Phosphorylation of P1, a high mobility group-like protein, catalyzed by casein kinase II, protein kinase C, cyclic AMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase II

• Published in: FEBS letters Vol. 258; no. 1; pp. 106 - 108
• Main Authors: Walaas, S.Ivar, C. Østvold, Anne, Laland, Søren G.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 20.11.1989; Elsevier
• Subjects: Adenosine Triphosphate - metabolism; Analytical, structural and metabolic biochemistry; Animals; Autoradiography; Biological and medical sciences; Brain - enzymology; Casein Kinases; Electrophoresis, Polyacrylamide Gel; Fundamental and applied biological sciences. Psychology; High Mobility Group Proteins - analysis; Holoproteins; liver; Liver - enzymology; Nuclear proteins; Peptide Mapping; Phosphoprotein; Phosphoproteins - biosynthesis; Phosphorylation; Protein kinase; Protein Kinase C - analysis; Protein Kinase C - metabolism; Protein Kinases - analysis; Protein Kinases - metabolism; Protein P1; Proteins; Rats; Ribosomal Proteins; Phosphoprotein; Protein P1; Protein kinase; Peptide mapping; Phosphorylation; Enzyme; Kinase; Analog; Electrophoretic mobility; In vitro; Nuclear protein; Aminoacid sequence
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(89)81626-6

P1, a high mobility group-like nuclear protein, phosphorylated by casein kinase II on multiple sites in situ, has been found to be phosphorylated in vitro by protein kinase C, cyclic AMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase II on multiple and mostly distinct thennolytic peptides. All these enzymes phosphorylated predominantly serine residues, with casein kinase II and protein kinase C also labeling threonine residues. Both casein kinase II and second messenger-regulated protein kinases, particularly protein kinase C, might therefore be involved in the physiological regulation of multisite phosphorylation of PI.