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