Inhibition of Protein Phosphatase 2A (PP2A) Prevents Mcl-1 Protein Dephosphorylation at the Thr-163/Ser-159 Phosphodegron, Dramatically Reducing Expression in Mcl-1-amplified Lymphoma Cells - Nifoussi, Shanna K.; Ratcliffe, Nora R.; Ornstein, Deborah L.; Kasof, Gary; Strack, Stefan; Craig, Ruth W. (The Journal of biological chemistry, 2014)
Keywords: Binding Sites; Burkitt Lymphoma - drug therapy; Burkitt Lymphoma - genetics; Burkitt Lymphoma - metabolism; Cell Line, Tumor; Drug Resistance, Neoplasm; Enzyme Inhibitors - pharmacology; Gene Expression; Gene Knockdown Techniques; Humans; MAP Kinase Signaling System; Marine Toxins; Molecular Bases of Disease; Myeloid Cell Leukemia Sequence 1 Protein - chemistry; Myeloid Cell Leukemia Sequence 1 Protein - genetics; Myeloid Cell Leukemia Sequence 1 Protein - metabolism; Okadaic Acid - pharmacology; Oxazoles - pharmacology; Phosphorylation - drug effects; Protein Phosphatase 2 - antagonists & inhibitors; Protein Phosphatase 2 - genetics; Proteolysis; Serine - chemistry; Tetradecanoylphorbol Acetate - pharmacology; Threonine - chemistry; Mcl-1; B-cell Lymphoma 2 (Bcl-2) Family; Cell Death; Cancer; Extracellular Signal-regulated Kinase (ERK); Protein Phosphatase 2 (PP2A)