Identification of phosphorylation sites on human deoxycytidine kinase after overexpression in eucaryotic cells.
Nucleosides Nucleotides Nucleic Acids
; 25(9-11): 1141-6, 2006.
Article
en En
| MEDLINE
| ID: mdl-17065079
ABSTRACT
Compelling evidence suggests that deoxycytidine kinase (dCK), a key enzyme in the salvage of deoxyribonucleosides and in the activation of clinically relevant nucleoside analogues, can be regulated by reversible phosphorylation. In this study, we show that dCK overexpressed in HEK-293T cells was labelled after incubation of the cells with [32P]orthophosphate. Tandem mass spectrometry allowed the identification of 4 in vivo phosphorylation sites, Thr3, Ser11, Ser15, and Ser74. These results provide the first evidence that dCK is constitutively multiphosphorylated in intact cells. In addition, site-directed mutagenesis demonstrated that phosphorylation of Ser74, the major in vivo phosphorylation site, is crucial for dCK activity.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Regulación Enzimológica de la Expresión Génica
/
Desoxicitidina Quinasa
/
Células Eucariotas
Tipo de estudio:
Diagnostic_studies
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Nucleosides Nucleotides Nucleic Acids
Asunto de la revista:
BIOQUIMICA
Año:
2006
Tipo del documento:
Article
País de afiliación:
Bélgica