[Biophysical and Biochemical Research of Animal Rhodopsins]

Yakugaku Zasshi. 2021;141(10):1155-1160. doi: 10.1248/yakushi.21-00144.
[Article in Japanese]

Abstract

Opsins (also called animal rhodopsins) are universal photoreceptive proteins that provide the molecular basis of visual and nonvisual photoreception in animals, including humans. Opsins consist of seven helical α-transmembrane domains and use retinal, a derivative of vitamin A, as a chromophore. In many opsins, light absorption triggers photo-isomerization from 11-cis retinal to all-trans retinal, resulting in activation via dynamic structural changes in the protein moiety. Activated opsins stimulate cognate trimeric G proteins to induce signal transduction cascades in cells. Recently, molecular and physiological analyses of diverse opsins have progressively advanced. This review introduces the molecular basis and physiological functions of opsins. Based on the functions of opsins, I will discuss the potential of opsins as target molecules to treat and prevent visual and nonvisual diseases such as sleep disorder and depression.

Keywords: G protein coupled receptor; opsin; retinal; rhodopsin; vision.

Publication types

  • Review

MeSH terms

  • Amino Acid Motifs
  • Animals
  • Biophysical Phenomena
  • Depression / etiology
  • Depression / prevention & control
  • Depression / therapy
  • GTP-Binding Proteins / metabolism
  • Humans
  • Molecular Targeted Therapy
  • Mutation
  • Opsins / chemistry*
  • Opsins / genetics
  • Opsins / physiology*
  • Protein Domains
  • Receptors, G-Protein-Coupled / metabolism
  • Retinaldehyde / chemistry
  • Rhodopsin
  • Signal Transduction
  • Sleep Wake Disorders / etiology
  • Sleep Wake Disorders / prevention & control
  • Sleep Wake Disorders / therapy
  • Vision Disorders / etiology
  • Vision Disorders / prevention & control
  • Vision Disorders / therapy
  • Vision, Ocular / physiology*

Substances

  • Opsins
  • Receptors, G-Protein-Coupled
  • Rhodopsin
  • GTP-Binding Proteins
  • Retinaldehyde