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. 2016 May 3;11(5):e1147643.
doi: 10.1080/15592324.2016.1147643.

Plant endosomal NHX antiporters: Activity and function

Quan-Sheng Qiu  1
Affiliations

Plant endosomal NHX antiporters: Activity and function

Quan-Sheng Qiu. Plant Signal Behav. .

Erratum in

  • Addendum to: Wang L, Wu X, Liu Y, Qiu QS. AtNHX5 and AtNHX6 control cellular K+ and pH homeostasis in Arabidopsis: Three conserved acidic residues are essential for K+ transport. PLoS One 2015; 10 (12): e0144716. doi:10.1371/journal.pone.0144716. doi: 10.1371/journal.pone.0144716

Abstract

The Arabidopsis NHX antiporter family contains eight members that are divided into three subclasses: vacuolar, endosomal, and plasma membrane. While the plasma membrane and vacuolar NHXs have been studied extensively, the activity and function of the endosomal NHXs are beginning to be discovered. AtNHX5 and AtNHX6 are endosomal Na(+),K(+)/H(+) antiporters that share high sequence similarity. They are localized in the Golgi, trans-Golgi network (TGN), and prevacuolear compartment (PVC). Studies have shown that AtNHX5 and AtNHX6 mediate K(+) and Na(+) transport, and regulate cellular pH homeostasis. Sequence alignment has found that AtNHX5 and AtNHX6 contain four conserved acidic amino acid residues in transmembrane domains that align with yeast and human NHXs. Three of these conserved acidic residues are critical for K(+) transport and seedling growth in Arabidopsis. Moreover, studies have shown that the precursors of the seed storage proteins are missorted to the apoplast in the nhx5 nhx6 knockout mutant, suggesting that AtNHX5 and AtNHX6 regulate protein transport into the vacuole. Further analysis found that AtNHX5 and AtNHX6 regulated the binding of VSR to its cargoes. Taken together, AtNHX5 and AtNHX6 play an important role in cellular ion and pH homeostasis, and are essential for protein transport into the vacuole.

Keywords: Arabidopsis; Na+,K+/H+ antiporters; conserved acidic residues; endosome; ion transport; pH homeostasis; protein transport.

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