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多胺对植物细胞膜离子转运的调节:了解胁迫下的特定作用模式

Modulation of Ion Transport Across Plant Membranes by Polyamines: Understanding Specific Modes of Action Under Stress.

作者信息

Pottosin Igor, Olivas-Aguirre Miguel, Dobrovinskaya Oxana, Zepeda-Jazo Isaac, Shabala Sergey

机构信息

International Research Centre for Environmental Membrane Biology, Foshan University, Foshan, China.

Biomedical Center, University of Colima, Colima, Mexico.

出版信息

Front Plant Sci. 2021 Jan 26;11:616077. doi: 10.3389/fpls.2020.616077. eCollection 2020.

Abstract

This work critically discusses the direct and indirect effects of natural polyamines and their catabolites such as reactive oxygen species and γ-aminobutyric acid on the activity of key plant ion-transporting proteins such as plasma membrane H and Ca ATPases and K-selective and cation channels in the plasma membrane and tonoplast, in the context of their involvement in stress responses. Docking analysis predicts a distinct binding for putrescine and longer polyamines within the pore of the vacuolar TPC1/SV channel, one of the key determinants of the cell ionic homeostasis and signaling under stress conditions, and an additional site for spermine, which overlaps with the cytosolic regulatory Ca-binding site. Several unresolved problems are summarized, including the correct estimates of the subcellular levels of polyamines and their catabolites, their unexplored effects on nucleotide-gated and glutamate receptor channels of cell membranes and Ca-permeable and K-selective channels in the membranes of plant mitochondria and chloroplasts, and pleiotropic mechanisms of polyamines' action on H and Ca pumps.

摘要

这项工作批判性地讨论了天然多胺及其代谢产物(如活性氧和γ-氨基丁酸)对关键植物离子转运蛋白活性的直接和间接影响,这些蛋白包括质膜H⁺和Ca²⁺ ATP酶以及质膜和液泡膜中的K⁺选择性和阳离子通道,同时探讨了它们在应激反应中的作用。对接分析预测,腐胺和更长链的多胺在液泡TPC1/SV通道的孔内有独特的结合,该通道是应激条件下细胞离子稳态和信号传导的关键决定因素之一,精胺还有一个额外的结合位点,与胞质调节性Ca²⁺结合位点重叠。总结了几个未解决的问题,包括多胺及其代谢产物亚细胞水平的正确估计、它们对细胞膜核苷酸门控和谷氨酸受体通道以及植物线粒体和叶绿体膜中Ca²⁺通透和K⁺选择性通道的未探索影响,以及多胺对H⁺和Ca²⁺泵作用的多效性机制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/60e2/7870501/d6507046a1f3/fpls-11-616077-g001.jpg

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