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

Domains in macromolecular complexes are often considered structurally and functionally conserved while energetically coupled to each other. In the mod...
5MB Sizes 1 Downloads 10 Views

Recommend Documents

The Molecular Basis of Polyunsaturated Fatty Acid Interactions with the Shaker Voltage-Gated Potassium Channel.
Voltage-gated potassium (KV) channels are membrane proteins that respond to changes in membrane potential by enabling K+ ion flux across the membrane. Polyunsaturated fatty acids (PUFAs) induce channel opening by modulating the voltage-sensitivity, w

Functional diversity of potassium channel voltage-sensing domains.
Voltage-gated potassium channels or Kv's are membrane proteins with fundamental physiological roles. They are composed of 2 main functional protein domains, the pore domain, which regulates ion permeation, and the voltage-sensing domain, which is in

Purification and structural study of the voltage-sensor domain of the human KCNQ1 potassium ion channel.
KCNQ1 (also known as KV7.1 or KVLQT1) is a voltage-gated potassium channel modulated by members of the KCNE protein family. Among multiple functions, KCNQ1 plays a critical role in the cardiac action potential. This channel is also subject to inherit

Migration of PIP2 lipids on voltage-gated potassium channel surface influences channel deactivation.
Published studies of lipid-protein interactions have mainly focused on lipid binding to an individual site of the protein. Here, we show that a lipid can migrate between different binding sites in a protein and this migration modulates protein functi

Voltage-gated potassium channel antibody-associated limbic encephalitis.
We are emphasising the importance of considering a rare diagnosis, voltage-gated Potassium channel antibody-associated limbic encephalitis, in an 80-year-old gentleman who presented with memory impairment, seizure and hyponatraemia. He was found to h

Axonal dysfunction with voltage gated potassium channel complex antibodies.
Although autoantibodies targeted against voltage-gated potassium channel (VGKC)-associated proteins have been identified in limbic encephalitis (LE) and acquired neuromyotonia (aNMT), the role of these antibodies in disease pathophysiology has not be

The Thumb Domain Mediates Acid-sensing Ion Channel Desensitization.
Acid-sensing ion channels (ASICs) are cation-selective proton-gated channels expressed in neurons that participate in diverse physiological processes, including nociception, synaptic plasticity, learning, and memory. ASIC subunits contain intracellul

Cyclic expression of the voltage-gated potassium channel KV10.1 promotes disassembly of the primary cilium.
The primary cilium, critical for morphogenic and growth factor signaling, is assembled upon cell cycle exit, but the links between ciliogenesis and cell cycle progression are unclear. KV10.1 is a voltage-gated potassium channel frequently overexpress

Free-energy landscape of ion-channel voltage-sensor-domain activation.
Voltage sensor domains (VSDs) are membrane-bound protein modules that confer voltage sensitivity to membrane proteins. VSDs sense changes in the transmembrane voltage and convert the electrical signal into a conformational change called activation. A

Cation and voltage dependence of lidocaine inhibition of the hyperpolarization-activated cyclic nucleotide-gated HCN1 channel.
Lidocaine is known to inhibit the hyperpolarization-activated mixed cation current (Ih) in cardiac myocytes and neurons, as well in cells transfected with cloned Hyperpolarization-activated Cyclic Nucleotide-gated (HCN) channels. However, the molecul