Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Ludwig, S. et al.

The stress inducer arsenite activates mitogen-activated protein kinases extracellular signal-regulated kinases 1 and 2 via a MAPK kinase 6/ p38-dependent pathway.

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.[1]

References

The stress inducer arsenite activates mitogen-activated protein kinases extracellular signal-regulated kinases 1 and 2 via a MAPK kinase 6/p38-dependent pathway. Ludwig, S., Hoffmeyer, A., Goebeler, M., Kilian, K., Häfner, H., Neufeld, B., Han, J., Rapp, U.R. J. Biol. Chem. (1998) [Pubmed]

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