Activation of Raf-1 is defective in annexin 6 overexpressing Chinese hamster ovary cells

FEBS Lett. 2001 Jul 13;501(1):69-73. doi: 10.1016/s0014-5793(01)02635-7.

Abstract

Annexin 6 is a Ca2+-dependent phospholipid-binding protein involved in membrane trafficking. In this study we demonstrate the association of Raf-1 with recombinant rat annexin 6. Raf-annexin 6 interaction was shown to be independent of cell activation by epidermal growth factor (EGF) or phorbol esters (12-O-tetradecanoyl-phorbol-13-acetate (TPA)). A stable Chinese hamster ovary (CHO)-anx6 cell line overexpressing annexin 6 was established to examine the function of annexin 6. In these cells, no increase of Ras-GTP levels, induced by EGF or TPA, was detected. In addition, the activity of Raf was completely inhibited, whereas the mitogen-activated protein kinase-P was unaffected.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Annexin A6 / genetics
  • Annexin A6 / metabolism*
  • CHO Cells
  • Cricetinae
  • Enzyme Activation / drug effects
  • Epidermal Growth Factor / pharmacology
  • Guanosine Triphosphate / metabolism
  • Mitogen-Activated Protein Kinases / metabolism
  • Protein Binding / drug effects
  • Proto-Oncogene Proteins c-raf / antagonists & inhibitors*
  • Proto-Oncogene Proteins c-raf / metabolism*
  • Rats
  • Recombinant Fusion Proteins / metabolism
  • Signal Transduction / drug effects
  • Tetradecanoylphorbol Acetate / pharmacology
  • Transfection
  • ras Proteins / metabolism

Substances

  • Annexin A6
  • Recombinant Fusion Proteins
  • Epidermal Growth Factor
  • Guanosine Triphosphate
  • Proto-Oncogene Proteins c-raf
  • Mitogen-Activated Protein Kinases
  • ras Proteins
  • Tetradecanoylphorbol Acetate