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

FEBS Letters

Walaas, S.Ivar¹  Laland, Søren G.²  C. Østvold, Anne² 

[1] Institute of Medical Biochemistry, University of Oslo, POB 1112, Blindern, 0317 Oslo 3, Norway;Department of Biochemistry, University of Oslo, POB 1041 Blindern, 0316 Oslo 3, Norway

关键词: Protein P1;    Phosphoprotein;    Protein kinase;    Peptide mapping;   

DOI  :  10.1016/0014-5793(89)81626-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown