Unit

UNIT 24.8 Global Proteomics Analysis of Protein Lysine Methylation

  1. Xing-Jun Cao,
  2. Benjamin A. Garcia

Published Online: 1 NOV 2016

DOI: 10.1002/cpps.16

Current Protocols in Protein Science

Current Protocols in Protein Science

How to Cite

Cao, X.-J. and Garcia, B.A. 2016. Global proteomics analysis of protein lysine methylation. Curr. Protoc. Protein Sci. 86:24.8.1-24.8.19. doi: 10.1002/cpps.16

Author Information

  1. Epigenetics Program, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania

Publication History

  1. Published Online: 1 NOV 2016

Abstract

Lysine methylation is a common protein post-translational modification dynamically mediated by protein lysine methyltransferases (PKMTs) and protein lysine demethylases (PKDMs). Beyond histone proteins, lysine methylation on non-histone proteins plays a substantial role in a variety of functions in cells and is closely associated with diseases such as cancer. A large body of evidence indicates that the dysregulation of some PKMTs leads to tumorigenesis via their non-histone substrates. However, most studies on other PKMTs have made slow progress owing to the lack of approaches for extensive screening of lysine methylation sites. However, recently, there has been a series of publications to perform large-scale analysis of protein lysine methylation. In this unit, we introduce a protocol for the global analysis of protein lysine methylation in cells by means of immunoaffinity enrichment and mass spectrometry. © 2016 by John Wiley & Sons, Inc.

Keywords:

  • immunoaffinity enrichment;
  • methylation;
  • mass spectrometry;
  • non-histone;
  • post-translational modification;
  • proteomics