Consequences of dimerization of the voltage-gated proton channel.
Consequences of dimerization of the voltage-gated proton channel.
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DOI:
10.1016/b978-0-12-386931-9.00012-x
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发表时间:
2013
影响因子:
--
通讯作者:
DeCoursey, Thomas E.
中科院分区:
文献类型:
--
作者:
Smith, Susan M. E.;DeCoursey, Thomas E.
The human voltage gated proton channel, hHV1, appears to exist mainly as a dimer. Teleologically, this is puzzling, because each protomer retains the main properties that characterize this protein: proton conduction that is regulated by conformational (channel opening and closing) changes that occur in response to both voltage and pH. The HV1 dimer is mainly linked by C terminal coiled-coil interactions. Several types of mutations produce monomeric constructs that open ~5 times faster than the WT dimeric channel, but with weaker voltage dependence. Intriguingly, the quintessential function of the HV1 dimer, opening to allow H+ conduction, occurs cooperatively. Both protomers undergo a conformational change, but both must undergo this transition before either can conduct. The teleological purpose of dimerization may be to steepen the voltage-dependence of channel opening, at least in phagocytes. In other cells, the purpose is not understood. Finally, several single-celled species have HV that are likely monomeric.