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HSP70-3 Interacts with Phospholipase D delta and Participates in Heat Stress Defense

文献类型： 外文期刊

作者： Song, Ping 1 ; Jia, Qianru 1 ; Xiao, Xingkai 1 ; Tang, Yiwen 1 ; Liu, Chengjian 1 ; Li, Wenyan 1 ; Li, Teng 1 ; Li, Li 1 ; C 1 ;

作者机构： 1.Nanjing Agr Univ, Coll Life Sci, State Key Lab Crop Genet & Germplasm Enhancement, Nanjing 210095, Peoples R China

2.Jiangsu Prov & Chinese Acad Sci, Inst Bot, Nanjing Bot Garden Mem Sun Yat Sen, Nanjing 210014, Peoples R China

3.Jiangsu Acad Agr Sci, Inst Ind Crops, Nanjing 210014, Peoples R China

期刊名称：PLANT PHYSIOLOGY （ 影响因子：6.902； 五年影响因子：7.52 ）

ISSN： 0032-0889

年卷期： 2021 年 185 卷 3 期

页码：

收录情况： SCI

摘要： Heat shock proteins (HSPs) function as molecular chaperones and are key components responsible for protein folding, assembly, translocation, and degradation under stress conditions. However, little is known about how HSPs stabilize proteins and membranes in response to different hormonal or environmental cues in plants. Here, we combined molecular, biochemical, and genetic approaches to elucidate the involvement of cytosolic HSP70-3 in plant stress responses and the interplay between HSP70-3 and plasma membrane (PM)-localized phospholipase D delta (PLD delta) in Arabidopsis (Arabidopsis thaliana). Analysis using pull-down, coimmunoprecipitation, and bimolecular fluorescence complementation revealed that HSP70-3 specifically interacted with PLE306. HSP70-3 bound to microtubules, such that it stabilized cortical microtubules upon heat stress. We also showed that heat shock induced recruitment of HSP70-3 to the PM, where HSP70-3 inhibited PLD delta activity to mediate microtubule reorganization, phospholipid metabolism, and plant thermotolerance, and this process depended on the HSP70-3-PLD delta interaction. Our results suggest a model whereby the interplay between HSP70-3 and PLD delta facilitates the re-establishment of cellular homeostasis during plant responses to external stresses and reveal a regulatory mechanism in regulating membrane lipid metabolism.

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