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Patch clamp studies of the potassium-transport proteins TRK1,2 in Saccharomyces cerevisiae have revealed large chloride efflux currents: at clamp voltages negative to -100 mV, and intracellular chloride concentrations &gt;10 mM (J. Membr. Biol. 198:177, 2004). Stationary-state current-voltage analysis led to an in-series two-barrier model for chloride activation: the lower barrier (α) being 10-13 kcal/mol located ~30% into the membrane from the cytoplasmic surface; and the higher one (β) being 12-16 kcal/mol located at the outer surface. Measurements carried out with lyotrophic anions and osmoprotective solutes have now demonstrated the following new properties: (1) selectivity for highly permeant anions changes with extracellular pH; at pH(o)= 5.5: I(-)≈ Br(-) &gt;Cl(-) &gt;SCN(-) &gt;NO (3)(-) , and at pH(o) 7.5: I(-)≈ Br(-) &gt; SCN(-) &gt; NO(3)(-) &gt;Cl(-). (2) NO(2)(-) acts like "superchoride", possibly enhancing the channel's intrinsic permeability to Cl(-). (3) SCN(-) and NO(3)(-) block chloride permeability. (4) The order of selectivity for several slightly permeant anions (at pH(o)= 5.5 only) is formate&gt;gluconate&gt;acetate&gt;&gt;phosphate(-1). (5) All anion conductances are modulated (choked) by osmoprotective solutes. (6) The data and descriptive two-barrier model evoke a hypothetical structure (Biophys. J. 77:789, 1999) consisting of an intramembrane homotetramer of fungal TRK molecules, arrayed radially around a central cluster of four single helices (TM7) from each monomer. (7) That tetrameric cluster would resemble the hydrophobic core of (pentameric) ligand-gated ion channels, and would suggest voltage-modulated hydrophobic gating to underlie anion permeation.

Anion currents in yeast K+ transporters (TRK) characterize a structural homologue of ligand-gated ion channels