Phosphorylation influences water and ion channel function of AtPIP2;1

磷酸化 爪蟾 突变体 生物物理学 丝氨酸 化学 细胞生物学 离子运输机 异源表达 亚细胞定位 蛋白质磷酸化 水运 生物化学 生物 水流 细胞质 蛋白激酶A 重组DNA 基因 环境工程 工程类
作者
Jiaen Qiu,Samantha McGaughey,Michael Groszmann,Stephen D. Tyerman,Caitlin S. Byrt
出处
期刊:Plant Cell and Environment [Wiley]
卷期号:43 (10): 2428-2442 被引量:43
标识
DOI:10.1111/pce.13851
摘要

Abstract The phosphorylation state of two serine residues within the C‐terminal domain of AtPIP2;1 (S280, S283) regulates its plasma membrane localization in response to salt and osmotic stress. Here, we investigated whether the phosphorylation state of S280 and S283 also influence AtPIP2;1 facilitated water and cation transport. A series of single and double S280 and S283 phosphomimic and phosphonull AtPIP2;1 mutants were tested in heterologous systems. In Xenopus laevis oocytes, phosphomimic mutants AtPIP2;1 S280D, S283D, and S280D/S283D had significantly greater ion conductance for Na + and K + , whereas the S280A single phosphonull mutant had greater water permeability. We observed a phosphorylation‐dependent inverse relationship between AtPIP2;1 water and ion transport with a 10‐fold change in both. The results revealed that phosphorylation of S280 and S283 influences the preferential facilitation of ion or water transport by AtPIP2;1. The results also hint that other regulatory sites play roles that are yet to be elucidated. Expression of the AtPIP2;1 phosphorylation mutants in Saccharomyces cerevisiae confirmed that phosphorylation influences plasma membrane localization, and revealed higher Na + accumulation for S280A and S283D mutants. Collectively, the results show that phosphorylation in the C‐terminal domain of AtPIP2;1 influences its subcellular localization and cation transport capacity.
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