Phosphorylation of the CD20 phosphoprotein in resting B lymphocytes. Regulation by protein kinase C

• Published in: The Journal of biological chemistry Vol. 264; no. 19; pp. 11282 - 11287
• Main Authors: VALENTINE, M. A, MEIER, K. E, ROSSIE, S, CLARK, E. A
• Format: Journal Article
• Language: English
• Published: Bethesda, MD American Society for Biochemistry and Molecular Biology 05.07.1989
• Subjects: 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine; Analytical, structural and metabolic biochemistry; Antigens, CD20; Antigens, Differentiation, B-Lymphocyte; B-Lymphocytes - immunology; B-Lymphocytes - metabolism; Biological and medical sciences; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Humans; Immunoglobulin M - immunology; Isoquinolines - pharmacology; Lymphocyte Activation; Peptide Fragments - metabolism; Phosphorylation; Piperazines - pharmacology; Protein Kinase C - antagonists & inhibitors; Protein Kinase C - metabolism; Protein Kinase Inhibitors; Receptors, Antigen, B-Cell - immunology; Sulfonamides - pharmacology; Tetradecanoylphorbol Acetate - pharmacology; Transferases; Trypsin; Human; Phosphorylation; Protein kinase C; Radiolabelling; Gel electrophoresis; Enzyme inhibitor; B-Lymphocyte; Chromatography; Proteins; Immunoprecipitation reaction; Phosphoproteins; Protein kinase; Substrate specificity; Immunofluorescence

CD20, a B cell integral membrane protein, regulates B cell activation and is differently phosphorylated in resting and activated cells. We have previously shown that CD20 phosphorylation is increased in activated cells and in phorbol ester-treated resting cells. Phosphorylation is also altered by ag...