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Your search keyword '"Two P domains"' showing total 6 results
Start Over Descriptor "Two P domains" Publication Year Range Last 50 years
6 results on '"Two P domains"'

1. Sequence and function of the two P domain potassium channels: implications of an emerging superfamily

Author

Goldstein, SAN, Wang, K-W, Ilan, Nitza, and Pausch, Mark H

Subjects
Medicinal and Biomolecular Chemistry, Chemical Sciences, Prevention, Amino Acid Sequence, Animals, Humans, Molecular Sequence Data, Potassium Channels, Structure-Activity Relationship, potassium channel, two P domains, TOK1, d-ORK1, HOHO1, h-TPKC1, Immunology, Medicinal and biomolecular chemistry
Abstract

A new superfamily of K+ channels has emerged in the past 2 years. Notable for possessing two pore-forming P domains in each subunit, members of the superfamily have been recognized through phylogeny from micro-organisms to humans. Four subfamilies of two P domain channels have been isolated thus far; among these are the first cloned examples of outward rectifier and open rectifier (or leak) K+ channels. The two P domain K+ channels offer a new perspective from which to glimpse the molecular basis for function and dysfunction of K+-selective ion channels.

Published
1998

2. ORK1, a potassium-selective leak channel with two pore domains cloned from Drosophila melanogaster by expression in Saccharomyces cerevisiae

Author

Goldstein, Steve AN, Price, Laura A, Rosenthal, David N, and Pausch, Mark H

Subjects
Genetics, 1.1 Normal biological development and functioning, Underpinning research, Generic health relevance, Amino Acid Sequence, Animals, Barium, Base Sequence, Cloning, Molecular, DNA, Complementary, Drosophila Proteins, Drosophila melanogaster, Female, Genetic Complementation Test, Membrane Potentials, Molecular Sequence Data, Oocytes, Plant Proteins, Potassium, Potassium Channels, Potassium Channels, Inwardly Rectifying, Saccharomyces cerevisiae, Sequence Homology, Amino Acid, Xenopus laevis, K+ channel, two P domains, yeast, muscles, nerves
Abstract

A K+ channel gene has been cloned from Drosophila melanogaster by complementation in Saccharomyces cerevisiae cells defective for K+ uptake. Naturally expressed in the neuromuscular tissues of adult flies, this gene confers K+ transport capacity on yeast cells when heterologously expressed. In Xenopus laevis oocytes, expression yields an ungated K(+)-selective current whose attributes resemble the "leak" conductance thought to mediate the resting potential of vertebrate myelinated neurons but whose molecular nature has long remained elusive. The predicted protein has two pore (P) domains and four membrane-spanning helices and is a member of a newly recognized K+ channel family. Expression of the channel in flies and yeast cells makes feasible studies of structure and in vivo function using genetic approaches that are not possible in higher animals.

Published
1996

3. The structure, function and distribution of the mouse TWIK-1 K+ channel

Author

Michel Fink, Inger Lauritzen, Catherine Heurteaux, Roberto V. Reyes, Florian Lesage, Fabrice Duprat, and Michel Lazdunski

Subjects
DNA, Complementary, Potassium Channels, Xenopus, Blotting, Western, Molecular Sequence Data, Biophysics, In situ hybridization, Biology, Biochemistry, Membrane Potentials, Mice, Potassium Channels, Tandem Pore Domain, Structural Biology, Genetics, medicine, Animals, Amino Acid Sequence, RNA, Messenger, Molecular Biology, Protein kinase C, In Situ Hybridization, Messenger RNA, Base Sequence, Quinine, Skeletal muscle, Brain, Cell Biology, biology.organism_classification, Molecular biology, Potassium channel, Cell biology, Molecular Weight, medicine.anatomical_structure, Cerebral cortex, Barium, Two P domains, Oocytes, Heterologous expression, Xenopus oocyte, Dimerization
Abstract

The two P domain K+ channel mTWIK-1 has been cloned from mouse brain. In Xenopus oocytes, mTWIK-1 currents are K+-selective, instantaneous, and weakly inward rectifying. These currents are blocked by Ba2+ and quinine, decreased by protein kinase C and increased by internal acidification. The apparent molecular weight of mTWIK-1 in brain is 81 kDa. A 40 kDa form is revealed after treatment with a reducing agent, strongly suggesting that native mTWIK-1 subunits dimerize via a disulfide bridge. TWIK-1 mRNA is expressed abundantly in brain and at lower levels in lung, kidney, and skeletal muscle. In situ hybridization shows that mTWIK-1 expression is restricted to a few brain regions, with the highest levels in cerebellar granule cells, brainstem, hippocampus and cerebral cortex.

Published
1997

4. Sequence and function of the two P domain potassium channels: implications of an emerging superfamily.

Author

Goldstein, SA, Goldstein, SA, Wang, KW, Ilan, N, Pausch, MH, Goldstein, SA, Goldstein, SA, Wang, KW, Ilan, N, and Pausch, MH

Abstract

A new superfamily of K+ channels has emerged in the past 2 years. Notable for possessing two pore-forming P domains in each subunit, members of the superfamily have been recognized through phylogeny from micro-organisms to humans. Four subfamilies of two P domain channels have been isolated thus far; among these are the first cloned examples of outward rectifier and open rectifier (or leak) K+ channels. The two P domain K+ channels offer a new perspective from which to glimpse the molecular basis for function and dysfunction of K+-selective ion channels.

Published
1998

5. ORK1, a potassium-selective leak channel with two pore domains cloned from Drosophila melanogaster by expression in Saccharomyces cerevisiae.

Author

Goldstein, SA, Goldstein, SA, Price, LA, Rosenthal, DN, Pausch, MH, Goldstein, SA, Goldstein, SA, Price, LA, Rosenthal, DN, and Pausch, MH

Abstract

A K+ channel gene has been cloned from Drosophila melanogaster by complementation in Saccharomyces cerevisiae cells defective for K+ uptake. Naturally expressed in the neuromuscular tissues of adult flies, this gene confers K+ transport capacity on yeast cells when heterologously expressed. In Xenopus laevis oocytes, expression yields an ungated K(+)-selective current whose attributes resemble the "leak" conductance thought to mediate the resting potential of vertebrate myelinated neurons but whose molecular nature has long remained elusive. The predicted protein has two pore (P) domains and four membrane-spanning helices and is a member of a newly recognized K+ channel family. Expression of the channel in flies and yeast cells makes feasible studies of structure and in vivo function using genetic approaches that are not possible in higher animals.

Published
1996

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