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Related Concept Videos

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Most organisms use photoreceptors to sense and respond to light. Examples of photoreceptors include bacteriorhodopsins and bacteriophytochromes in some bacteria, phytochromes in plants, and rhodopsins in the photoreceptor cells of the vertebral retina. The light-sensitive property of these receptors is because of the bound chromophores, such as bilin in the phytochromes and retinal in the rhodopsins.
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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.
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At the molecular level, visual signals trigger transformations in photopigment molecules, resulting in changes in the photoreceptor cell's membrane potential. The photon's energy level is denoted by its wavelength, with each specific wavelength of visible light associated with a distinct color. The spectral range of visible light, classified as electromagnetic radiation, spans from 380 to 720 nm. Electromagnetic radiation wavelengths exceeding 720 nm fall under the infrared category,...
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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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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.
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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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Structure-function analysis suggests that the photoreceptor LITE-1 is a light-activated ion channel.

Sonya M Hanson1, Jan Scholüke2, Jana Liewald2

  • 1Center for Computational Biology and Center for Computational Mathematics, Flatiron Institute, Simons Foundation, 162 5th Avenue, New York, NY 10010, USA; Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt, Germany.

Current Biology : CB
|August 1, 2023
PubMed
Summary

The nematode LITE-1 protein detects light using tryptophans and a chromophore, acting as a photon and H2O2 coincidence detector to control ion channels for escape behavior.

Keywords:
AlphaFold2Caenorhabditis elegansUV-sensorchromophoregustatory receptorhydrogen peroxideion channelmolecular dynamics simulationnociceptorphotosensor

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Light sensation is crucial for organism survival.
  • The nematode Caenorhabditis elegans uses the photosensor LITE-1 for UV and blue light detection, triggering escape responses.
  • LITE-1 absorbs UV photons efficiently through essential tryptophan residues.

Purpose of the Study:

  • To model the structure and dynamics of LITE-1 using computational and experimental methods.
  • To characterize LITE-1's function, including light absorption, channel gating, and photo-oxidation mechanisms.
  • To identify the chromophore binding site and understand the photon-induced signaling pathway.

Main Methods:

  • AlphaFold2-multimer modeling and molecular dynamics (MD) simulations.
  • Mutational and behavioral assays in C. elegans.
  • Electrophysiological recordings to assess LITE-1's function as a photon and H2O2 detector.

Main Results:

  • LITE-1 structure resembles insect olfactory and gustatory receptors, functioning as tetrameric ion channels.
  • Identified key residues for channel gating, light absorption, and photo-oxidation, including a potential PRDX-2 binding site.
  • Discovered a chromophore binding pocket with a critical cysteine attachment site, elucidating the photon-induced conformational changes and channel gating mechanism.

Conclusions:

  • LITE-1 functions as a photon and hydrogen peroxide (H2O2) coincidence detector.
  • The protein fold and assembly, similar to insect chemoreceptors, may have evolved into a light-activated ion channel.
  • Related proteins like C. elegans GUR-3 likely employ similar photon detection mechanisms.