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Related Concept Videos

Non-gated Ion Channels01:24

Non-gated Ion Channels

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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 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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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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G-Protein Gated Ion Channels01:21

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GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory...
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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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Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

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Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that...
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Related Experiment Video

Updated: Mar 9, 2026

Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4
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Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4

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A conserved gating element in TRPV6 channels.

Laura Hofmann1, Hongmei Wang1, Andreas Beck1

  • 1Experimentelle und Klinische Pharmakologie und Toxikologie, Universität des Saarlandes, 66421 Homburg, Germany.

Cell Calcium
|December 29, 2016
PubMed
Summary
This summary is machine-generated.

Mutations in the TRPV6 channel

Keywords:
Calcium influxChannel gatingIon channelSignal transductionTRPV6Transient receptor potential

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Purification and Reconstitution of TRPV1 for Spectroscopic Analysis
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Purification and Reconstitution of TRPV1 for Spectroscopic Analysis
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Area of Science:

  • Molecular Biology
  • Ion Channel Physiology
  • Biophysics

Background:

  • The Ca2+-selective Transient Receptor Potential Vanilloid 6 (TRPV6) channel plays a crucial role in calcium homeostasis.
  • TRPV6 exhibits constitutive activity that is subject to Ca2+-induced inactivation.
  • Inactivation mechanisms involve phospholipase C activation, phosphatidylinositol 4,5-bisphosphate depletion, and calmodulin binding.

Purpose of the Study:

  • To investigate the role of specific residues in the cytosolic S4-S5 linker and S6-TRP-domain linker in TRPV6 channel gating.
  • To determine how mutations in these linkers affect channel conformation, activity, and inactivation.

Main Methods:

  • Site-directed mutagenesis was used to introduce specific amino acid substitutions in the human TRPV6 protein (G516S and T621A).
  • Electrophysiological recordings were performed to assess channel activity and Ca2+ currents.
  • Analysis was informed by the crystal structure of the rat TRPV6 channel.

Main Results:

  • Replacing glycine 516 with serine (G516S) in the S4-S5 linker resulted in a constitutively open TRPV6 channel conformation, enhancing Ca2+ entry and preventing inactivation.
  • A secondary mutation (T621A) in the S6-TRP-domain linker partially rescued the TRPV6 function by reducing constitutive activity.
  • Structural data indicated that T621 is located near the S6-TRP-domain linker, suggesting its involvement in channel gating.

Conclusions:

  • The S4-S5 linker and the S6-TRP-domain linker are critical for TRPV6 channel gating.
  • Alterations in these linker regions can lead to constitutive Ca2+ entry by disrupting normal channel gating mechanisms.