Phosphorylation of the protein kinase mutated in Peutz-Jeghers cancer syndrome, LKB1/STK11, at Ser431 by p90(RSK) and cAMP-dependent protein kinase, but not its farnesylation at Cys(433), is essential for LKB1 to suppress cell vrowth. [electronic resource]
- The Journal of biological chemistry Jun 2001
- 19469-82 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0021-9258
10.1074/jbc.M009953200 doi
AMP-Activated Protein Kinase Kinases AMP-Activated Protein Kinases Animals Binding Sites Calcium-Calmodulin-Dependent Protein Kinases--metabolism Cell Division Cell Line Cloning, Molecular Colforsin--pharmacology Cyclic AMP--metabolism Cyclic AMP-Dependent Protein Kinases--metabolism Cysteine--chemistry Enzyme Activation Enzyme Inhibitors--pharmacology Epidermal Growth Factor--metabolism Glutathione Transferase--metabolism Humans Immunoblotting Isoquinolines--pharmacology Mevalonic Acid--pharmacology Mice Models, Biological Mutation Peutz-Jeghers Syndrome--genetics Phosphorylation Precipitin Tests Protein Prenylation Protein Serine-Threonine Kinases--genetics Rats Ribosomal Protein S6 Kinases--metabolism Ribosomal Protein S6 Kinases, 90-kDa Serine--chemistry Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Sulfonamides Time Factors Transfection