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M701888200v1
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Papers In Press, published online ahead of print June 22, 2007
J. Biol. Chem, 10.1074/jbc.M701888200
Submitted on March 5, 2007
Revised on June 21, 2007
Accepted on June 22, 2007

Arabidopsis MAPK phosphatase MKP2 positively regulates oxidative stress tolerance and inactivates the MPK3 and MPK6 mitogen-activated protein kinases

Jin Suk Lee and Brian E. Ellis

Michael Smith Laboratories, University of British Columbia, Vancouver, BC V6T 1Z4

Corresponding Author: bee{at}interchange.ubc.ca

Two closely related Arabidopsis mitogen-activated protein kinases (MAPKs), MPK3 and MPK6, are rapidly but transiently activated in plants exposed to ozone. Although the contribution of these MAPKs to control of redox stress has been examined extensively, it remains unclear whether the dual-specificity MAPK phosphatases (MKPs) play an essential role in the regulation of these processes. To explore this question, specific knock-down of each of the five putative MKPs in Arabidopsis was performed, and the ozone sensitivity phenotype of each MKP-suppressed line was assessed. Silencing of only one previously uncharacterized MKP, designated AtMKP2, rendered the plants hypersensitive to oxidative stress. AtMKP2-suppressed plants displayed significantly prolonged MPK3 and MPK6 activation during ozone treatment, and recombinant AtMKP2 was able to dephosphorylate both phospho-MPK3 and phospho-MPK6 in vitro, providing direct evidence that AtMKP2 may target these oxidant-activated MAPKs. In addition, the in vitro phosphatase activity of AtMKP2 was enhanced by co-incubation with either recombinant MPK3 or MPK6. In AtMKP2:YFP-expressing plants, the fusion protein was localized predominantly in the nucleus, the same compartment into which ozone-activated MPK3 and MPK6 have previously been shown to be translocated. Taken together, these data suggest that AtMKP2, a novel MKP protein in Arabidopsis, acts upon MPK3 and 6, and serves as a positive regulator of the cellular response to oxidant challenge.


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