An unexpected journey: lysine methylation across the proteome

Biochim Biophys Acta. 2014 Dec;1839(12):1395-403. doi: 10.1016/j.bbagrm.2014.02.008. Epub 2014 Feb 20.

Abstract

The dynamic modification of histone proteins by lysine methylation has emerged over the last decade as a key regulator of chromatin functions. In contrast, our understanding of the biological roles for lysine methylation of non-histone proteins has progressed more slowly. Though recently it has attracted less attention, ε-methyl-lysine in non-histone proteins was first observed over 50 years ago. In that time, it has become clear that, like the case for histones, non-histone methylation represents a key and common signaling process within the cell. Recent work suggests that non-histone methylation occurs on hundreds of proteins found in both the nucleus and the cytoplasm, and with important biomedical implications. Technological advances that allow us to identify lysine methylation on a proteomic scale are opening new avenues in the non-histone methylation field, which is poised for dramatic growth. Here, we review historical and recent findings in non-histone lysine methylation signaling, highlight new methods that are expanding opportunities in the field, and discuss outstanding questions and future challenges about the role of this fundamental post-translational modification (PTM).

Keywords: Lysine methylation; Methylation signaling; Non-histone methylation; Post-translational modification; Proteome-wide.

Publication types

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

MeSH terms

  • Animals
  • Histone Methyltransferases
  • Histone-Lysine N-Methyltransferase / metabolism*
  • Histones / metabolism*
  • Humans
  • Lysine / metabolism*
  • Methylation
  • Protein Processing, Post-Translational*
  • Proteome / metabolism*

Substances

  • Histones
  • Proteome
  • Histone Methyltransferases
  • Histone-Lysine N-Methyltransferase
  • Lysine