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Protein kinase OsSAPK8 functions as an essential activator of S-type anion channel OsSLAC1, which is nitrate-selective in rice

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Abstract

Main conclusion

OsSAPK8 is an essential activator of OsSLAC1 by phosphorylation, and OsSLAC1 is a nitrate-selective anion channel.

S-type anion channel AtSLAC1 and protein kinase AtOST1 have been well-characterized as two core components of ABA signaling cascade in Arabidopsis guard cells, and AtOST1 functions as a main upstream activator of AtSLAC1 for drought stress- and ABA-induced stomata closure. However, the identity of the ortholog of AtOST1 in rice, the main activator of OsSLAC1, is still unknown. Here, we report that protein kinase OsSAPK8 interacts with and activates OsSLAC1 mainly by phosphorylating serine 129 (S129) of OsSLAC1, and this phosphorylating site corresponds to the specific phosphorylating site serine 120 (S120) of AtSLAC1 for AtOST1. Additionally, we found that OsSLAC1 is a nitrate-selective anion channel without obvious permeability to chloride, malate, and sulfate, and the expression of OsSLAC1 in Arabidopsis slac1-3 (atslac1-3) mutant successfully rescued the hypersensitive phenotype of this mutant to drought stress. Together, this research suggests that OsSAPK8 is a counterpart of AtOST1 for the activation of OsSLAC1, which is a nitrate-selective anion channel.

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Acknowledgments

This research was supported by the National Basic Research Program of China (973 program; Grant number 2012CB114300), a basic research key project from Science and Technology Commission of Shanghai Municipality (13JC1406100), the National Natural Science Foundation of China (31100213), the Knowledge Innovation Program of Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences (2011KIP508), and the Postdoctoral Science Foundation of China (20110490759). The authors gratefully acknowledge the support of SANOFI-SIBS Scholarship Program. We thank Hong-Wei Xue’s group (SIPPE, SIBS, CAS, China) for help with in vitro protein phosphorylation assay, and Hong-Xuan Lin (SIPPE, SIBS, CAS, China) for rice seeds Zhonghua 11. pGEMHE vector was from Wei-Hua Wu’s group (China Agricultural University, Beijing, China). atslac1-3 mutant was from Julian I Schroeder’s group (UC, San Diego, USA), and originally from Jaakko Kangasjärvi’s group (University of Helsinki, Finland).

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    1. National Key Laboratory of Plant Molecular Genetics, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, 200032, China

      Shu-Jing Sun, Guo-Ning Qi, Qi-Fei Gao, Hui-Qin Wang, Fen-Yong Yao, Jamshaid Hussain & Yong-Fei Wang

    2. University of Chinese Academy of Sciences, Shanghai, 200032, China

      Qi-Fei Gao & Fen-Yong Yao

    3. Biotechnology Program, Department of Environmental Sciences, COMSATS Institute of Information Technology, Abbottabad, 22060, Pakistan

      Jamshaid Hussain

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    S.-J. Sun and G.-N. Qi contributed equally to this work.

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    Supplemental Fig. 1 OsSAPK9 and OsSAPK10 are incapable to activate OsSLAC1 obviously compared with OsSAPK8. a Typical whole-oocyte recordings. b-c Average voltage–current curves (b), and the average current amplitudes of whole-oocyte currents recorded at -100 mV (c) as shown in b. The numbers of oocytes tested are 8 for control, 8 for OsSLAC1 + OsSAPK9, 11 for OsSLAC1 + OsSAPK10, 17 for OsSLAC1 + AtOST1, and 12 for OsSLAC1 + OsSAPK9. Error bars depict means ± s.e.m. Supplemental Fig. 2 The alignment of the N terminus of OsSLAC1 and AtSLAC1 predicts that S129 and S59 are two phosphorylating sites of OsSLAC1 as indicated by stars. (PDF 466 kb)

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    Sun, SJ., Qi, GN., Gao, QF. et al. Protein kinase OsSAPK8 functions as an essential activator of S-type anion channel OsSLAC1, which is nitrate-selective in rice. Planta 243, 489–500 (2016). https://doi.org/10.1007/s00425-015-2418-x

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