TY - JOUR
T1 - Voltage sensor of ion channels and enzymes
AU - Gonzalez, Carlos
AU - Contreras, Gustavo F.
AU - Peyser, Alexander
AU - Larsson, Peter
AU - Neely, Alan
AU - Latorre, Ramón
N1 - Funding Information:
Acknowledgments Supported by Fondecyt grants 1110430 to R.L, 1980635 to A.N., and HL-095920 and American Heart Association Grant 10GRNT4150069 to H.P.L. The Centro Interdisciplinario de Neurociencia de Valparaíso is a Scientific Millennium Institute.
PY - 2012/3
Y1 - 2012/3
N2 - Placed in the cell membrane (a two-dimensional environment), ion channels and enzymes are able to sense voltage. How these proteins are able to detect the difference in the voltage across membranes has attracted much attention, and at times, heated debate during the last few years. Sodium, Ca2+ and K+ voltage-dependent channels have a conserved positively charged transmembrane (S4) segment that moves in response to changes in membrane voltage. In voltage-dependent channels, S4 forms part of a domain that crystallizes as a well-defined structure consisting of the first four transmembrane (S1-S4) segments of the channel-forming protein, which is defined as the voltage sensor domain (VSD). The VSD is tied to a pore domain and VSD movements are allosterically coupled to the pore opening to various degrees, depending on the type of channel. How many charges are moved during channel activation, how much they move, and which are the molecular determinants that mediate the electromechanical coupling between the VSD and the pore domains are some of the questions that we discuss here. The VSD can function, however, as a bona fide proton channel itself, and, furthermore, the VSD can also be a functional part of a voltage-dependent phosphatase.
AB - Placed in the cell membrane (a two-dimensional environment), ion channels and enzymes are able to sense voltage. How these proteins are able to detect the difference in the voltage across membranes has attracted much attention, and at times, heated debate during the last few years. Sodium, Ca2+ and K+ voltage-dependent channels have a conserved positively charged transmembrane (S4) segment that moves in response to changes in membrane voltage. In voltage-dependent channels, S4 forms part of a domain that crystallizes as a well-defined structure consisting of the first four transmembrane (S1-S4) segments of the channel-forming protein, which is defined as the voltage sensor domain (VSD). The VSD is tied to a pore domain and VSD movements are allosterically coupled to the pore opening to various degrees, depending on the type of channel. How many charges are moved during channel activation, how much they move, and which are the molecular determinants that mediate the electromechanical coupling between the VSD and the pore domains are some of the questions that we discuss here. The VSD can function, however, as a bona fide proton channel itself, and, furthermore, the VSD can also be a functional part of a voltage-dependent phosphatase.
KW - BK channels
KW - Cav Channels
KW - Kv channels
KW - Proton channels and VSP
KW - Voltage sensor
UR - http://www.scopus.com/inward/record.url?scp=84863977992&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84863977992&partnerID=8YFLogxK
U2 - 10.1007/s12551-011-0061-8
DO - 10.1007/s12551-011-0061-8
M3 - Review article
AN - SCOPUS:84863977992
VL - 4
SP - 1
EP - 15
JO - Biophysical Reviews
JF - Biophysical Reviews
SN - 1867-2450
IS - 1
ER -