SP600125 inhibits cap-dependent translation independently of the c-Jun N-terminal kinase pathway.
Cell Struct Funct
; 36(1): 27-33, 2011.
Article
em En
| MEDLINE
| ID: mdl-21263197
ABSTRACT
We investigated the effects of SP600125 (formerly called c-Jun N-terminal kinase (JNK) inhibitor II) on translation using cultured mouse cells. SP600125 (50 µM) treatment rapidly repressed overall protein synthesis, accompanied by a reduction in the mRNAs for housekeeping genes such as glyceraldehyde-3-phosphate dehydrogenase in the polysomal fraction. SP600125 decreased polysomes with a concomitant increase in free ribosomal subunits in the cytoplasm, suggesting that global translation was inhibited at the initiation step. A reporter analysis using exogenous mRNAs showed that SP600125 inhibited cap-dependent but not internal ribosome entry site-dependent translation. SP600125 significantly attenuated phosphorylation of components in the mTOR pathway, which is responsible for cap-dependent translation. In contrast to SP600125, short hairpin RNAs for JNK1 and JNK2 failed to affect overall protein synthesis. Collectively, SP600125 inhibits cap-dependent translation, independent of the JNK pathway.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Biossíntese de Proteínas
/
Proteínas Quinases JNK Ativadas por Mitógeno
/
Inibidores de Proteínas Quinases
/
Antracenos
Limite:
Animals
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article