Histone methylation modifiers in cellular signaling pathways

Cell Mol Life Sci. 2015 Dec;72(23):4577-92. doi: 10.1007/s00018-015-2023-y. Epub 2015 Aug 25.

Abstract

Histone methyltransferases and demethylases epigenetically regulate gene expression by modifying histone methylation status in numerous cellular processes, including cell differentiation and proliferation. These modifiers also control methylation levels of various non-histone proteins, such as effector proteins that play critical roles in cellular signaling networks. Dysregulated histone methylation modifiers alter expression of oncogenes and tumor suppressor genes and change methylation states of effector proteins, frequently resulting in aberrant cellular signaling cascades and cellular transformation. In this review, we summarize the role of histone methylation modifiers in regulating the following signaling pathways: NF-κB, RAS/RAF/MEK/MAPK, PI3K/Akt, Wnt/β-catenin, p53, and ERα.

Keywords: Histone demethylase; Histone methylation; Histone methyltransferase; Oncogenic signaling; Tumor suppressor pathway.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Arginine / metabolism
  • Histone Methyltransferases
  • Histone-Lysine N-Methyltransferase / chemistry
  • Histone-Lysine N-Methyltransferase / metabolism*
  • Histones / metabolism*
  • Humans
  • Lysine / metabolism
  • MAP Kinase Signaling System
  • Methylation
  • Molecular Sequence Data
  • NF-kappa B / metabolism*
  • Phosphatidylinositol 3-Kinases / metabolism
  • Proto-Oncogene Proteins c-akt / metabolism
  • Proto-Oncogene Proteins c-raf / metabolism
  • Signal Transduction
  • Wnt Signaling Pathway*

Substances

  • Histones
  • NF-kappa B
  • Arginine
  • Histone Methyltransferases
  • Histone-Lysine N-Methyltransferase
  • SMYD3 protein, human
  • Phosphatidylinositol 3-Kinases
  • Proto-Oncogene Proteins c-akt
  • Proto-Oncogene Proteins c-raf
  • Lysine