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Ad E1A 243R oncoprotein promotes association of proto-oncogene product MYC with the NuA4/Tip60 complex via the E1A

Ling-Jun Zhao1, Paul M Loewenstein1, Maurice Green1

  • 1Department of Microbiology and Molecular Immunology/Institute for Molecular Virology, Saint Louis University School of Medicine, Doisy Research Center, St. Louis, MO 63104, USA.

Virology
|September 25, 2016
PubMed

Insights

Adenovirus E1A oncoprotein interacts with the NuA4 complex, including TRRAP and Tip60, to influence MYC activity. This interaction is crucial for cellular transformation mediated by both E1A and MYC.

Area of Science:

  • Molecular Biology
  • Oncology
  • Virology

Background:

  • Adenovirus E1A oncoprotein targets TRRAP, a scaffold protein for histone acetyltransferase (HAT) complexes.
  • The NuA4/Tip60 complex, involving TRRAP, regulates the proto-oncogene MYC and cancer cell phenotype.
  • The mechanism of E1A-mediated cellular transformation via TRRAP is not fully understood.

Purpose of the Study:

  • To investigate the interaction between adenovirus E1A 243R oncoprotein and the NuA4/Tip60 complex.
  • To elucidate the role of the E1A TRRAP-targeting domain in these interactions.
  • To understand the implications for cellular transformation.

Main Methods:

  • Proteomic analysis of the E1A 1-80 N-terminal transcriptional repression domain.
  • Co-immunoprecipitation assays.
  • Analysis of protein associations with DMAP1, Tip60, and MYC.

Main Results:

  • Identified novel interactions between E1A 1-80 and NuA4 components (TRRAP, p400, DMAP1, RUVBL1, RUVBL2).
  • Confirmed E1A 243R association with the NuA4 complex.
  • Demonstrated that E1A 243R promotes MYC/MAX association with the NuA4/Tip60 complex.

Conclusions:

  • Adenovirus E1A 243R directly interacts with multiple NuA4 complex members.
  • E1A utilizes its TRRAP-targeting domain to engage with NuA4 components and MYC.
  • The MYC/NuA4 pathway is implicated in cellular transformation driven by both E1A and MYC.
Keywords:
243RDMAP1E1A 1-80NuA4RUVBL1RUVBL2TRRAPTip60

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