Xinting Wang and Xin Liu contributed equally to this article.
Coactivator P100 Protein Enhances STAT6-Dependent Transcriptional Activation But Has No Effect on STAT1-Mediated Gene Transcription
Article first published online: 11 MAR 2010
Copyright © 2010 Wiley-Liss, Inc.
The Anatomical Record
Volume 293, Issue 6, pages 1010–1016, June 2010
How to Cite
Wang, X., Liu, X., Fang, J., Lu, Y., He, J., Yao, X., Yao, Z. and Yang, J. (2010), Coactivator P100 Protein Enhances STAT6-Dependent Transcriptional Activation But Has No Effect on STAT1-Mediated Gene Transcription. Anat Rec, 293: 1010–1016. doi: 10.1002/ar.21143
- Issue published online: 19 MAY 2010
- Article first published online: 11 MAR 2010
- Manuscript Accepted: 27 DEC 2009
- Manuscript Received: 16 SEP 2009
- Ministry of Science and Technology of China (863 project). Grant Number: 2007AA02Z115
- National Natural Science Foundation of China. Grant Numbers: 90919032, 30970562, 30670441, 30670802
- Tianjin Municipal Science and Technology Commission. Grant Numbers: 08ZCGHHZ01900, 08JCYBJC07700, 2009CB918903
- 973 Program. Grant Number: 2009CB918903
- Specialized Fund for the Doctoral Program of Higher Education. Grant Number: 20091202110001
- Tianjin Educational Committee Foundation. Grant Number: 2008ZD01
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. Anat Rec, 2010. © 2010 Wiley-Liss, Inc.