Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1996 Nov;10(5):869-52.
doi: 10.1046/j.1365-313x.1996.10050869.x.

Alkali cation selectivity of the wheat root high-affinity potassium transporter HKT1

Affiliations
Free article

Alkali cation selectivity of the wheat root high-affinity potassium transporter HKT1

W Gassman et al. Plant J. 1996 Nov.
Free article

Abstract

The wheat root high-affinity K+ transporter HKT1 functions as a sodium-coupled potassium co-uptake transporter. At toxic millimolar levels of sodium (Na+), HKT1 mediates low-affinity Na+ uptake while potassium (K+) uptake is blocked. In roots, low-affinity Na+ uptake and inhibition of K+ uptake contribute to Na+ toxicity. In the present study, the selectivity among alkali cations of HKT1 expressed in Xenopus oocytes and yeast was investigated under various ionic conditions at steady state. The data show that HKT1 is highly selective for uptake of the two physiologically significant alkali cations, K+ and Na+ over Rb+, Cs+ and Li+. In addition, Rb+ and Cs+, and an excess of extracellular K+ over Na+, are shown to partially reduce or block HKT1-mediated K(+)-Na+ uptake. Furthermore, K+, Rb+ and Cs+ also effectively reduce outward currents mediated by HKT1, thereby causing depolarizations. In yeast, HKT1 can produce high-affinity Rb+ uptake at approximately 15-fold lower rates than for K+. Rb+ influx in yeast can be mediated by the ability of the yeast plasma membrane proton pump to balance the >or= 35-fold lower HKT1 conductance for Rb+. A model for HKT1 activity is presented involving a high-affinity K+ binding site and a high-affinity Na+ binding site, and competitive interactions of K+, Na+ and other alkali cations for binding to these two sites. Possible implications of the presented results for physiological K+ and Na+ uptake in plants are discussed.

PubMed Disclaimer

Similar articles

Cited by

Publication types

LinkOut - more resources