HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 282, Issue 37, 27239-27249, September 14, 2007

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 282/37/27239    most recent M700351200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map 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 Chou, C.-C. Articles by Chen, H. Search for Related Content PubMed PubMed Citation Articles by Chou, C.-C. Articles by Chen, H. Social Bookmarking                      What's this?

Small Ubiquitin-like Modifier Modification Regulates the DNA Binding Activity of Glial Cell Missing Drosophila Homolog a^*

Chih-Chine Chou, Chingwen Chang, Jyung-Hurng Liu, Liang-Fu Chen, Chwan-Deng Hsiao, and Hungwen Chen^¶1

From the Graduate Institute of Biochemical Sciences, National Taiwan University, Taipei 106, Taiwan, the Institute of Molecular Biology, Academia Sinica, Nankang, Taipei 115, Taiwan, and the ^¶Institute of Biological Chemistry, Academia Sinica, Nankang, Taipei 115, Taiwan

Glial cell missing Drosophila homolog a (GCMa) is an essential transcription factor for placental development, which controls the differentiation of the syncytiotrophoblast layer. Although the activity of GCMa can be post-translationally regulated by protein phosphorylation, ubiquitination, and acetylation, it is unknown whether GCMa activity can be regulated by sumoylation. In this report, we investigated the role of sumoylation in the regulation of GCMa activity. We demonstrated that Ubc9, the E2 component of the sumoylation machinery, specifically interacts with the N-terminal domain of GCMa and promotes GCMa sumoylation on lysine 156. Moreover, GCMa-mediated transcriptional activation was repressed by sumoylation but was enhanced in the presence of the SUMO-specific protease, SENP1. The repressive effect of sumoylation on GCMa transcriptional activity was attributed to decreased DNA binding activity of GCMa. Furthermore, structural analysis revealed a steric clash between the SUMO1 moiety of sumoylated GCMa and the DNA-binding surfaces of GCMa, which may destabilize the interaction between GCMa and its cognate DNA sequence. Our study demonstrates that GCMa is a new sumoylation substrate and its activity is down-regulated by sumoylation.

Received for publication, January 12, 2007 , and in revised form, July 20, 2007.

^* This work was supported by National Science Council of Taiwan Grant 96-2311-B-001-034, National Taiwan University Grant 95R0066-BM06-02, and a grant from Academia Sinica of Taiwan (all to H. C.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement"in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. 1–4.

¹ To whom correspondence should be addressed: Institute of Biological Chemistry, Academia Sinica, Nankang, Taipei 115, Taiwan. Tel.: 11-886-2-27855696 (ext. 6090); Fax: 11-886-2-27889759; E-mail: hwchen{at}gate.sinica.edu.tw.

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

This article has been cited by other articles:

				Y. Tateishi, M. Ariyoshi, R. Igarashi, H. Hara, K. Mizuguchi, A. Seto, A. Nakai, T. Kokubo, H. Tochio, and M. Shirakawa Molecular Basis for SUMOylation-dependent Regulation of DNA Binding Activity of Heat Shock Factor 2 J. Biol. Chem., January 23, 2009; 284(4): 2435 - 2447. [Abstract] [Full Text] [PDF]

				L. A. Campbell, E. J. Faivre, M. D. Show, J. G. Ingraham, J. Flinders, J. D. Gross, and H. A. Ingraham Decreased Recognition of SUMO-Sensitive Target Genes following Modification of SF-1 (NR5A1) Mol. Cell. Biol., December 15, 2008; 28(24): 7476 - 7486. [Abstract] [Full Text] [PDF]

				M.-H. Chiang, L.-F. Chen, and H. Chen Ubiquitin-Conjugating Enzyme UBE2D2 Is Responsible for FBXW2 (F-Box and WD Repeat Domain Containing 2)-Mediated Human GCM1 (Glial Cell Missing Homolog 1) Ubiquitination and Degradation Biol Reprod, November 1, 2008; 79(5): 914 - 920. [Abstract] [Full Text] [PDF]

				S. W. Schubert, A. Abendroth, K. Kilian, T. Vogler, B. Mayr, I. Knerr, and S. Hashemolhosseini bZIP-Type transcription factors CREB and OASIS bind and stimulate the promoter of the mammalian transcription factor GCMa/Gcm1 in trophoblast cells Nucleic Acids Res., June 1, 2008; 36(11): 3834 - 3846. [Abstract] [Full Text] [PDF]