Adenylylation: renaissance of a forgotten post-translational modification

Trends Biochem Sci. 2011 Apr;36(4):221-8. doi: 10.1016/j.tibs.2010.12.004. Epub 2011 Jan 20.

Abstract

The stable post-translational modification of proteins by adenylylation or uridylylation was discovered more than four decades ago as a mechanism to regulate the activity of enzymes. Although many other processes involving the covalent transfer of an AMP residue to an amino acid side chain have been identified since then, these are transient adenylylation events that essentially use the free energy of ATP hydrolysis to activate specific processes. Recently, new examples of stable adenylylation of small GTPases involved in signal transduction and regulation of cellular events were discovered, which appear to modulate downstream processes such as cytoskeletal rearrangement and vesicular trafficking. We present a survey of the historical and modern phases of research in this area, focusing on the common and differing aspects of protein adenylylation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adenine / chemistry
  • Adenine / metabolism*
  • Adenosine Monophosphate / metabolism
  • Animals
  • Glutamate Synthase / chemistry
  • Glutamate Synthase / metabolism
  • Humans
  • Protein Processing, Post-Translational*
  • Proteins / metabolism

Substances

  • Proteins
  • Adenosine Monophosphate
  • Glutamate Synthase
  • Adenine