Regulation of Metabolite Flux through Voltage-Gating of VDAC Channels

1997 ◽  
Vol 157 (3) ◽  
pp. 271-279 ◽  
Author(s):  
T. Hodge ◽  
M. Colombini
Keyword(s):  
Voltage Gating ◽  
Vdac Channels

Ion Selectivity Reversal and Induction of Voltage-Gating by Site-Directed Mutations in theParacoccus denitrificansPorin†

Biochemistry ◽  
1999 ◽  
Vol 38 (7) ◽  
pp. 2206-2212 ◽  
Author(s):  
Krishna Saxena ◽  
Viktoria Drosou ◽  
Elke Maier ◽  
Roland Benz ◽  
Bernd Ludwig
Keyword(s):  
Ion Selectivity ◽  
Voltage Gating

scholarly journals Acidic pH Uncovers Desensitization and Structurally-Distinct Types of Voltage Gating in CNGA1 Channels

2013 ◽  
Vol 104 (2) ◽  
pp. 279a
Author(s):  
Manuel Arcangeletti ◽  
Arin Marchesi ◽  
Monica Mazzolini ◽  
Vincent Torre
Keyword(s):  
Voltage Gating ◽  
Acidic Ph ◽  
Cnga1 Channels

Reversal of glibenclamide and voltage block of an epithelial KATP channel

1996 ◽  
Vol 271 (4) ◽  
pp. C1122-C1130 ◽  
Author(s):  
O. Mayorga-Wark ◽  
W. P. Dubinsky ◽  
S. G. Schultz
Keyword(s):  
Hydrophobic Interactions ◽  
Basolateral Membrane ◽  
Electrical Potential ◽  
Membrane Vesicles ◽  
Voltage Gating ◽  
Electrical Potential Difference ◽  
Outer Solution ◽  
Channel Inhibition ◽  
K Concentration ◽  
Voltage Gate

K+ channels present in basolateral membrane vesicles isolated from Necturus maculosa small intestinal cells and reconstituted into planar phospholipid bilayers are inhibited by MgATP and sulfonylurea derivatives, such as tolbutamide and glibenclamide, when these agents are added to the solution bathing the inner mouth of the channel. In addition, these channels possess an intrinsic "voltage gate" and are blocked when the electrical potential difference across the channel is oriented so that the inner solution is electrically positive with respect to the outer solution. We now show that increasing the concentration of permeant ions such as K+ or Rb+ in the outer solution reverses channel inhibition resulting from the addition of 50 microM glibenclamide to the inner solution and also inhibits intrinsic voltage gating; these effects are not elicited by increasing the concentrations of the relatively impermeant ions, Na+ or choline, in the outer solution. Furthermore, increasing the K+ concentration in the outer solution in the absence of glibenclamide inhibits voltage gating, and, under these conditions, the subsequent addition of glibenclamide to the inner solution is ineffective. These results are consistent with a model in which the voltage gate is an open-channel blocker whose action is directly reversed by elevating the external concentration of relatively permeant cations and where the action of glibenclamide is to stabilize the inactivated state of the channel, possibly through hydrophobic interactions.

scholarly journals Models of the Structure and Voltage-Gating Mechanism of the Shaker K+ Channel

2004 ◽  
Vol 87 (4) ◽  
pp. 2116-2130 ◽  
Author(s):  
Stewart R. Durell ◽  
Indira H. Shrivastava ◽  
H. Robert Guy
Keyword(s):  
Voltage Gating ◽  
K Channel ◽  
Gating Mechanism

scholarly journals Identification of a translocated gating charge in a voltage-dependent channel. Colicin E1 channels in planar phospholipid bilayer membranes.

1991 ◽  
Vol 98 (1) ◽  
pp. 77-93 ◽  
Author(s):  
C K Abrams ◽  
K S Jakes ◽  
A Finkelstein ◽  
S L Slatin
Keyword(s):  
Voltage Dependence ◽  
Ion Selectivity ◽  
Lipid Vesicles ◽  
Voltage Gating ◽  
Site Directed Mutagenesis ◽  
Phospholipid Bilayer ◽  
Voltage Gated ◽  
Colicin E1 ◽  
Gating Charge ◽  
Ion Conducting

The availability of primary sequences for ion-conducting channels permits the development of testable models for mechanisms of voltage gating. Previous work on planar phospholipid bilayers and lipid vesicles indicates that voltage gating of colicin E1 channels involves translocation of peptide segments of the molecule into and across the membrane. Here we identify histidine residue 440 as a gating charge associated with this translocation. Using site-directed mutagenesis to convert the positively charged His440 to a neutral cysteine, we find that the voltage dependence for turn-off of channels formed by this mutant at position 440 is less steep than that for wild-type channels; the magnitude of the change in voltage dependence is consistent with residue 440 moving from the trans to the cis side of the membrane in association with channel closure. The effect of trans pH changes on the ion selectivity of channels formed by the carboxymethylated derivative of the cysteine 440 mutant independently establishes that in the open channel state, residue 440 lies on the trans side of the membrane. On the basis of these results, we propose that the voltage-gated opening of colicin E1 channels is accompanied by the insertion into the bilayer of a helical hairpin loop extending from residue 420 to residue 459, and that voltage-gated closing is associated with the extrusion of this loop from the interior of the bilayer back to the cis side.

scholarly journals Spatial Structure of Zervamicin IIB Bound to DPC Micelles: Implications for Voltage-Gating

2002 ◽  
Vol 82 (2) ◽  
pp. 762-771 ◽  
Author(s):  
Z.O. Shenkarev ◽  
T.A. Balashova ◽  
R.G. Efremov ◽  
Z.A. Yakimenko ◽  
T.V. Ovchinnikova ◽  
...  
Keyword(s):  
Spatial Structure ◽  
Voltage Gating
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