A 'molecular switchboard'--covalent modifications to proteins and their impact on transcription

Org Biomol Chem. 2004 Jan 7;2(1):1-7. doi: 10.1039/b312466e. Epub 2003 Dec 2.


Proteins undergo a remarkable variety of posttranslational modifications, with more than 200 distinct modifications identified to date. Increasing evidence suggests that many proteins bear multiple, distinct modifications, and the ability of one modification to antagonize or synergize the deposition of another can have significant biological consequences. Here, we illustrate the importance of posttranslational modifications within the context of transcriptional regulation, and we offer a perspective on the emerging role of combinatorial networks of modifications. Finally, we discuss the potential for chemical approaches to transform our understanding of the field.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cyclic AMP Response Element-Binding Protein / chemistry
  • Cyclic AMP Response Element-Binding Protein / physiology
  • Histones / chemistry
  • Molecular Sequence Data
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / metabolism*
  • Nuclear Proteins / physiology
  • Protein Conformation
  • Protein Processing, Post-Translational*
  • RNA Polymerase II / chemistry
  • Transcription, Genetic*
  • Tumor Suppressor Protein p53 / chemistry
  • Tumor Suppressor Protein p53 / physiology


  • Cyclic AMP Response Element-Binding Protein
  • Histones
  • Nuclear Proteins
  • Tumor Suppressor Protein p53
  • RNA Polymerase II