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 Lett
; 258(1): 106-8, 1989 Nov 20.
Article
em En
| MEDLINE
| ID: mdl-2591527
ABSTRACT
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosfoproteínas
/
Proteínas Quinases
/
Proteína Quinase C
/
Proteínas de Grupo de Alta Mobilidade
Limite:
Animals
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1989
Tipo de documento:
Article
País de afiliação:
Noruega