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USP11 Stabilizes HPV-1 6E7 and Further Modulates the E7 Biological Activity.

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Title: USP11 Stabilizes HPV-1 6E7 and Further Modulates the E7 Biological Activity.
Authors: Ching-Hui Lin1, Hung-Shu Chang2, Yu, Winston C. V.2 winston@nhri.org.tw
Source: Journal of Biological Chemistry. 6/6/2008, Vol. 283 Issue 23, p15681-15688. 8p. 6 Graphs.
Subjects: Cervical cancer, Cell transformation, Ubiquitin, Proteins, Proteolytic enzymes, Biochemistry
Abstract: HPV-16E7 is a major transforming protein, which has been implicated in the development of cervical cancer. The stability of E7 is thus important to ensure its fully functional status. Using the yeast two-hybrid system, we found that USP11 (ubiq-uitin-specific protease 11), a member of a protein family that cleaves polyubiquitin chains and/or ubiquitin precursors, inter- acts and forms a specific complex with HPV-16E7. Our results indicate that the USP11 can greatly increase the steady state level of HPV-16E7 by reducing ubiquitination and attenuating E7 degradation. In contrast, a catalytically inactive mutant of USP11 abolished the deubiquitinating ability and returned E7 to a normal rate of degradation. Moreover, USP11 not only protected E7 from ubiquitination but also influenced E7 function as a modulator of cell growth status. These results suggest that USP11 plays an important role in regulating the levels of E7 protein and subsequently affects the biological function of E7 as well as its contribution to cell transformation by HPV-16E7. [ABSTRACT FROM AUTHOR]
Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
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  Data: USP11 Stabilizes HPV-1 6E7 and Further Modulates the E7 Biological Activity.
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  Data: <searchLink fieldCode="AR" term="%22Ching-Hui+Lin%22">Ching-Hui Lin</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Hung-Shu+Chang%22">Hung-Shu Chang</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Yu%2C+Winston+C%2E+V%2E%22">Yu, Winston C. V.</searchLink><relatesTo>2</relatesTo><i> winston@nhri.org.tw</i>
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+Biological+Chemistry%22">Journal of Biological Chemistry</searchLink>. 6/6/2008, Vol. 283 Issue 23, p15681-15688. 8p. 6 Graphs.
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  Data: <searchLink fieldCode="DE" term="%22Cervical+cancer%22">Cervical cancer</searchLink><br /><searchLink fieldCode="DE" term="%22Cell+transformation%22">Cell transformation</searchLink><br /><searchLink fieldCode="DE" term="%22Ubiquitin%22">Ubiquitin</searchLink><br /><searchLink fieldCode="DE" term="%22Proteins%22">Proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Proteolytic+enzymes%22">Proteolytic enzymes</searchLink><br /><searchLink fieldCode="DE" term="%22Biochemistry%22">Biochemistry</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: HPV-16E7 is a major transforming protein, which has been implicated in the development of cervical cancer. The stability of E7 is thus important to ensure its fully functional status. Using the yeast two-hybrid system, we found that USP11 (ubiq-uitin-specific protease 11), a member of a protein family that cleaves polyubiquitin chains and/or ubiquitin precursors, inter- acts and forms a specific complex with HPV-16E7. Our results indicate that the USP11 can greatly increase the steady state level of HPV-16E7 by reducing ubiquitination and attenuating E7 degradation. In contrast, a catalytically inactive mutant of USP11 abolished the deubiquitinating ability and returned E7 to a normal rate of degradation. Moreover, USP11 not only protected E7 from ubiquitination but also influenced E7 function as a modulator of cell growth status. These results suggest that USP11 plays an important role in regulating the levels of E7 protein and subsequently affects the biological function of E7 as well as its contribution to cell transformation by HPV-16E7. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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      – Type: doi
        Value: 10.1074/jbc.M708278200
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      – Code: eng
        Text: English
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        PageCount: 8
        StartPage: 15681
    Subjects:
      – SubjectFull: Cervical cancer
        Type: general
      – SubjectFull: Cell transformation
        Type: general
      – SubjectFull: Ubiquitin
        Type: general
      – SubjectFull: Proteins
        Type: general
      – SubjectFull: Proteolytic enzymes
        Type: general
      – SubjectFull: Biochemistry
        Type: general
    Titles:
      – TitleFull: USP11 Stabilizes HPV-1 6E7 and Further Modulates the E7 Biological Activity.
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            NameFull: Ching-Hui Lin
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            NameFull: Hung-Shu Chang
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            NameFull: Yu, Winston C. V.
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            – D: 06
              M: 06
              Text: 6/6/2008
              Type: published
              Y: 2008
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