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Related Concept Videos

Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

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Voltage-gated ion channels are transmembrane proteins that open and close in response to changes in the membrane potential. They are present on the membranes of all electrically excitable cells such as neurons, heart, and muscle cells.
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The Role of Ion Channels in Neuronal Computation01:19

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A postsynaptic neuron usually receives numerous impulses from several other presynaptic neurons. The axon hillock of the postsynaptic neuron integrates all these signals and determines the likelihood of firing an action potential.
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Mechanically-gated Ion Channels01:12

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Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
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Non-gated Ion Channels01:24

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Ion channels are specialized proteins on the plasma membrane that allow charged ions to pass down their electrochemical gradient. Their main function is to maintain the membrane potential which is critical for cell viability. These channels are either gated or non-gated and can transport more than a thousand ions within milliseconds for the cellular event to occur.
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Ligand-Gated Ion Channel Receptor: Gating Mechanism

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Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
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The movement of ions like sodium, potassium, and calcium into and out of the cell is essential to maintain the electrochemical gradient in living cells. The ion channels—a class of membrane transport proteins—help maintain this ionic gradient for the smooth functioning of physiological activities such as maintaining cell size and volume, conducting nerve impulses, and gas and nutrient exchange.
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Related Experiment Video

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Recapitulation of an Ion Channel IV Curve Using Frequency Components
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Structure and physiological function of the human KCNQ1 channel voltage sensor intermediate state.

Keenan C Taylor1,2, Po Wei Kang3, Panpan Hou3

  • 1Department of Biochemistry, Vanderbilt University, Nashville, United States.

Elife
|February 26, 2020
PubMed
Summary

Researchers determined the intermediate structure of the human KCNQ1 voltage-gated potassium channel voltage sensor domain. This finding reveals how KCNQ1 channels contribute to cardiac and epithelial functions.

Keywords:
E. colielectrophysiologyion channelsmolecular biophysicssolution NMR spectroscopystructural biologyvoltage-gatingxenopus

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Area of Science:

  • Molecular Biology
  • Biophysics
  • Structural Biology

Background:

  • Voltage-gated ion channels are crucial for cellular electrical signaling.
  • Their voltage sensor domains (VSDs) cycle through resting, intermediate, and activated states.
  • The intermediate VSD conformation structure has been difficult to determine experimentally.

Purpose of the Study:

  • To determine the three-dimensional structure of the human KCNQ1 VSD in its intermediate state.
  • To functionally map the determinants of S4 helix motion during channel activation.
  • To demonstrate the physiological relevance of intermediate state KCNQ1 conductance.

Main Methods:

  • Experimental determination of the KCNQ1 VSD intermediate state structure.
  • Site-directed mutagenesis and electrophysiology in Xenopus laevis oocytes.
  • Voltage-clamp fluorometry.

Main Results:

  • The first experimental 3D structure of the human KCNQ1 VSD in the intermediate state was determined.
  • Key determinants of S4 helix movement from the intermediate to the activated state were identified.
  • Intermediate state conductance was shown to contribute to KCNQ1 channel function.

Conclusions:

  • This study elucidates the structure of the VSD intermediate state for KCNQ1.
  • The intermediate state's conductivity is vital for KCNQ1's dual role in cardiac (IKs) and epithelial currents.
  • Understanding this state provides insights into ion channel gating mechanisms and versatility.