Involvement of the Membrane Trafficking Factor PATROL1 in the Salinity Stress Tolerance of Arabidopsis thaliana

被引:4
|
作者
Sato, Fumiya [1 ]
Iba, Koh [2 ]
Higaki, Takumi [3 ]
机构
[1] Kumamoto Univ, Grad Sch Sci & Technol, Chuo Ku, Kumamoto 8608555, Japan
[2] Kyushu Univ, Fac Sci, Dept Biol, Fukuoka 8190395, Japan
[3] Kumamoto Univ, Int Res Org Adv Sci & Technol, Chuo Ku, Kumamoto 8608555, Japan
基金
日本学术振兴会;
关键词
Arabidopsis thaliana; Membrane trafficking; PATROL1; Salinity stress tolerance; PROTEIN; EXOCYTOSIS; RESPONSES; DYNAMICS; PATHWAY;
D O I
10.1508/cytologia.86.119
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The Arabidopsis thaliana stomatal complex contains a pair of guard cells surrounded by subsidiary cells, which assist in turgor-driven stomatal movement and receive water and ions. This transport, driven by environmental signals, involves a translocation factor of the plasma membrane proton pump H+-ATPase AHA1, PATROL1. In this study, we investigated the responses of PATROL1 to salinity and hyperosmotic stresses. Specifically, we analyzed the effects of 125 mM NaCl or 231 mM mannitol on the cotyledon pavement cell cortexes in transgenic A. thaliana seedlings expressing green fluorescent protein (GFP)-tagged PATROL1. Cells treated with NaCl had few GFP-PATROL1-labeled dot-like structures but contained unusual labeled large bodies and rod-like structures. Cells treated with mannitol had similar large bodies, but not rods, indicating that the rod-like structures form specifically under salinity stress conditions. Dual observations of GFP-PATROL1 and red fluorescent protein (RFP)-tagged AHA1 in stress-treated cells revealed that the latter did not accumulate in the stress-induced GFP-PATROL1 structures, suggesting that the stress-induced GFP-PATROL1 structures are not involved in RFP-AHA1 localization. Additionally, the primary root growth of the patrol1 mutant was more sensitive to NaCl treatment than was that of wild type. Thus, PATROL1 appears to contribute to salinity stress tolerance, possibly by regulating membrane trafficking.
引用
收藏
页码:119 / 126
页数:8
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