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Inhibition of Bak-induced apoptosis by HPV-18 E6

M Thomas1, L Banks

  • 1International Centre for Genetic Engineering and Biotechnology, Trieste, Italy.

Oncogene
|January 9, 1999
PubMed

Insights

Human papillomavirus (HPV) E6 protein targets Bak protein for degradation, inhibiting apoptosis. This interaction reveals Bak as a novel E6AP target, impacting cellular processes.

Area of Science:

  • Molecular Biology
  • Virology
  • Cellular Biology

Background:

  • Human papillomavirus (HPV) E6 proteins are known to inhibit apoptosis through p53-dependent and independent pathways.
  • The Bcl-2 family regulates apoptosis, with Bak protein highly expressed in differentiating keratinocytes where HPV replicates.

Purpose of the Study:

  • To investigate the mechanism by which HPV-18 E6 inhibits Bak-induced apoptosis.
  • To identify the interaction between HPV-18 E6 and Bak proteins.
  • To determine if Bak is a natural substrate for the ubiquitin ligase E6AP.

Main Methods:

  • Investigated the interaction between HPV-18 E6 and Bak proteins.
  • Assessed the degradation of Bak protein in vivo.
  • Examined the interaction of Bak protein with the ubiquitin ligase E6AP using wild-type and mutant Bak.

Main Results:

  • HPV-18 E6 inhibits Bak-induced apoptosis via a direct interaction with Bak.
  • This interaction leads to the in vivo degradation of Bak protein.
  • Bak protein interacts with E6AP, and a Bak mutant defective in E6AP binding shows increased expression compared to wild type.

Conclusions:

  • HPV-18 E6 targets and degrades Bak protein, thereby inhibiting apoptosis.
  • Bak is identified as a natural substrate for the ubiquitin ligase E6AP.
  • These findings elucidate a novel mechanism of viral oncoprotein-mediated apoptosis evasion.

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