Regulation of Claspin degradation by the ubiquitin-proteosome pathway during the cell cycle and in response to ATR-dependent checkpoint activation.
FEBS Lett
; 580(17): 4176-81, 2006 Jul 24.
Article
en En
| MEDLINE
| ID: mdl-16828751
ABSTRACT
Claspin is involved in ATR-dependent activation of Chk1 during DNA replication and in response to DNA damage. We show that degradation of Claspin by the ubiquitin-proteosome pathway is regulated during the cell cycle. Claspin is stabilized in S-phase but is abruptly degraded in mitosis and is absent from early G(1) cells in which the phosphorylation of Chk1 by ATR is abrogated. In response to hydroxyurea, UV or aphidicolin, Claspin is phosphorylated in the Chk1-binding domain and its protein levels are increased in an ATR-dependent manner. Thus, the Chk1 pathway is regulated through both phosphorylation of Claspin and its controlled degradation.
Buscar en Google
Banco de datos:
MEDLINE
Asunto principal:
Fase G1
/
Fase S
/
Proteínas Serina-Treonina Quinasas
/
Proteínas de Ciclo Celular
/
Ubiquitina
/
Complejo de la Endopetidasa Proteasomal
/
Proteínas Adaptadoras Transductoras de Señales
Límite:
Humans
Idioma:
En
Revista:
FEBS Lett
Año:
2006
Tipo del documento:
Article
País de afiliación:
Reino Unido