Focal adhesion kinase: exploring Fak structure to gain insight into function

Int Rev Cell Mol Biol. 2011:288:185-225. doi: 10.1016/B978-0-12-386041-5.00005-4.

Abstract

Focal adhesion kinase (FAK) and proline-rich tyrosine kinase 2 (Pyk2) are closely related nonreceptor protein tyrosine kinases. FAK can regulate cell proliferation, survival, and motility, and plays an essential role in development. Pyk2 shares some functions with FAK but is a nonessential gene product during development. Recent discoveries related to FAK and Pyk2 structure have provided important insights into the regulatory mechanisms of catalytic activity, molecular basis of assembly of signaling complexes, and the transmission of downstream signals. This chapter reviews these advances in FAK/Pyk2 structure/function, compares and contrasts features of these kinases, and discusses new drug discoveries in the context of molecular structure.

Publication types

  • Review

MeSH terms

  • Animals
  • Biosensing Techniques
  • Drug Design
  • Enzyme Activation
  • Enzyme Inhibitors / therapeutic use
  • Focal Adhesion Kinase 2 / antagonists & inhibitors
  • Focal Adhesion Kinase 2 / chemistry
  • Focal Adhesion Kinase 2 / physiology
  • Focal Adhesion Protein-Tyrosine Kinases / antagonists & inhibitors
  • Focal Adhesion Protein-Tyrosine Kinases / chemistry*
  • Focal Adhesion Protein-Tyrosine Kinases / physiology*
  • Humans
  • Models, Molecular
  • Neoplasms / enzymology
  • Protein Conformation*
  • Signal Transduction / physiology

Substances

  • Enzyme Inhibitors
  • Focal Adhesion Kinase 2
  • Focal Adhesion Protein-Tyrosine Kinases