
An endoplasmic reticulum–localized cytochrome b 5 regulates high-affinity K + transport in response to salt stress in rice
Author(s) -
Tengzhao Song,
Yiyuan Shi,
Like Shen,
Chengjuan Cao,
Yue Shen,
Wen Jing,
Quanxiang Tian,
Feng Lin,
Wenyu Li,
Wenhua Zhang
Publication year - 2021
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2114347118
Subject(s) - endoplasmic reticulum , transporter , intracellular , homeostasis , biochemistry , chemistry , intracellular ph , microbiology and biotechnology , sodium , cytochrome , atp binding cassette transporter , biophysics , biology , enzyme , gene , organic chemistry
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.