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Human Papillomavirus 16 E6 Oncoprotein Interferences with Insulin Signaling Pathway by Binding to Tuberin

Lu, Zheming, Hu, Xiuhua, Li, Yong, Zheng, Li, Zhou, Yue, Jiang, Haidi, Ning, Tao, Basang, Zhuoma, Zhang, Chunfeng, Ke, Yang·2004·Journal of Biological Chemistry
DOI 10.1074/jbc.m403385200
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Abstract

Tuberous sclerosis complex (TSC) is a genetic disorder caused by mutations in either TSC1 or TSC2 tumor suppressor gene. TSC1 and TSC2 products, Harmatin and Tuberin, form the functional complex to serve as the negative regulator for insulin-induced phosphorylation of S6 kinase and elF4E-binding protein 1. High-risk human papillomavirus (HPV) infection is the necessary cause for cervical cancer. E6 oncoprotein encoded by HPV plays a pivotal role in carcinogenesis by interference with the host intracellular protein functions. In this study, we show that HPV16 E6 interacts with tumor suppressor gene TSC2 product, Tuberin, and results in the phosphorylation of S6 kinase and S6 even in the absence of insulin. The overexpression of Tuberin overcomes the effect of E6 on S6 kinase phosphorylation. Binding with HPV16 E6 causes the proteasome-mediated degradation of Tuberin. A DILG motif and an ELVG motif located in the carboxyl-terminal of Tuberin are required for E6 binding. In addition, the Tuberin interaction region in E6 has been mapped in the amino-terminal portion of HPV16 E6, which is different from the binding domain with p53. These results provide a possible link between E6-induced oncogenesis and the insulin-stimulated cell proliferation signaling pathway.

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Cited by

Metadata

Authors
Lu, Z., Hu, X., Li, Y., Zheng, L., Zhou, Y., Jiang, H., Ning, T., Basang, Z., Zhang, C., & Ke, Y.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2004-08
Volume
279
Issue
34
Pages
35664-35670
ISSN
0021-9258
DOI
10.1074/jbc.m403385200
Cited by
96
References
4
Language
en
Licence

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