This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Tian, Y. Articles by Benjamin, T. Search for Related Content PubMed PubMed Citation Articles by Tian, Y. Articles by Benjamin, T.

 Previous Article  |  Next Article 

Journal of Virology, November 2004, p. 12657-12664, Vol. 78, No. 22
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.22.12657-12664.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Identification of TAZ as a Binding Partner of the Polyomavirus T Antigens

Department of Pathology, Harvard Medical School, Boston Massachusetts

Received 26 January 2004/ Accepted 9 July 2004

A polyomavirus mutant isolated by the tumor host range selection procedure (19) has a three-amino-acid deletion (2-4) in the common N terminus of the T antigens. To search for a cellular protein bound by wild-type but not the mutant T antigen(s), a yeast two-hybrid screen of a mouse embryo cDNA library was carried out with a bait of wild-type small T antigen (sT) fused N terminally to the DNA-binding domain of Gal4. TAZ, a transcriptional coactivator with a WW domain and PDZ-binding motif (17), was identified as a binding partner. TAZ bound in vivo to all three T antigens with different apparent affinities estimated as 1:7:100 (large T antigen [lT]:middle T antigen [mT]:sT). The 2-4 mutant T antigens showed no detectable binding. The sT and mT of the host range transformation-defective (hr-t) mutant NG59 with an alteration in the common sT/mT region (179 DNI) and a normal N terminus also failed to bind TAZ, while the unaltered lT bound but with reduced affinity compared to that seen in a wild-type virus infection. The WW domain but not the PDZ-binding motif of TAZ was essential for T antigen binding. The 2-4 mutant was defective in viral DNA replication. Forced overexpression of TAZ blocked wild-type DNA replication in a manner dependent on the binding site for the polyomavirus enhancer-binding protein 2. Wild-type polyomavirus T antigens effectively block transactivation by TAZ. The functional significance of TAZ interactions with polyomavirus T antigens is discussed.

This article has been cited by other articles:

• Chan, S. W., Lim, C. J., Guo, K., Ng, C. P., Lee, I., Hunziker, W., Zeng, Q., Hong, W. (2008). A Role for TAZ in Migration, Invasion, and Tumorigenesis of Breast Cancer Cells. Cancer Res. 68: 2592-2598 [Abstract] [Full Text]  
• Lei, Q.-Y., Zhang, H., Zhao, B., Zha, Z.-Y., Bai, F., Pei, X.-H., Zhao, S., Xiong, Y., Guan, K.-L. (2008). TAZ Promotes Cell Proliferation and Epithelial-Mesenchymal Transition and Is Inhibited by the Hippo Pathway. Mol. Cell. Biol. 28: 2426-2436 [Abstract] [Full Text]  
• Tian, Y., Kolb, R., Hong, J.-H., Carroll, J., Li, D., You, J., Bronson, R., Yaffe, M. B., Zhou, J., Benjamin, T. (2007). TAZ Promotes PC2 Degradation through a SCF{beta}-Trcp E3 Ligase Complex. Mol. Cell. Biol. 27: 6383-6395 [Abstract] [Full Text]