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Cell cycle-dependent acetylation of Rb2/p130 in NIH3T3 cells

F Schwarze1, J Meraner, M Lechner

  • 1Division of Molecular Biology, Biocenter, Innsbruck Medical University, Innsbruck, Austria.

Oncogene
|August 3, 2010
PubMed

Insights

Acetylation modifies the cell cycle regulator retinoblastoma protein 2 (Rb2)/p130, impacting its nuclear function. This acetylation is cell cycle-dependent and influenced by human papilloma virus 16 E7 protein.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Pocket proteins, including retinoblastoma protein (pRb) and its relatives p130 and p107, are key regulators of the cell cycle.
  • Their function is modulated by phosphorylation and, for pRb, also by acetylation.
  • The role of acetylation in p130 regulation remains less understood.

Purpose of the Study:

  • To investigate the acetylation of retinoblastoma 2 (Rb2)/p130.
  • To determine the cell cycle-dependency and localization of acetylated p130.
  • To identify the specific acetylation sites on p130 and assess the impact of HPV16 E7 protein.

Main Methods:

  • Western blotting to detect acetylated p130 in NIH3T3 cells.
  • In vitro acetylation assays using recombinant p130 and p300.
  • Mass spectrometry to identify acetylation sites.
  • Analysis of HPV16 E7 protein interaction with p130.

Main Results:

  • Hyperphosphorylated Rb2/p130 is acetylated in NIH3T3 cells, localized to the nucleus.
  • Acetylation occurs during the S to G2 phases of the cell cycle.
  • K1079 in the C-terminus is the major acetylation site, with minor sites in the N- and C-termini.
  • Human papilloma virus 16 E7 protein binds preferentially to acetylated p130 and enhances its acetylation.

Conclusions:

  • Acetylation is a novel regulatory mechanism for Rb2/p130 during the cell cycle.
  • Specific acetylation sites on p130 are identified.
  • HPV16 E7 interaction suggests a role for p130 acetylation in viral oncogenesis.

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