Toward Understanding Molecular Recognition between PRMTs and their Substrates

Curr Protein Pept Sci. 2020;21(7):713-724. doi: 10.2174/1389203721666200124143145.

Abstract

Protein arginine methylation is a widespread eukaryotic posttranslational modification that occurs with as much frequency as ubiquitinylation. Yet, how the nine different human protein arginine methyltransferases (PRMTs) recognize their respective protein targets is not well understood. This review summarizes the progress that has been made over the last decade or more to resolve this significant biochemical question. A multipronged approach involving structural biology, substrate profiling, bioorthogonal chemistry and proteomics is discussed.

Keywords: PRMT; PRMT molecular recognition; arginine methylation; arginine methylome; substrate specificity; target recognition.

Publication types

  • Review

MeSH terms

  • Animals
  • Arginine / metabolism*
  • Epigenesis, Genetic
  • Histones / genetics
  • Histones / metabolism
  • Humans
  • Isoenzymes / chemistry
  • Isoenzymes / classification
  • Isoenzymes / genetics
  • Isoenzymes / metabolism
  • Methylation
  • Models, Molecular
  • Peptides / chemistry*
  • Peptides / metabolism
  • Protein Interaction Domains and Motifs
  • Protein Processing, Post-Translational*
  • Protein Structure, Secondary
  • Protein-Arginine N-Methyltransferases / chemistry
  • Protein-Arginine N-Methyltransferases / classification
  • Protein-Arginine N-Methyltransferases / genetics
  • Protein-Arginine N-Methyltransferases / metabolism*
  • Proteomics / methods
  • Signal Transduction
  • Substrate Specificity

Substances

  • Histones
  • Isoenzymes
  • Peptides
  • Arginine
  • Protein-Arginine N-Methyltransferases