title: Dichotomy in the Epigenetic Mark Lysine Acetylation is Critical for the Proliferation of Prostate Cancer Cells.
abstract: The dynamics of lysine acetylation serve as a major epigenetic mark, which regulates cellular response to inflammation, DNA damage and hormonal changes. Microarray assays reveal changes in gene expression, but cannot predict regulation of a protein function by epigenetic modifications. The present study employs computational tools to inclusively analyze microarray data to understand the potential role of acetylation during development of androgen-independent PCa. The data revealed that the androgen receptor interacts with 333 proteins, out of which at least 92 proteins were acetylated. Notably, the number of cellular proteins undergoing acetylation in the androgen-dependent PCa was more as compared to the androgen-independent PCa. Specifically, the 32 lysine-acetylated proteins in the cellular models of androgen-dependent PCa were mainly involved in regulating stability as well as pre- and post-processing of mRNA. Collectively, the data demonstrate that protein lysine acetylation plays a crucial role during the transition of androgen-dependent to -independent PCa, which importantly, could also serve as a functional axis to unravel new therapeutic targets.
authors: Department of Structural and Chemical Biology, Mount Sinai School of Medicine, 1425 Madison Ave, New York, NY 10029, USA. ravipathak@aol.in.
authors: Ravi
authors: R
authors: Pathak
authors: Medgar Evers College, City University of New York, 1638 Bedford Ave, 403D, Brooklyn, NY 11225, USA. marc.philizaire@student.mec.cuny.edu.
authors: Marc
authors: M
authors: Philizaire
authors: Department of Structural and Chemical Biology, Mount Sinai School of Medicine, 1425 Madison Ave, New York, NY 10029, USA. smujtaba@mec.cuny.edu.|Medgar Evers College, City University of New York, 1638 Bedford Ave, 403D, Brooklyn, NY 11225, USA. smujtaba@mec.cuny.edu.
authors: Shiraz
authors: S
authors: Mujtaba
keywords: androgen; androgen receptor; deacetylation and molecular interactions; lysine acetylation; prostate cancer