STAT3 forms stable homodimers in the presence of divalent cations prior to activation

被引：57

作者：

Novak, U

Ji, H

Kanagasundaram, V

Simpson, R

Paradiso, L

机构：

[1] Univ Melbourne, Royal Melbourne Hosp, Dept Med, Parkville, Vic 3050, Australia

[2] Ludwig Inst Canc Res, Joint Prot Struct Lab, Parkville, Vic 3050, Australia

[3] Walter & Eliza Hall Inst Med Res, Parkville, Vic 3050, Australia

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1998年 / 247卷 / 03期

基金：

英国医学研究理事会;

关键词：

D O I：

10.1006/bbrc.1998.8829

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We present evidence that the transcription factor STAT3, derived from uninduced cells, can form stable homodimers, which are independent of the tyrosine phosphorylation status of the protein. The strong interaction, which is resistant to many denaturing agents, is dependent on the presence of divalent cations. The presence of the homodimer was initially observed in immunoprecipitates of STAT3 and was detected upon fractionation of cell lysates. These dimers are different in structure from dimers observed after cytokine stimulation of cells, which results in tyrosine phosphorylation of STAT3 and dimerization involving the SH2 domain of STAT3. (C) 1998 Academic Press.

引用

页码：558 / 563

页数：6

共 28 条

[1] Interleukin-2 activation of STAT5 requires the convergent action of tyrosine kinases and a serine/threonine kinase pathway distinct from the Raf1/ERK2 MAP kinase pathway [J].