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.
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 thermolytic 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 P1.
Walaas
S I
SI
Institute of Medical Biochemistry, University of Oslo, Norway.
Ostvold
A C
AC
Laland
S G
SG
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001345:Autoradiography; D001921:Brain / Q000201:enzymology; D047388:Casein Kinases; D004591:Electrophoresis, Polyacrylamide Gel; D006609:High Mobility Group Proteins / Q000032:analysis*; D008099:Liver / Q000201:enzymology; D010449:Peptide Mapping; D010750:Phosphoproteins / Q000096:biosynthesis*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000032:analysis / Q000378:metabolism*; D011494:Protein Kinases / Q000032:analysis / Q000378:metabolism*; D051381:Rats; D012269:Ribosomal Proteins
D006609:High Mobility Group Proteins; D010750:Phosphoproteins; D012269:Ribosomal Proteins; C035690:ribosomal phosphoprotein P1; D000255:Adenosine Triphosphate; D011494:Protein Kinases; D047388:Casein Kinases; D011493:Protein Kinase C