ArticleThe EMBO journal1998
Mutations in the pore regions of the yeast K+ channel YKC1 affect gating by extracellular K+.
Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 27 citations in OpenAlex.
- Voltage-sensor transitions of the inward-rectifying K+ channel KAT1 indicate a latching mechanism biased by hydration within the voltage sensor.Plant physiology · 2014Article
- Clustering of the K+ channel GORK of Arabidopsis parallels its gating by extracellular K+.The Plant journal : for cell and molecular biology · 2014Article
- Selective mobility and sensitivity to SNAREs is exhibited by the Arabidopsis KAT1 K+ channel at the plasma membrane.The Plant cell · 2006Article
- Interactive domains between pore loops of the yeast K+ channel TOK1 associate with extracellular K+ sensitivity.The Biochemical journal · 2006Article
- Regulation of the fast vacuolar channel by cytosolic and vacuolar potassium.Biophysical journal · 2003Article
- Outer pore residues control the H(+) and K(+) sensitivity of the Arabidopsis potassium channel AKT3.The Plant cell · 2002Article
- Regulation of ROMK by extracellular cations.Biophysical journal · 2001Article
- Ca2+ channels at the plasma membrane of stomatal guard cells are activated by hyperpolarization and abscisic acid.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The product of the Saccharomyces cerevisiae K+-channel gene YKC1 includes two pore-loop sequences that are thought to form the hydrophilic lining of the pore. Gating of the channel is promoted by membrane depolarization and is regulated by extracellular K+ concentration ([K+]o) both in the yeast and when expressed in Xenopus oocytes. Analysis of the wild-type current now shows that: (i) [K+]o suppresses a very slowly relaxing component, accelerating activation; (ii) [K+]o slows deactivation in a dose-dependent fashion; and (iii) Rb+, Cs+ and, to a lesser extent, Na+ substitute for K+ in its action on gating. We have identified single residues, L293 and A428, at equivalent positions within the two pore loops that affect the [K+]o sensitivity. Substitution of these residues gave channels with reduced sensitivity to [K+]o in macroscopic current kinetics and voltage dependence, but had only minor effects on selectivity among alkali cations in gating and on single-channel conductance. In some mutants, activation was slowed sufficiently to confer a sigmoidicity to current rise at low [K+]o. The results indicate that these residues are involved in [K+]o sensing. Their situation close to the permeation pathway points to an interaction between gating and permeation.
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