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An endoplasmic reticulum–localized cytochrome <i>b</i> <sub>5</sub> regulates high-affinity K <sup>+</sup> transport in response to salt stress in rice

Tengzhao Song, Yiyuan Shi, Like Shen, Chengjuan Cao, Yue Shen, Wen Jing, Quanxiang Tian, Feng Lin, Wenyu Li, Wenhua Zhang

2021Proceedings of the National Academy of Sciences50 citationsDOIOpen Access PDF

Abstract

Significance High-affinity K + (HAK) transporter-mediated K + uptake has an important role when plants are subjected to stresses. This work identifies a mechanism of HAK regulation. The affinity of HAK at the plasma membrane for K + depends on the binding of a cytochrome (CYB5) protein at the endoplasmic reticulum. This improves K + uptake and the ability of plants to survive under saline conditions. The HAK–CYB5 interaction not only constitutes a mechanism of HAK regulation but also reflects interorganelle communication mediated by functional protein interactions under conditions of stress.

Topics & Concepts

Endoplasmic reticulumTransporterIntracellularHomeostasisChemistryBiochemistryIntracellular pHCell biologySodiumBiophysicsBiologyGeneOrganic chemistryPlant Stress Responses and TolerancePlant nutrient uptake and metabolismPhotosynthetic Processes and Mechanisms
An endoplasmic reticulum–localized cytochrome <i>b</i> <sub>5</sub> regulates high-affinity K <sup>+</sup> transport in response to salt stress in rice | Litcius