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J. Biol. Chem., Vol. 281, Issue 49, 37536-37546, December 8, 2006

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The Arabidopsis Protein Kinase PTI1-2 Is Activated by Convergent Phosphatidic Acid and Oxidative Stress Signaling Pathways Downstream of PDK1 and OXI1^*

Richard G. Anthony¹, Safina Khan, Joana Costa, Maria S. Pais^¶, and László Bögre

From the School of Biological Sciences, Royal Holloway, University of London, Egham Hill, Egham, Surrey TW20 0EX, United Kingdom, Centre for Plant Sciences, School of Biology, University of Leeds, Leeds LS2 9JT, United Kingdom, and ^¶Laboratory for Plant Biotechnology-Instituto de Ciência Aplicada e Tecnologia, Faculdade de Ciências da Universidade de Lisboa, Gampo Grande, 1749-016 Lisboa, Portugal

Arabidopsis PDK1 activity is regulated by binding to the lipid phosphatidic acid (PA) resulting in activation of the oxidative stress-response protein kinase OXI1/AGC2-1. Thus there is an inferred link between lipid signaling and oxidative stress signaling modules. Among a panel of hormones and stresses tested, we found that, in addition to PA, the fungal elicitor xylanase activated PDK1, suggesting that PDK1 has a role in plant pathogen defense mechanisms. The downstream OXI1 was activated by additional stress factors, including PA, H₂O₂, and partially by xylanase. We have isolated an interacting partner of OXI1, a Ser/Thr kinase (PTI1-2), which is downstream of OXI1. Its sequence closely resembles the tomato Pti kinase, which has been implicated in the hypersensitive response, a localized programmed cell death that occurs at the site of pathogen infection. PTI1-2 is activated by the same stresses/elicitors as OXI1 and additionally flagellin. We have used RNA interference to knock out the expression of PDK1 and OXI1 and to study the effects on PTI1-2 activity. We show that specific lipid signaling pathways converge on PTI1-2 via the PDK1-OXI1 axis, whereas H₂O₂ and flagellin signals to OXI1-PTI1-2 via a PDK1-independent pathway. PTI1-2 represents a new downstream component that integrates diverse lipid and reactive oxygen stress signals and functions closely with OXI1.

Received for publication, August 2, 2006 , and in revised form, September 25, 2006.

^* This work was supported by Biotechnology and Biological Sciences Research Council grant (to R. G. A., S. K., and L. B.), the European Framework 5 Project, GVE, the Fundação para a Ciência e a Tecnologia, Ministério da Ciência e do Ensino Superior Grant SFRH/BD/10560/2002 (to J. C.), and Wellcome Trust Grants 067411/Z/02/Z and GA AVCR 204/04/1013 (to L. B.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. 1.

¹ To whom correspondence should be addressed. Tel.: 44-0-1784-443539; Fax: 44-0-1784-430100; E-mail: r.g.anthony{at}rhul.ac.uk.

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