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The Plant Cell 19:2098
Phosphatase AP2C1 Is a Key Component of MAPK Signaling in Arabidopsisneckardt{at}aspb.org
MAPK signaling is prevalent among eukaryotes and is implicated in the regulation of numerous processes, including the cell cycle and cell proliferation, differentiaton, and development, and environmental responses. MAPKs function as a component of a kinase signaling cascade that operates through sequential phosphorylation steps, wherein a MAPK kinase kinase phosphorylates a MAPK kinase, which in turn phosphorylates a MAPK. A phosphorylated MAPK is capable of phosphorylating other substrates, such as transcription factors. Several Arabidopsis MAPKs have been identified as components of stress response and plant defense signaling pathways receiving input from jasmonic acid, ethylene, salicylic acid, and other signals. MAPK cascades may provide for intricate control over cellular responses. For example, in the case of ethylene signaling in plants, MAPK signaling feeds forward to various downstream responses and feeds back to affect ethylene biosynthesis. A critical component of MAPK signaling is provided by phosphatases that dephosphorylate and inactivate MAPKs, but this aspect of MAPK signaling is not well understood. Schweighofer et al. (pages 2213–2224) show that the Arabidopsis Ser/Thr phosphatase AP2C1 inactivates the stress-responsive MAPKs MPK4 and MPK6. This function of AP2C1 was found to play an important role in plant response to environmental stress related to jasmonate and ethylene signaling, including wounding, herbivore attack, and challenge with necrotrophic pathogens. The results suggest that under some circumstances, AP2C1 may control the amount of damage the plant incurs in response to biotic challenge through its regulation of MAPK signaling.
Footnotes www.plantcell.org/cgi/doi/10.1105/tpc.107.190710 Related articles in Plant Cell:
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