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Related Concept Videos

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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Mechanically-gated Ion Channels01:12

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Ion Channels01:19

Ion Channels

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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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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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Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

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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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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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Updated: Mar 24, 2026

One-channel Cell-attached Patch-clamp Recording
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Human PIEZO1 Ion Channel Functions as a Split Protein.

Chilman Bae1, Thomas M Suchyna1, Lynn Ziegler1

  • 1Department of Physiology and Biophysics, 302 Cary Hall, State University of New York at Buffalo, Buffalo, NY, United States of America.

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Co-expressing two segments of the PIEZO1 channel protein restores its function. This indicates that both halves are necessary for forming a functional mechanosensitive ion channel.

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Area of Science:

  • Molecular Biology
  • Biophysics
  • Cell Biology

Background:

  • PIEZO1 is a mechanosensitive ion channel critical for cellular mechanotransduction.
  • Previous work demonstrated functional fluorescent protein insertion into the hPIEZO1 sequence.
  • The functional domains of PIEZO1 and their necessity for channel activity remain incompletely understood.

Purpose of the Study:

  • To determine if co-expression of split PIEZO1 protein segments reconstitutes a functional mechanosensitive channel.
  • To investigate whether channel gating and ion permeation are localized to specific segments.
  • To confirm the association of the split PIEZO1 domains.

Main Methods:

  • Expressing split hPIEZO1 channel protein segments (1-1591 and 1592-2521) using a bicistronic plasmid in HEK293 cells.
  • Performing whole-cell, cell-attached, and outside-out patch-clamp electrophysiology to measure channel currents.
  • Utilizing Förster Resonance Energy Transfer (FRET) measurements to confirm protein segment association.

Main Results:

  • Co-expression of the two hPIEZO1 segments resulted in the formation of a functional mechanosensitive channel, as evidenced by patch-clamp recordings.
  • Neither individual segment, when expressed alone, produced measurable currents.
  • FRET measurements confirmed the association of the N-terminal and C-terminal segments.
  • Electrophysiological data revealed voltage-dependent inactivation and altered activation kinetics compared to wild-type PIEZO1.

Conclusions:

  • The PIEZO1 channel requires the association of both its N-terminal and C-terminal domains for functional activity.
  • Neither segment alone contains the complete machinery for channel gating and ion permeation.
  • This study provides critical insights into the structural and functional organization of the PIEZO1 mechanosensitive channel.