Structure and regulation of the c-Fes protein-tyrosine kinase

Front Biosci (Landmark Ed). 2011 Jun 1;16:3146-55. doi: 10.2741/3902.

Abstract

The c-Fes protein-tyrosine kinase is the normal cellular ortholog of several avian and feline retroviral oncoproteins. Unlike its transforming viral counterparts, c-Fes tyrosine kinase activity is tightly regulated in vivo through a mechanism involving coiled-coil oligomerization domains and other unique structural features found in its long N-terminal region. This review is focused on the regulatory features and structural biology of c-Fes, which has been implicated in normal cellular growth regulation, the innate immune response, and tumorigenesis.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Antibodies
  • Bone Marrow Cells / enzymology
  • Cell Transformation, Neoplastic
  • Cell Transformation, Viral
  • Fusion Proteins, gag-onc / immunology
  • Humans
  • Oncogenes
  • Protein Structure, Tertiary
  • Proto-Oncogene Proteins c-fes / chemistry
  • Proto-Oncogene Proteins c-fes / genetics*
  • Proto-Oncogene Proteins c-fes / metabolism*

Substances

  • Antibodies
  • Fusion Proteins, gag-onc
  • Proto-Oncogene Proteins c-fes