This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Verslues, P. E. Articles by Zhu, J.-K. Search for Related Content PubMed PubMed Citation Articles by Verslues, P. E. Articles by Zhu, J.-K.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, November 2007, p. 7771-7780, Vol. 27, No. 22
0270-7306/07/$08.00+0     doi:10.1128/MCB.00429-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Interaction of SOS2 with Nucleoside Diphosphate Kinase 2 and Catalases Reveals a Point of Connection between Salt Stress and H₂O₂ Signaling in Arabidopsis thaliana

Paul E. Verslues,¹ Giorgia Batelli,^1,2 Stefania Grillo,² Fernanda Agius,¹ Yong-Sig Kim,³ Jianhua Zhu,¹ Manu Agarwal,¹ Surekha Katiyar-Agarwal,¹ and Jian-Kang Zhu^1*

Institute for Integrative Genome Biology and Department of Botany and Plant Sciences, University of California, Riverside, California 92521,¹ Research Centre for Vegetable Breeding, National Research Council, University of Naples, 80055 Portici, Italy,² Department of Plant Sciences, University of Arizona, Tucson, Arizona 85721³

Received 13 March 2007/ Returned for modification 24 May 2007/ Accepted 20 August 2007

SOS2, a class 3 sucrose-nonfermenting 1-related kinase, has emerged as an important mediator of salt stress response and stress signaling through its interactions with proteins involved in membrane transport and in regulation of stress responses. We have identified additional SOS2-interacting proteins that suggest a connection between SOS2 and reactive oxygen signaling. SOS2 was found to interact with the H₂O₂ signaling protein nucleoside diphosphate kinase 2 (NDPK2) and to inhibit its autophosphorylation activity. A sos2-2 ndpk2 double mutant was more salt sensitive than a sos2-2 single mutant, suggesting that NDPK2 and H₂O₂ are involved in salt resistance. However, the double mutant did not hyperaccumulate H₂O₂ in response to salt stress, suggesting that it is altered signaling rather than H₂O₂ toxicity alone that is responsible for the increased salt sensitivity of the sos2-2 ndpk2 double mutant. SOS2 was also found to interact with catalase 2 (CAT2) and CAT3, further connecting SOS2 to H₂O₂ metabolism and signaling. The interaction of SOS2 with both NDPK2 and CATs reveals a point of cross talk between salt stress response and other signaling factors including H₂O₂.

---

* Corresponding author. Mailing address: Institute of Integrative Genome Biology and Department of Botany and Plant Sciences, University of California, Riverside, CA 92521. Phone: (951) 827-7117. Fax: (951) 827-7115. E-mail: jian-kang.zhu{at}ucr.edu

Published ahead of print on 4 September 2007.

---

Molecular and Cellular Biology, November 2007, p. 7771-7780, Vol. 27, No. 22
0270-7306/07/$08.00+0     doi:10.1128/MCB.00429-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

This article has been cited by other articles:

• Fujii, H., Zhu, J.-K. (2009). An Autophosphorylation Site of the Protein Kinase SOS2 Is Important for Salt Tolerance in Arabidopsis. Mol Plant 0: ssn087v1-ssn087 [Abstract] [Full Text]  
• Van Breusegem, F., Bailey-Serres, J., Mittler, R. (2008). Unraveling the Tapestry of Networks Involving Reactive Oxygen Species in Plants. Plant Physiol. 147: 978-984 [Full Text]