Brefeldin A inhibits protein synthesis through the phosphorylation of the alpha-subunit of eukaryotic initiation factor-2.
Brefeldin A is a fungal metabolite which disrupts protein traffic through the Golgi apparatus and thereby inhibits protein secretion. Recently, it has been shown that Brefeldin A also causes a marked decrease in the rate of protein synthesis in cells in culture [1992, FEBS Lett. 314, 371-374]. We show here that treatment of rat GH3 pituitary cells with Brefeldin A leads to an inhibition of protein synthesis at the level of peptide-chain initiation through a mechanism involving the phosphorylation of the alpha-subunit of eukaryotic initiation factor-2 (eIF-2 alpha).
Mellor
H
H
Department of Cellular and Molecular Physiology, College of Medicine, Pennsylvania State University, Hershey 17033.
Kimball
S R
SR
Jefferson
L S
LS
D000818:Animals; D015153:Blotting, Western; D020126:Brefeldin A; D003517:Cyclopentanes / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D015852:Eukaryotic Initiation Factor-2 / Q000737:chemistry / Q000378:metabolism*; D010442:Peptide Chain Initiation, Translational / Q000187:drug effects; D010766:Phosphorylation; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology*; D051381:Rats; D014407:Tumor Cells, Cultured
D003517:Cyclopentanes; D015852:Eukaryotic Initiation Factor-2; D011500:Protein Synthesis Inhibitors; D020126:Brefeldin A