in order to further analyze the functional role of this orphan transcription factor. We found that SPI-C interacted specifically with the C-terminus of STAT6 in yeast. By co-immunoprecipitation in transfected COS7 cells the physical interaction between SPI-C and STAT6 was confirmed. Furthermore, this protein-protein interaction is functional since we could demonstrate that SPI-C and STAT6 stimulated IL4 induced Iepsilon transcription synergistically but only when both proteins bound to DNA. Thus, a protein interaction between SPI-C and STAT6 is the basis for a novel mechanism for regulation of IL4 induced gene expression.

摘要

SPI-C是一种在B淋巴细胞中表达的新型ETS蛋白。迄今为止，尚未确定SPI-C的靶基因。为了进一步分析这种孤儿转录因子的功能作用，我们以SPI-C为诱饵进行了酵母双杂交筛选。我们发现SPI-C在酵母中与STAT6的C末端特异性相互作用。通过在转染的COS7细胞中进行共免疫沉淀，证实了SPI-C与STAT6之间的物理相互作用。此外，这种蛋白质-蛋白质相互作用具有功能，因为我们可以证明SPI-C和STAT6协同刺激IL4诱导的Iepsilon转录，但前提是两种蛋白质都与DNA结合。因此，SPI-C与STAT6之间的蛋白质相互作用是IL4诱导基因表达调控新机制的基础。