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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.
Compared to the gated ion channels, the non-gated channels, also known as leakage or passive channels, have no gating mechanism....
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Ligand-gated Ion Channels01:19

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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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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.
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several types of...
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Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

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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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Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

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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G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

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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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Regulatory switch at the cytoplasmic interface controls TRPV channel gating.

Lejla Zubcevic1, William F Borschel1, Allen L Hsu2

  • 1Department of Biochemistry, Duke University School of Medicine, Durham, United States.

Elife
|May 10, 2019
PubMed
Summary

Temperature-sensitive transient receptor potential vanilloid (thermoTRPV) channels use a unique cytoplasmic ring for gating. This study reveals how rearrangements in this ring, particularly at the inter-protomer interface, control channel opening.

Keywords:
TRP channelcryo-electronmicroscopyelectrophysiologyhumanion channelligand dependent gatingmolecular biophysicssensitizationstructural biology

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biophysics

Background:

  • Temperature-sensitive transient receptor potential vanilloid (thermoTRPV) channels are crucial for physiological processes, activated by heat and ligands.
  • These channels feature a large cytoplasmic ring, comprising N-terminal ankyrin repeat domains (ARD) and C-terminal domains (CTD).
  • The unique cytoplasmic inter-protomer interface, with CTD coiled around a β-sheet contacting ARD, is implicated in function, but its gating mechanism remains unclear.

Purpose of the Study:

  • To elucidate the mechanism by which the cytoplasmic ring structure of thermoTRPV channels, specifically TRPV3, is involved in channel gating.
  • To investigate the role of the cytoplasmic inter-protomer interface in thermoTRPV channel function and subtype-specific properties.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine high-resolution structures.
  • Electrophysiological studies to assess channel activity and gating mechanisms.
  • Structural and functional analysis of the cytoplasmic ring and inter-protomer interface.

Main Results:

  • Cryo-EM and electrophysiology reveal that TRPV3 gating involves significant rearrangements at the cytoplasmic inter-protomer interface.
  • These rearrangements trigger coupling between cytoplasmic and transmembrane domains, initiating the channel opening process.
  • The study identifies the critical role of this interface in conferring distinct biophysical and physiological properties to different thermoTRPV subtypes.

Conclusions:

  • The cytoplasmic inter-protomer interface is a key regulatory site for thermoTRPV channel gating.
  • Structural rearrangements at this interface are essential for coupling thermal and ligand stimuli to channel opening.
  • Understanding this interface provides insights into the diverse functions and properties of thermoTRPV channels.