Linking the kinome and phosphorylome--a comprehensive review of approaches to find kinase targets

Mol Biosyst. 2008 Sep;4(9):920-33. doi: 10.1039/b801724g. Epub 2008 Jul 17.


Protein phosphorylation is associated with most cell signaling and developmental processes in eukaryotes. Despite the vast extent of the phosphoproteome within the cell, connecting specific kinases with relevant targets remains a significant experimental frontier. The challenge of linking kinases and their substrates reflects the complexity of kinase function. For example, kinases tend to exert their biological effects through supernumerary, redundant phosphorylation, often on multiple protein complex components. Although these types of phosphorylation events are biologically significant, those kinases responsible are often difficult to identify. Recent methods for global analysis of protein phosphorylation promise to substantially accelerate efforts to map the dynamic phosphorylome. Here, we review both conventional methods to identify kinase targets and more comprehensive genomic and proteomic approaches to connect the kinome and phosphorylome.

Publication types

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

MeSH terms

  • Animals
  • Enzyme Inhibitors / chemistry
  • Humans
  • Mass Spectrometry
  • Models, Biological
  • Phosphorylation
  • Protein Kinases / chemistry*
  • Protein Kinases / genetics
  • Protein Kinases / isolation & purification
  • Proteomics
  • RNA Interference
  • Signal Transduction
  • Substrate Specificity
  • Two-Hybrid System Techniques


  • Enzyme Inhibitors
  • Protein Kinases