Arabidopsis decuple mutant reveals the importance of SnRK2 kinases in osmotic stress responses in vivo

被引:265
|
作者
Fujii, Hiroaki [1 ,2 ]
Verslues, Paul E. [1 ]
Zhu, Jian-Kang [1 ,2 ,3 ]
机构
[1] Univ Calif Riverside, Dept Bot & Plant Sci, Riverside, CA 92521 USA
[2] King Abdullah Univ Sci & Technol, Ctr Plant Stress Genom & Technol, Thuwal 239556900, Saudi Arabia
[3] Purdue Univ, Dept Hort & Landscape Architecture, W Lafayette, IN 47907 USA
基金
美国国家卫生研究院;
关键词
abiotic stress; water deficit; osmosensing; signal transduction; phosphorylation; ACTIVATED PROTEIN-KINASES; ABSCISIC-ACID; SIGNAL-TRANSDUCTION; HYPEROSMOTIC STRESS; GENE-EXPRESSION; SNF1-RELATED PROTEIN-KINASE-2; SEED-GERMINATION; DROUGHT; SALT; PHOSPHORYLATION;
D O I
10.1073/pnas.1018367108
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Osmotic stress associated with drought or salinity is a major factor that limits plant productivity. Protein kinases in the SNF1-related protein kinase 2 (SnRK2) family are activated by osmotic stress, suggesting that the kinases are involved in osmotic stress signaling. However, due to functional redundancy, their contribution to osmotic stress responses remained unclear. In this report, we constructed an Arabidopsis line carrying mutations in all 10 members of the SnRK2 family. The decuple mutant snrk2.1/2/3/4/5/6/7/8/9/10 grew poorly under hyperosmotic stress conditions but was similar to the wild type in culture media in the absence of osmotic stress. The mutant was also defective in gene regulation and the accumulation of abscisic acid (ABA), proline, and inositol 1,4,5-trisphosphate under osmotic stress. In addition, analysis of mutants defective in the ABA-activated SnRK2s (snrk2.2/3/6) and mutants defective in the rest of the SnRK2s (snrk2.1/4/5/7/8/9/10) revealed that SnRK2s are a merging point of ABA-dependent and -independent pathways for osmotic stress responses. These results demonstrate critical functions of the SnRK2s in mediating osmotic stress signaling and tolerance.
引用
收藏
页码:1717 / 1722
页数:6
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