Activation of the plasma membrane Na/H antiporter Salt-Overly-Sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain

被引:318
作者
Quintero, Francisco J. [2 ]
Martinez-Atienza, Juliana [2 ]
Villalta, Irene [2 ]
Jiang, Xingyu [2 ]
Kim, Woe-Yeon [3 ]
Ali, Zhair [3 ]
Fujii, Hiroaki [1 ]
Mendoza, Imelda [2 ]
Yun, Dae-Jin [3 ]
Zhu, Jian-Kang [1 ,4 ]
Pardo, Jose M. [1 ,2 ]
机构
[1] King Abdullah Univ Sci & Technol, Ctr Plant Stress Genom & Technol, Thuwal 239556900, Saudi Arabia
[2] Consejo Super Invest Cient, Inst Recursos Nat & Agrobiol, Seville 41012, Spain
[3] Gyeongsang Natl Univ, Grad Sch, Plant Mol Biol & Biotechnol Res Ctr, Div Appl Life Sci,Program BK21, Jinju 660701, South Korea
[4] 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
ion transport; salinity; sodium tolerance; ARABIDOPSIS-THALIANA; NA+/H+ ANTIPORTER; K+ TRANSPORT; TOLERANCE; PLANTS; CONSERVATION; EXPRESSION; EXCHANGER; ENCODES; PATHWAY;
D O I
10.1073/pnas.1018921108
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
The plasma membrane sodium/proton exchanger Salt-Overly-Sensitive 1 (SOS1) is a critical salt tolerance determinant in plants. The SOS2-SOS3 calcium-dependent protein kinase complex up-regulates SOS1 activity, but the mechanistic details of this crucial event remain unresolved. Here we show that SOS1 is maintained in a resting state by a C-terminal auto-inhibitory domain that is the target of SOS2-SOS3. The auto-inhibitory domain interacts intramolecularly with an adjacent domain of SOS1 that is essential for activity. SOS1 is relieved from auto-inhibition upon phosphorylation of the auto-inhibitory domain by SOS2-SOS3. Mutation of the SOS2 phosphorylation and recognition site impeded the activation of SOS1 in vivo and in vitro. Additional amino acid residues critically important for SOS1 activity and regulation were identified in a genetic screen for hypermorphic alleles.
引用
收藏
页码:2611 / 2616
页数:6
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