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Related Concept Videos

Channel Rhodopsins01:11

Channel Rhodopsins

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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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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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The eye is a spherical, hollow structure composed of three tissue layers. The outer layer — the fibrous tunic, comprises the sclera — a white structure — and the cornea, which is transparent. The sclera encompasses some of the ocular surface, most of which is not visible. However, the 'white of the eye' is distinctively visible in humans compared to other species. The cornea, a clear covering at the front of the eye, enables light penetration. The eye's middle...
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Vision is the result of light being detected and transduced into neural signals by the retina of the eye. This information is then further analyzed and interpreted by the brain. First, light enters the front of the eye and is focused by the cornea and lens onto the retina—a thin sheet of neural tissue lining the back of the eye. Because of refraction through the convex lens of the eye, images are projected onto the retina upside-down and reversed.
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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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Rhodopsin, light-sensor of vision.

Klaus Peter Hofmann1, Trevor D Lamb2

  • 1Institut für Medizinische Physik und Biophysik (CC2), Charité, and, Zentrum für Biophysik und Bioinformatik, Humboldt-Unversität zu Berlin, Berlin, 10117, Germany.

Progress in Retinal and Eye Research
|October 23, 2022
PubMed
Summary

Rhodopsin, the light sensor for low-light vision, efficiently captures photons to activate vision. This review details its structure, function, and role in phototransduction, highlighting areas needing further research.

Keywords:
ArrestinG protein-coupled receptorPhototransductionProtein structureReceptor activationReceptor shut-offRhodopsinRhodopsin kinaseRod photoreceptorTransducin

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Vision Science

Background:

  • Rhodopsin is the key G-protein-coupled receptor for vertebrate scotopic (low-light) vision.
  • It comprises a polypeptide chain bound to the chromophore 11-cis-retinal, possessing unique physicochemical properties.
  • Rhodopsin is stable in the dark but isomerizes its chromophore upon photon absorption, initiating phototransduction.

Purpose of the Study:

  • To review the properties and role of rhodopsin in rod phototransduction.
  • To examine rhodopsin's molecular structure, activation mechanisms, and function in both dark and active states.
  • To identify knowledge gaps and future research directions in understanding rhodopsin's contribution to scotopic vision.

Main Methods:

  • Review of existing literature on rhodopsin structure, function, and phototransduction.
  • Analysis of rhodopsin's photochemical and biochemical properties across different time scales.
  • Examination of molecular interactions governing rhodopsin's states and signaling.

Main Results:

  • Rhodopsin exhibits high photon absorption efficiency and rapid activation of its G-protein, transducin.
  • Photochemical events occur on the picosecond scale, while biochemical signaling and recovery take milliseconds to tens of minutes.
  • Detailed insights into rhodopsin's dark and active Meta states, and interactions with signaling partners.

Conclusions:

  • Rhodopsin's molecular properties are finely tuned for efficient phototransduction across a wide range of light intensities.
  • Despite advances, the precise link between rhodopsin's molecular interactions and scotopic vision properties requires further elucidation.
  • Significant research challenges remain in fully understanding rhodopsin's role in low-light vision.