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Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

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...
Non-gated Ion Channels01:24

Non-gated Ion Channels

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.
Non-gated Ion Channels01:24

Non-gated Ion Channels

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.
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

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 include the...
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

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 include the...
G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

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 organs,...

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Related Experiment Video

Updated: Jun 2, 2026

Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability
12:26

Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability

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pH-dependent gating in a FocA formate channel.

Wei Lü1, Juan Du, Tobias Wacker

  • 1Lehrstuhl für Biochemie, Institut für organische Chemie und Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104 Freiburg, Germany.

Science (New York, N.Y.)
|April 16, 2011
PubMed
Summary

The formate transporter FocA switches function with pH changes. Structural and electrophysiological studies reveal pH-dependent gating mechanisms in this crucial formate/H(+) channel.

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • The formate transporter FocA facilitates formate and proton transport across cell membranes.
  • FocA exhibits pH-dependent functional switching, operating as an exporter at high pH and an importer at low pH.

Purpose of the Study:

  • To elucidate the structural and mechanistic basis of FocA's pH-dependent gating and functional switch.
  • To understand how proton concentration influences the transport activity of FocA.

Main Methods:

  • X-ray crystallography of Salmonella typhimurium FocA at pH 4.0.
  • Electrophysiological studies at varying pH levels (pH 7.0 and 5.1).

Main Results:

  • The crystal structure revealed major rearrangements in the amino termini of FocA protomers at low pH.
  • These rearrangements involve amino-terminal helices that cooperatively open or block the channel.
  • Electrophysiology confirmed FocA functions as a specific formate channel at pH 7.0 and closes at pH 5.1.

Conclusions:

  • FocA gating is a pH-dependent process mediated by concerted conformational changes in its amino-terminal helices.
  • The structural insights explain the observed functional switch from passive export to active import.
  • This provides a molecular mechanism for pH-regulated transport in FocA.