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Title: Physical and functional interactions of human papillomavirus E2 protein with nuclear receptor coactivators

Journal Article · · Biochemical and Biophysical Research Communications
 [1];  [2];  [3];  [1];  [4];  [5]
  1. Graduate Institute of Life Sciences, National Defense Medical Center, Taipei City 114, Taiwan (China)
  2. Molecular Genetics and Biochemistry Laboratory, Cathay Medical Research Institute, Cathay General Hospital, Taipei County 221, Taiwan (China)
  3. Department of Biochemistry, National Defense Medical Center, Taipei City 114, Taiwan (China)
  4. Division of Hematology/Oncology, Tri-Service General Hospital, National Defense Medical Center, Taipei City 114, Taiwan (China)
  5. Graduate Institute of Life Sciences, National Defense Medical Center, Taipei City 114, Taiwan (China) and Department of Biochemistry, National Defense Medical Center, Taipei City 114, Taiwan (China)

In addition to the human papillomavirus (HPV)-induced immortalization of epithelial cells, which usually requires integration of the viral DNA into the host cell genome, steroid hormone-activated nuclear receptors (NRs) are thought to bind to specific DNA sequences within transcriptional regulatory regions on the long control region to either increase or suppress transcription of dependent genes. In this study, our data suggest that the NR coactivator function of HPV E2 proteins might be mediated through physical and functional interactions with not only NRs but also the NR coactivators GRIP1 (glucocorticoid receptor-interacting protein 1) and Zac1 (zinc-finger protein which regulates apoptosis and cell cycle arrest 1), reciprocally regulating their transactivation activities. GRIP1 and Zac1 both were able to act synergistically with HPV E2 proteins on the E2-, androgen receptor-, and estrogen receptor-dependent transcriptional activation systems. GRIP1 and Zac1 might selectively function with HPV E2 proteins on thyroid receptor- and p53-dependent transcriptional activation, respectively. Hence, the transcriptional function of E2 might be mediated through NRs and NR coactivators to regulate E2-, NR-, and p53-dependent transcriptional activations.

OSTI ID:
20991329
Journal Information:
Biochemical and Biophysical Research Communications, Vol. 356, Issue 3; Other Information: DOI: 10.1016/j.bbrc.2007.02.162; PII: S0006-291X(07)00450-0; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
Country of Publication:
United States
Language:
English

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