Voltage-gated proton (Hv 1) channels, a singular voltage sensing domain

FEBS Letters ◽  
2015 ◽  
Vol 589 (22) ◽  
pp. 3471-3478 ◽  
Author(s):  
Karen Castillo ◽  
Amaury Pupo ◽  
David Baez-Nieto ◽  
Gustavo F. Contreras ◽  
Francisco J. Morera ◽  
...  
Keyword(s):  
Voltage Sensing ◽  
Voltage Gated ◽  
Voltage Sensing Domain

scholarly journals Voltage-Sensing Domain of Voltage-Gated Proton Channel Hv1 Shares Mechanism of Block with Pore Domains

Neuron ◽  
2013 ◽  
Vol 77 (2) ◽  
pp. 274-287 ◽  
Author(s):  
Liang Hong ◽  
Medha M. Pathak ◽  
Iris H. Kim ◽  
Dennis Ta ◽  
Francesco Tombola
Keyword(s):  
Proton Channel ◽  
Voltage Sensing ◽  
Voltage Gated ◽  
Voltage Sensing Domain ◽  
Pore Domains

scholarly journals The voltage-sensing domain of a phosphatase gates the pore of a potassium channel

2013 ◽  
Vol 141 (3) ◽  
pp. 389-395 ◽  
Author(s):  
Cristina Arrigoni ◽  
Indra Schroeder ◽  
Giulia Romani ◽  
James L. Van Etten ◽  
Gerhard Thiel ◽  
...  
Keyword(s):  
Electromechanical Coupling ◽  
K Channel ◽  
Modular Architecture ◽  
Voltage Sensing ◽  
Mode Shift ◽  
Voltage Gated ◽  
Kv Channels ◽  
Pore Properties ◽  
Voltage Sensing Domain

The modular architecture of voltage-gated K+ (Kv) channels suggests that they resulted from the fusion of a voltage-sensing domain (VSD) to a pore module. Here, we show that the VSD of Ciona intestinalis phosphatase (Ci-VSP) fused to the viral channel Kcv creates KvSynth1, a functional voltage-gated, outwardly rectifying K+ channel. KvSynth1 displays the summed features of its individual components: pore properties of Kcv (selectivity and filter gating) and voltage dependence of Ci-VSP (V1/2 = +56 mV; z of ∼1), including the depolarization-induced mode shift. The degree of outward rectification of the channel is critically dependent on the length of the linker more than on its amino acid composition. This highlights a mechanistic role of the linker in transmitting the movement of the sensor to the pore and shows that electromechanical coupling can occur without coevolution of the two domains.

scholarly journals The isolated voltage sensing domain of the Shaker potassium channel forms a voltage-gated cation channel

eLife ◽  
2016 ◽  
Vol 5 ◽  
Author(s):  
Juan Zhao ◽  
Rikard Blunck
Keyword(s):  
Transmembrane Helix ◽  
Voltage Sensing ◽  
Shaker Potassium Channel ◽  
Voltage Gated ◽  
Kv Channel ◽  
C Terminus ◽  
Ion Conducting ◽  
Voltage Gated Ion Channels ◽  
Voltage Sensing Domain ◽  
Pore Domain

Domains in macromolecular complexes are often considered structurally and functionally conserved while energetically coupled to each other. In the modular voltage-gated ion channels the central ion-conducting pore is surrounded by four voltage sensing domains (VSDs). Here, the energetic coupling is mediated by interactions between the S4-S5 linker, covalently linking the domains, and the proximal C-terminus. In order to characterize the intrinsic gating of the voltage sensing domain in the absence of the pore domain, the Shaker Kv channel was truncated after the fourth transmembrane helix S4 (Shaker-iVSD). Shaker-iVSD showed significantly altered gating kinetics and formed a cation-selective ion channel with a strong preference for protons. Ion conduction in Shaker-iVSD developed despite identical primary sequence, indicating an allosteric influence of the pore domain. Shaker-iVSD also displays pronounced 'relaxation'. Closing of the pore correlates with entry into relaxation suggesting that the two processes are energetically related.

scholarly journals Voltage-Sensing Domain of Voltage-Gated Proton Channel Hv1 Shares Mechanism of Block with Pore Domains

Neuron ◽  
2013 ◽  
Vol 79 (1) ◽  
pp. 202
Author(s):  
Liang Hong ◽  
Medha M. Pathak ◽  
Iris H. Kim ◽  
Dennis Ta ◽  
Francesco Tombola
Keyword(s):  
Proton Channel ◽  
Voltage Sensing ◽  
Voltage Gated ◽  
Voltage Sensing Domain ◽  
Pore Domains
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