CSN1 inhibits c-Jun phosphorylation and down-regulates ectopic expression of JNK1
Protein & Cell
;
(12): 423-432, 2011.
Artículo
en Inglés
| WPRIM
| ID: wpr-757091
ABSTRACT
CSN1 is a component of the COP9 signalosome (CSN), a conserved protein complex with pleiotropic functions in many organs and cell types. CSN regulates ubiquitinproteasome dependent protein degradation via the deneddylation and the associated deubiquitination activities. In addition, CSN associates with protein kinases and modulates cell signaling, particularly the activator protein 1 (AP-1) pathway. We have shown previously that CSN1 suppresses AP-1 transcription activity and inhibits ultraviolet (UV) and serum activation of c-fos expression. Here we show that CSN1 can inhibit phosphorylation of proto-oncogene c-Jun product and repress c-Jun dependent transcription. Further, CSN1 dramatically downregulates ectopic expression of c-Jun N-terminal kinase 1 (JNK1) in cultured cells. The decline in JNK1 is not caused by excessive proteolysis or by 3' UTR-dependent mRNA instability, but by CSN1-dependent repression of one or multiple steps in transcriptional and posttranscriptional mechanisms. Thus, in contrast to CSN5/Jab1, which promotes AP-1 activity, CSN1 displays a negative effect on the AP-1 pathway. Finally, we discuss about the dynamic equilibrium of the CSN complexes in regulation of the AP-1 pathway.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Fosforilación
/
Regulación hacia Abajo
/
Línea Celular
/
Proteínas Proto-Oncogénicas c-jun
/
Factor de Transcripción AP-1
/
Regiones no Traducidas 3'
/
Proteína Quinasa 8 Activada por Mitógenos
/
Péptidos y Proteínas de Señalización Intracelular
/
Complejo del Señalosoma COP9
/
Genética
Límite:
Animales
/
Humanos
Idioma:
Inglés
Revista:
Protein & Cell
Año:
2011
Tipo del documento:
Artículo
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