The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
A new family of outwardly rectifying potassium channel proteins with two pore domains in tandem
Open accessAbstract
POTASSIUM channels catalyse the permeation of K+ ions across cellular membranes and are identified by a common structural motif, a highly conserved signature sequence of eight amino acids in the P domain of each channel's pore-forming α-subunit1,2. Here we describe a novel K+ channel (TOK1) from Saccharomyces cerevisiae that contains two P domains within one continuous poly-peptide. Xenopus laevis oocytes expressing the channel exhibit a unique, outwardly rectifying, K+-selective current. The channel is permeable to outward flow of ions at membrane potentials above the K+ equilibrium potential; its conductionvoltage relationship is thus sensitive to extracellular K+ ion concentration. In excised membrane patches, external divalent cations block the channel in a voltage-dependent manner, and their removal in this configuration allows inward channel current. These attributes are similar to those described for inwardly rectifying K+ channels3,4, but in the opposite direction, a previously unrecognized channel behaviour. Our results identify a new class of K+ channel which is distinctive in both its primary structure and functional properties. Structural homo-logues of the channel are present in the genome of Caenorhabditis elegans.
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Phylogenetic Relationships within Cation Transporter Families of Arabidopsis
Mäser, P., Thomine, S., Schroeder, J. I., Ward, J. M., Hirschi, K., Sze, H., Talke, I. N., Amtmann, A., Maathuis, F. J. M., Sanders, D., et al. (2001) · Plant Physiology · doi:10.1104/pp.126.4.1646 · Cited by 1,257
Inhalational anesthetics activate two-pore-domain background K+ channels
Patel, A. J., Honoré, E., Lesage, F., Fink, M., Romey, G., & Lazdunski, M. (1999) · Nature Neuroscience · doi:10.1038/8084 · Cited by 655
Mechanically Activated Ion Channels
Ranade, S. S., Syeda, R., & Patapoutian, A. (2015) · Neuron · doi:10.1016/j.neuron.2015.08.032 · Cited by 652
TWIK-1, a ubiquitous human weakly inward rectifying K+ channel with a novel structure.
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Sumoylation Silences the Plasma Membrane Leak K+ Channel K2P1
Rajan, S., Plant, L. D., Rabin, M. L., Butler, M. H., & Goldstein, S. A. N. (2005) · Cell · doi:10.1016/j.cell.2005.01.019 · Cited by 263
Self-citation
Metadata
- Authors
- Ketchum, K. A., Joiner, W. J., Sellers, A. J., Kaczmarek, L. K., & Goldstein, S. A. N.
- Venue
- Nature
- Published
- 1995-08
- Volume
- 376
- Issue
- 6542
- Pages
- 690-695
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2087787002
- Cited by
- 438
- References
- 23
- FWCI
- 9.00
- Type
- journal article
- Language
- en
- Open access
- green
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- Ketchum, K. A., Joiner, W. J., Sellers, A. J., Kaczmarek, L. K., & Goldstein, S. A. N. (1995). A new family of outwardly rectifying potassium channel proteins with two pore domains in tandem. Nature. https://doi.org/10.1038/376690a0
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