scholarly journals Voltage-dependent gating of KCNH potassium channels lacking a covalent link between voltage-sensing and pore domains

2015 ◽  
Vol 6 (1) ◽  
Author(s):  
Éva Lörinczi ◽  
Juan Camilo Gómez-Posada ◽  
Pilar de la Peña ◽  
Adam P. Tomczak ◽  
Jorge Fernández-Trillo ◽  
...  
Keyword(s):  
Potassium Channels ◽  
Voltage Sensing ◽  
Voltage Dependent ◽  
Pore Domains

scholarly journals Unconventional voltage sensing in an inwardly rectifying potassium channel

2021 ◽  
Vol 153 (6) ◽  
Author(s):  
Harley T. Kurata
Keyword(s):  
Potassium Channels ◽  
Potassium Channel ◽  
Voltage Dependence ◽  
Voltage Sensing ◽  
Inwardly Rectifying Potassium Channel ◽  
Inwardly Rectifying Potassium Channels ◽  
Voltage Dependent ◽  
Inwardly Rectifying ◽  
Surprising Finding ◽  
Heteromeric Channels

Inwardly rectifying potassium channels are generally thought to achieve their physiological voltage dependence via an “extrinsic” mechanism involving voltage-dependent block by polyamines. A surprising finding of polyamine-independent gating of Kir4.1/Kir5.1 heteromeric channels suggests a mechanism of voltage dependence arising from interactions with permeating ions.

scholarly journals Interaction between tetraethylammonium and amino acid residues in the pore of cloned voltage-dependent potassium channels.

1991 ◽  
Vol 266 (12) ◽  
pp. 7583-7587
Author(s):  
M P Kavanaugh ◽  
M D Varnum ◽  
P B Osborne ◽  
M J Christie ◽  
A E Busch ◽  
...  
Keyword(s):  
Amino Acid ◽  
Potassium Channels ◽  
Amino Acid Residues ◽  
Voltage Dependent

scholarly journals Activation-inactivation of potassium channels and development of the potassium-channel spike in internally perfused squid giant axons.

1981 ◽  
Vol 78 (1) ◽  
pp. 43-61 ◽  
Author(s):  
I Inoue
Keyword(s):  
Potassium Channels ◽  
Potassium Channel ◽  
Voltage Clamp ◽  
Time Constant ◽  
Equilibrium Potential ◽  
Giant Axons ◽  
Dependent Inactivation ◽  
Voltage Dependent ◽  
Time Courses ◽  
Calcium Permeability

A spike that is the result of calcium permeability through potassium channels was separated from the action potential is squid giant axons internally perfused with a 30 mM NaF solution and bathed in a 100 mM CaCl2 solution by blocking sodium channels with tetrodotoxin. Currents through potassium channels were studied under voltage clamp. The records showed a clear voltage-dependent inactivation of the currents. The inactivation was composed of at least two components; one relatively fast, having a time constant of 20--30 ms, and the other very slow, having a time constant of 5--10 s. Voltage clamp was carried out with a variety of salt compositions in both the internal and external solutions. A similar voltage-dependent inactivation, also composed of the two components, was recognized in all the current through potassium channels. Although the direction and intensity of current strongly depended on the salt composition of the solutions, the time-courses of these currents at corresponding voltages were very similar. These results strongly suggest that the inactivation of the currents in attributable to an essential, dynamic property of potassium channels themselves. Thus, the generation of a potassium-channel spike can be understood as an event that occurs when the equilibrium potential across the potassium channel becomes positive.

scholarly journals Structural mechanism of voltage-dependent gating in an isolated voltage-sensing domain

2014 ◽  
Vol 21 (3) ◽  
pp. 244-252 ◽  
Author(s):  
Qufei Li ◽  
Sherry Wanderling ◽  
Marcin Paduch ◽  
David Medovoy ◽  
Abhishek Singharoy ◽  
...  
Keyword(s):  
Voltage Sensing ◽  
Structural Mechanism ◽  
Voltage Dependent ◽  
Voltage Sensing Domain

scholarly journals Role of L‐type voltage dependent calcium and large conductance potassium channels in adenosine A 1 receptor mediated vasoconstriction through Cyp4a

2012 ◽  
Vol 26 (S1) ◽  
Author(s):  
Swati S Kunduri ◽  
Mohammed A Nayeem ◽  
Dovenia S Ponnoth ◽  
Stephen Tilley ◽  
S. Jamal Mustafa
Keyword(s):  
Potassium Channels ◽  
Voltage Dependent

Blockade of two voltage-dependent potassium channels, mKv1.1 and mKv1.2, by docosahexaenoic acid

1996 ◽  
Vol 314 (3) ◽  
pp. 393-396 ◽  
Author(s):  
Jennifer C. Garratt ◽  
Matthew P. McEvoy ◽  
David G. Owen
Keyword(s):  
Potassium Channels ◽  
Docosahexaenoic Acid ◽  
Voltage Dependent
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