Reading protein modifications with interaction domains

Nat Rev Mol Cell Biol. 2006 Jul;7(7):473-83. doi: 10.1038/nrm1960.


Proteins are controlled by a vast and dynamic array of post-translational modifications, many of which create binding sites for specific protein-interaction domains. We propose that these domains, working together, read the state of the proteome and therefore couple post-translational modifications to cellular organization. We also identify common strategies through which modification-dependent interactions synergize to regulate cell behaviour.

Publication types

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

MeSH terms

  • Amino Acid Motifs
  • Cell Physiological Phenomena
  • Models, Molecular
  • Molecular Structure
  • Protein Binding
  • Protein Conformation*
  • Protein Processing, Post-Translational*
  • Proteins / chemistry*
  • Proteins / genetics
  • Proteins / metabolism*


  • Proteins