AKT3, A Phloem-Localized K+ Channel, Is Blocked by Protons
The potassium-channel gene, AKT3, has recently been isolated from an Arabidopsis thaliana cDNA library. By using the whole-mount and in situ hybridization techniques, we found AKT3 predominantly expressed in the phloem. To study the physiological role of this channel type, AKT3 was heterologously ex...
Saved in:
Published in: | Proceedings of the National Academy of Sciences - PNAS Vol. 96; no. 13; pp. 7581 - 7586 |
---|---|
Main Authors: | , , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
United States
National Academy of Sciences of the United States of America
22-06-1999
National Acad Sciences National Academy of Sciences The National Academy of Sciences |
Subjects: | |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Summary: | The potassium-channel gene, AKT3, has recently been isolated from an Arabidopsis thaliana cDNA library. By using the whole-mount and in situ hybridization techniques, we found AKT3 predominantly expressed in the phloem. To study the physiological role of this channel type, AKT3 was heterologously expressed in Xenopus oocytes, and the electrical properties were examined with voltage-clamp techniques. Unlike the plant inward-rectifying guard cell K+ channels KAT1 and KST1, the AKT3 channels were only weakly regulated by the membrane potential. Furthermore, AKT3 was blocked by physiological concentrations of external Ca2+ and showed an inverted pH regulation. Extracellular acidification decreased the macroscopic AKT3 currents by reducing the single-channel conductance. Because assimilate transport in the vascular tissue coincides with both H+ and K+ fluxes, AKT3 K+ channels may be involved in K+ transport accompanying phloem loading and unloading processes. |
---|---|
Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 To whom reprint requests should be addressed. e-mail: marten@mbox.biophysik.uni-hannover.de. Communicated by Roland Douce, University of Grenoble, Grenoble, France |
ISSN: | 0027-8424 1091-6490 |
DOI: | 10.1073/pnas.96.13.7581 |