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AtTPK4, an Arabidopsis tandem-pore K+ channel, poised to control the pollen membrane voltage in a pH- and Ca2+-dependent manner.
- Source :
-
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2004 Nov 02; Vol. 101 (44), pp. 15621-6. Date of Electronic Publication: 2004 Oct 25. - Publication Year :
- 2004
-
Abstract
- The Arabidopsis tandem-pore K(+) (TPK) channels displaying four transmembrane domains and two pore regions share structural homologies with their animal counterparts of the KCNK family. In contrast to the Shaker-like Arabidopsis channels (six transmembrane domains/one pore region), the functional properties and the biological role of plant TPK channels have not been elucidated yet. Here, we show that AtTPK4 (KCO4) localizes to the plasma membrane and is predominantly expressed in pollen. AtTPK4 (KCO4) resembles the electrical properties of a voltage-independent K(+) channel after expression in Xenopus oocytes and yeast. Hyperpolarizing as well as depolarizing membrane voltages elicited instantaneous K(+) currents, which were blocked by extracellular calcium and cytoplasmic protons. Functional complementation assays using a K(+) transport-deficient yeast confirmed the biophysical and pharmacological properties of the AtTPK4 channel. The features of AtTPK4 point toward a role in potassium homeostasis and membrane voltage control of the growing pollen tube. Thus, AtTPK4 represents a member of plant tandem-pore-K(+) channels, resembling the characteristics of its animal counterparts as well as plant-specific features with respect to modulation of channel activity by acidosis and calcium.
- Subjects :
- Animals
Arabidopsis genetics
Arabidopsis Proteins genetics
Calcium metabolism
Cell Membrane metabolism
Female
Hydrogen-Ion Concentration
In Vitro Techniques
Kinetics
Membrane Potentials
Molecular Sequence Data
Mutation
Oocytes metabolism
Pollen metabolism
Potassium Channels, Tandem Pore Domain genetics
Recombinant Proteins genetics
Recombinant Proteins metabolism
Saccharomyces cerevisiae genetics
Saccharomyces cerevisiae metabolism
Xenopus
Arabidopsis metabolism
Arabidopsis Proteins metabolism
Potassium Channels, Tandem Pore Domain metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0027-8424
- Volume :
- 101
- Issue :
- 44
- Database :
- MEDLINE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Academic Journal
- Accession number :
- 15505206
- Full Text :
- https://doi.org/10.1073/pnas.0401502101