The stress inducer arsenite activates mitogen-activated protein kinases extracellular signal-regulated kinases 1 and 2 via a MAPK kinase 6/p38-dependent pathway.
J Biol Chem
; 273(4): 1917-22, 1998 Jan 23.
Article
en En
| MEDLINE
| ID: mdl-9442025
ABSTRACT
Cell response to a wide variety of extracellular signals is mediated by either mitogenic activation of the Raf/MEK/ERK kinase cascade or stress-induced activation of the mitogen-activated protein kinase (MAPK) family members c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) or p38. We have examined communications between these stress- and mitogen-induced signaling pathways. We show here that the stress cascade activator arsenite activates extracellular signal-regulated kinase (ERK) in addition to p38 albeit with different kinetics. Whereas p38 is an early response kinase, ERK activation occurs with delayed time kinetics at 2-4 h. We observed activation of ERK upon arsenite treatment in many different cell lines. ERK activation is strongly enhanced by overexpression of p38 and mitogen-activated protein kinase kinase 6 (MKK6) but is blocked by dominant negative kinase versions of p38 and MKK6 or the specific p38 inhibitor SB203580. Arsenite-induced ERK activation is mediated by Ras, Raf, and MEK but appears to be independent of de novo protein synthesis. These data provide the first evidence for a p38 dependent activation of the mitogenic kinase cascade in stress-stimulated cells.
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Colección:
01-internacional
Asunto principal:
Proteínas Quinasas
/
Proteínas Quinasas Dependientes de Calcio-Calmodulina
/
Arsenitos
/
Proteína Quinasa 1 Activada por Mitógenos
/
Proteínas Quinasas Activadas por Mitógenos
Límite:
Humans
Idioma:
En
Revista:
J Biol Chem
Año:
1998
Tipo del documento:
Article
País de afiliación:
Alemania