Switching on kinases: oncogenic activation of BRAF and the PDGFR family

Nat Rev Cancer. 2004 Sep;4(9):718-27. doi: 10.1038/nrc1434.


The cytoplasmic serine/threonine kinase BRAF and receptor tyrosine kinases of the platelet-derived growth factor receptor (PDGFR) family are frequently activated in cancer by mutations of an equivalent amino acid. Structural studies have provided important insights into why these very different kinases share similar oncogenic hot spots and why the PDGFR juxtamembrane region is also a frequent oncogenic target. This research has implications for other kinases that are mutated in human tumours and for the treatment of cancer using kinase inhibitors.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cell Transformation, Neoplastic
  • Enzyme Inhibitors / pharmacology
  • Gene Expression Regulation, Neoplastic*
  • Humans
  • Molecular Sequence Data
  • Mutation
  • Neoplasms / genetics
  • Neoplasms / physiopathology
  • Oncogenes
  • Phosphotransferases / antagonists & inhibitors
  • Phosphotransferases / pharmacology
  • Proto-Oncogene Proteins B-raf
  • Proto-Oncogene Proteins c-raf / biosynthesis*
  • Proto-Oncogene Proteins c-raf / genetics*
  • Receptors, Platelet-Derived Growth Factor / biosynthesis*
  • Receptors, Platelet-Derived Growth Factor / genetics*


  • Enzyme Inhibitors
  • Phosphotransferases
  • Receptors, Platelet-Derived Growth Factor
  • BRAF protein, human
  • Proto-Oncogene Proteins B-raf
  • Proto-Oncogene Proteins c-raf