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]
Producer: 20010726Description: 19469-82 p. digitalISSN:- 0021-9258
- 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
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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