Is there a code embedded in proteins that is based on post-translational modifications?

Nat Rev Mol Cell Biol. 2008 Oct;9(10):815-20. doi: 10.1038/nrm2502. Epub 2008 Sep 11.

Abstract

Covalent post-translational modifications (PTMs) provide vast indexing potential and expanded protein use. The 'histone code' hypothesis has inspired rapid advances throughout chromatin biology, and has recently been tapped for its relevance to non-histone proteins. Comprehensive analyses suggest that rather than constituting a general code, the covalent modifications of proteins (including histones) provide surfaces that are recognized by effectors that can give rise to intricate interactions and downstream events. These are reminiscent of other regulatory cascades in transcription and cell signalling.

Publication types

  • Review

MeSH terms

  • Animals
  • Histones / chemistry
  • Histones / genetics
  • Histones / metabolism
  • Humans
  • Methylation
  • Models, Biological
  • Phosphorylation
  • Protein Processing, Post-Translational*
  • Proteins / chemistry*
  • Proteins / genetics
  • Proteins / metabolism*
  • Transcription, Genetic
  • Tumor Suppressor Protein p53 / chemistry
  • Tumor Suppressor Protein p53 / genetics
  • Tumor Suppressor Protein p53 / metabolism

Substances

  • Histones
  • Proteins
  • Tumor Suppressor Protein p53