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Vitamin A₁/A₂ chromophore exchange: Its role in spectral tuning and visual plasticity.

ABSTRACT: Vertebrate rod and cone photoreceptors detect light via a specialized organelle called the outer segment. This structure is packed with light-sensitive molecules known as visual pigments that consist of a G-protein-coupled, seven-transmembrane protein known as opsin, and a chromophore prosthetic group, either 11-cis retinal ('A₁') or 11-cis 3,4-didehydroretinal ('A₂'). The enzyme cyp27c1 converts A₁ into A₂ in the retinal pigment epithelium. Replacing A₁ with A₂ in a visual pigment red-shifts its spectral sensitivity and broadens its bandwidth of absorption at the expense of decreased photosensitivity and increased thermal noise. The use of vitamin A₂-based visual pigments is strongly associated with the occupation of aquatic habitats in which the ambient light is red-shifted. By modulating the A₁/A₂ ratio in the retina, an organism can dynamically tune the spectral sensitivity of the visual system to better match the predominant wavelengths of light in its environment. As many as a quarter of all vertebrate species utilize A₂, at least during a part of their life cycle or under certain environmental conditions. A₂ utilization therefore represents an important and widespread mechanism of sensory plasticity. This review provides an up-to-date account of the A₁/A₂ chromophore exchange system.

SUBMITTER: Corbo JC

PROVIDER: S-EPMC8900494 | biostudies-literature |

REPOSITORIES: biostudies-literature

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