Article
A point mutation at the putative ATP-binding site of protein kinase C alpha abolishes the kinase activity and renders it down-regulation-insensitive. A molecular link between autophosphorylation and down-regulation.
The Journal of biological chemistry - 15 Apr 1990
Ohno S, Konno Y, Akita Y, Yano A, Suzuki K
Abstract excerpt
A protein kinase C alpha (PKC alpha) cDNA confers increased phorbol ester binding activity to intact cells when transiently expressed in COS cells or expressed stably in transfected rat 3Y1 fibroblasts. A point mutant (PKC alpha K----R) of PKC alpha, where Lys368 at the putative ATP-binding site...
Topics
- Adenosine Triphosphate
- Animals
- Base Sequence
- Cell Line
- Cytosol
- DNA
- Genetic Vectors
- Homeostasis
- Molecular Sequence Data
- Mutation
- Oligonucleotide Probes
- Phorbol 12,13-Dibutyrate
- Phosphorylation
- Plasmids
- Protein Kinase C
- Rats
- Subcellular Fractions
- Tetradecanoylphorbol Acetate