Sumoylation delimits KLF8 transcriptional activity associated with the cell cycle regulation

doi:10.1074/jbc.M513135200

HOME

QUICK SEARCH:

	Author:		Keyword(s):
Year:		Vol:		Page:

A more recent version of this article appeared on June 16, 2006

This Article

	Full Text (Accepted Manuscript)
	All Versions of this Article: 281/24/16664 most recent M513135200v1
	Alert me when this article is cited
	Alert me if a correction is posted

Services

	Email this article to a friend
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new issues of the journal
	Download to citation manager
	Request Permissions

Citing Articles

	Citing Articles via HighWire
	Citing Articles via Google Scholar

Google Scholar

	Articles by Wei, H.
	Articles by Zhao, J.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Wei, H.
	Articles by Zhao, J.

Social Bookmarking

	What's this?

Papers In Press, published online ahead of print April 13, 2006
J. Biol. Chem, 10.1074/jbc.M513135200
Submitted on December 8, 2005
Accepted on April 13, 2006

Sumoylation delimits KLF8 transcriptional activity associated with the cell cycle regulation

Huijun Wei, Xianhui Wang, Boyi Gan, Alison M. Urvalek, Zara K. Melkoumian, Jun-Lin Guan, and Jihe Zhao

Center for Cell Biology and Cancer Research, Albany Medical College, Albany, NY 12208

Corresponding Author: zhaojh{at}mail.amc.edu

The Krüppel-like factor 8 (KLF8) is a member of the Krüppel transcription factor family that binds CACCC elements in DNA and activates or represses their target genes in a context-dependent manner. Here we present sumoylation as a novel mechanism that regulates KLF8 post-translationally. We found that KLF8 can be covalently modified by SUMO-1, SUMO-2 and SUMO-3 in vivo. We showed that the interaction between KLF8 and SUMO E3 ligases PIAS family proteins PIAS1, PIASy and PIASxa but not with E2 SUMO conjugating enzyme Ubc9. Furthermore, we demonstrated that the E2 and E3 ligases enhanced the sumoylation of KLF8. In addition, site-directed mutagenesis identified lysine 67 as the major sumoylation site on KLF8. Lysine 67 to arginine mutation strongly enhanced activity of KLF8 as a repressor or activator to its physiological target promoters and as an inducer of the G1 cell cycle progression. Taken together, our results demonstrated that sumoylation of KLF8 negatively regulates its transcriptional activity and cellular functions.

Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Add to Reddit Reddit Add to Technorati Technorati What's this?

This article has been cited by other articles:

S. A. Eaton, A. P. W. Funnell, N. Sue, H. Nicholas, R. C. M. Pearson, and M. Crossley
A Network of Kruppel-like Factors (Klfs): Klf8 IS REPRESSED BY Klf3 AND ACTIVATED BY Klf1 IN VIVO
J. Biol. Chem., October 3, 2008; 283(40): 26937 - 26947.
[Abstract] [Full Text] [PDF]

X. Wang, A. M. Urvalek, J. Liu, and J. Zhao
Activation of KLF8 Transcription by Focal Adhesion Kinase in Human Ovarian Epithelial and Cancer Cells
J. Biol. Chem., May 16, 2008; 283(20): 13934 - 13942.
[Abstract] [Full Text] [PDF]

S. Chupreta, H. Brevig, L. Bai, J. L. Merchant, and J. A. Iniguez-Lluhi
Sumoylation-dependent Control of Homotypic and Heterotypic Synergy by the Kruppel-type Zinc Finger Protein ZBP-89
J. Biol. Chem., December 14, 2007; 282(50): 36155 - 36166.
[Abstract] [Full Text] [PDF]

X. Wang, M. Zheng, G. Liu, W. Xia, P. J. McKeown-Longo, M.-C. Hung, and J. Zhao
Kruppel-Like Factor 8 Induces Epithelial to Mesenchymal Transition and Epithelial Cell Invasion
Cancer Res., August 1, 2007; 67(15): 7184 - 7193.
[Abstract] [Full Text] [PDF]

A. P. W. Funnell, C. A. Maloney, L. J. Thompson, J. Keys, M. Tallack, A. C. Perkins, and M. Crossley
Erythroid Kruppel-Like Factor Directly Activates the Basic Kruppel-Like Factor Gene in Erythroid Cells
Mol. Cell. Biol., April 1, 2007; 27(7): 2777 - 2790.
[Abstract] [Full Text] [PDF]