ArticlePflugers Archiv : European journal of physiology2005
In the yeast potassium channel, Tok1p, the external ring of aspartate residues modulates both gating and conductance.
Article in Pflugers Archiv : European journal of physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- TOK channels use the two gates in classical KFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Article
- A structural model for K2P potassium channels based on 23 pairs of interacting sites and continuum electrostatics.The Journal of general physiology · 2009Article
- Functional consequences of leucine and tyrosine mutations in the dual pore motifs of the yeast K(+) channel, Tok1p.Pflugers Archiv : European journal of physiology · 2008Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
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Abstract
The yeast plasma-membrane potassium channel, Tok1p, is a voltage-dependent outward rectifier, the gating and steady-state conductance of which are conspicuously modulated by extracellular [K(+)] ([K(+)](o)). Activation is slow at high [K(+)](o), showing time constants (tau(a)) of approximately 90 ms when [K(+)](o) is 150 mM (depolarizing step to +100 mV), and inactivation is weak (<30%) during sustained depolarization. Lowering [K(+)](o) accelerates activation, increases peak current, and enhances inactivation, so that at 15 mM [K(+)](o) tau(a) is less than 50 ms and inactivation suppresses approximately 60% of peak current. Two negative residues, Asp292 and Asp426, near the mouth of the assembled channel, modulate both kinetics and conductance of the channel. Charge neutralization in the mutant Asp292Asn allows fast activation (tau(a) approximately 20 ms) at high [K(+)](o), peak currents diminishing with decreasing [K(+)](o), and fast, nearly complete, inactivation. The voltage dependence of tau(a) persists in the mutant, but the [K(+)](o) dependence almost disappears. Similar but smaller changes are seen in the Asp426Asn mutant, implying that pore geometry in the functional channel has twofold, not fourfold, symmetry.
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Registered trials
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