Wild-type p53 mediates apoptosis by E1A, which is inhibited by E1B.

No physical interaction between the E1B 19K and p53 proteins has been reported, the results presented here indicate that this possibility should be placed under closer scrutiny

M Debbas; E White

2007

Scholarcy highlights

  • The E1A gene products interact with and perturb the function of key regulators of cell growth, such as the retinoblastoma protein {Whyte et al 1988} and cyclin A
  • The E1B 19K protein was originally identified as an inhibitor of DNA fragmentation and cell death in human cells productively infected with adenovirus
  • Because DNA fragmentation is an indicator of cell death by apoptosis, E1A was thought to induce apoptosis and the E1B 19K protein was believed to function as an inhibitor of apoptosis
  • The mechanism by which the E1B 19K protein functions to suppress apoptosis was not known, the ability of the E1B 55K protein to do so suggested the involvement of p53
  • The amino terminus of E1A is required for induction of cellular DNA synthesis, enhancer repression, and transformation, but which of these activities is related to apoptosis remains to be determined
  • The PDdl mutation in E1A, can be distinguished from the other E1A mutants examined because it produces a mutant protein that is completely defective for induction of cellular DNA synthesis
  • The 19-kilodalton adenovirus E1B transforming protein inhibits programmed cell death and prevents cytolysis by tumor neclosis factor cx

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