Strategies for the identification of kinase substrates using analog-sensitive kinases

Eur J Cell Biol. Feb-Mar 2010;89(2-3):184-93. doi: 10.1016/j.ejcb.2009.11.024. Epub 2010 Jan 12.

Abstract

Phosphorylation of proteins is a prevalent post-translational modification, which affects intracellular signaling in many ways. About 2% of all eukaryotic genes code for protein kinases catalyzing phosphorylation events. Despite technological advances that have made it possible to identify thousands of phosphorylation sites simultaneously, identification of the substrates of a given kinase remains an exceptionally challenging task. Here, we summarize approaches for substrate identification that make use of genetically engineered 'analog-sensitive' kinases.

Publication types

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

MeSH terms

  • Adenosine Triphosphate / analogs & derivatives
  • Adenosine Triphosphate / chemistry
  • Adenosine Triphosphate / metabolism
  • Affinity Labels / chemistry
  • Affinity Labels / metabolism
  • Biological Assay / methods*
  • Molecular Structure
  • Phosphorylation
  • Protein Conformation
  • Protein Engineering
  • Protein Kinases / genetics
  • Protein Kinases / metabolism*
  • Protein Processing, Post-Translational*
  • Signal Transduction / physiology
  • Substrate Specificity*

Substances

  • Affinity Labels
  • adenosine 5'-O-(3-thiotriphosphate)
  • Adenosine Triphosphate
  • Protein Kinases