Sapkota, G P

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