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Coactivator P100 protein enhances STAT6-dependent transcriptional activation but has no effect on STAT1-mediated gene transcription.

Authors
  • Wang, Xinting
  • Liu, Xin
  • Fang, Jianfei
  • Lu, Yanxin
  • He, Jinyan
  • Yao, Xuyang
  • Yao, Zhi
  • Yang, Jie
Type
Published Article
Journal
Anatomical record (Hoboken, N.J. : 2007)
Publication Date
Jun 01, 2010
Volume
293
Issue
6
Pages
1010–1016
Identifiers
DOI: 10.1002/ar.21143
PMID: 20225206
Source
Medline
License
Unknown

Abstract

The family of STAT proteins consists of seven members that mediate highly specific functions in cytokine signaling. STAT6 is a critical regulator of transcription for interleukin-4 (IL-4)-induced genes. Activation of gene expression involves recruitment of coactivator proteins that function as bridging factors connecting sequence-specific transcription factors to the basal transcription machinery, and as chromatin-modifying enzymes. In this report, we show that the coacitivator p100 protein can interact with STAT6 through its SN domain both in vivo and in vitro, resulting in enhancement of STAT6-mediated gene transcriptional acitivation. Consistent with our previous reports, we identified intracellular localization of p100 and STAT-6 by confocal microscopy examined in response to IL-4. Moreover, in consideration of STAT molecules sharing significant homology in structure and function, we detected whether p100 can associate with STAT-1. In conclusion, this study found no evidence that p100 functions as a transcriptional coactivator for STAT1-dependent gene regulation.

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