A phosphoinositide-specific phospholipase C pathway elicits stress-induced Ca2+ signals and confers salt tolerance to rice
A phosphoinositide-specific phospholipase C pathway elicits stress-induced Ca2+ signals and confers salt tolerance to rice
复制标题
磷酸肌醇特异性磷脂酶 C 途径引发应激诱导的 Ca2 信号并赋予水稻耐盐性
DOI:
10.1111/nph.14426
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发表时间:
2017-05-01
期刊:
影响因子:
9.4
通讯作者:
Zhang, Wenhua
中科院分区:
文献类型:
--
作者:
Li, Li;Wang, Fawei;Zhang, Wenhua
In animal cells, phospholipase C (PLC) isoforms predominantly hydrolyze phosphatidylinositol- 4,5-biphosphates [PtdIns(4,5) P-2] into the second messengers diacylglycerol (DAG) and inositol 1,4,5-trisphosphate [Ins(1,4,5) P-3] to regulate diverse biological processes. By contrast, the molecular mechanisms and physiological significance of PLC signaling in plants still awaits full elucidation. Here, we identified a rice (Oryza sativa cv) PI-PLC, OsPLC1, which preferred to hydrolyze phosphatidylinositol-4-phosphate (PtdIns4P) and elicited stress-induced Ca2+ signals regulating salt tolerance.Analysis by ion chromatography revealed that the concentration of PtdIns4P was c. 28 times of that of PtdIns(4,5) P-2 in shoots. OsPLC1 not only converted PtdIns(4,5) P2 but also and even more efficiently - converted PtdIns4P into DAG and Ins(1,4,5) P-3 in vitro and in vivo.Salt stress induced the recruitment of OsPLC1 from cytoplasm to plasma membrane, where it hydrolyzed PtdIns4P. The stress-induced Ca2+ signaling was dependent on OsPLC1, and the PLC-mediated Ca2+ signaling was essential for controlling Na+ accumulation in leaf blades, thus establishing whole plant salt tolerance.Our work identifies a conversion pathway and physiological function for PtdIns4P pools in rice and reveals the connection between phosphoinositides and Ca2+ signals mediated by PLC during salt stress responses.