Structure and Dynamics of the Mthk K+ Channel Selectivity Filter during Gating
نویسندگان
چکیده
منابع مشابه
Voltage-dependent inactivation gating at the selectivity filter of the MthK K+ channel
Voltage-dependent K(+) channels can undergo a gating process known as C-type inactivation, which involves entry into a nonconducting state through conformational changes near the channel's selectivity filter. C-type inactivation may involve movements of transmembrane voltage sensor domains, although the mechanisms underlying this form of inactivation may be heterogeneous and are often unclear. ...
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In MthK, a Ca2+-gated K+ channel from Methanobacterium thermoautotrophicum, eight cytoplasmic RCK domains form an octameric gating ring that controls the intracellular gate of the ion conduction pore. The binding of Ca2+ ions to the RCK domains alters the conformation of the gating ring, thereby opening the gate. In the present study, we examined the Ca2+- and pH-regulated gating and the rectif...
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Ion channel opening and closing are fundamental to cellular signalling and homeostasis. Gates that control K(+) channel activity were found both at an intracellular pore constriction and within the selectivity filter near the extracellular side but the specific location of the gate that opens Ca(2+)-activated K(+) channels has remained elusive. Using the Methanobacterium thermoautotrophicum hom...
متن کاملAllosteric mechanism of Ca2+ activation and H+-inhibited gating of the MthK K+ channel
MthK is a Ca(2+)-gated K(+) channel whose activity is inhibited by cytoplasmic H(+). To determine possible mechanisms underlying the channel's proton sensitivity and the relation between H(+) inhibition and Ca(2+)-dependent gating, we recorded current through MthK channels incorporated into planar lipid bilayers. Each bilayer recording was obtained at up to six different [Ca(2+)] (ranging from ...
متن کاملThe Desensitization Gating of the MthK K+ Channel Is Governed by Its Cytoplasmic Amino Terminus
The RCK-containing MthK channel undergoes two inactivation processes: activation-coupled desensitization and acid-induced inactivation. The acid inactivation is mediated by the C-terminal RCK domain assembly. Here, we report that the desensitization gating is governed by a desensitization domain (DD) of the cytoplasmic N-terminal 17 residues. Deletion of DD completely removes the desensitizatio...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2015
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2014.11.669