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Cited by 28Photoreceptor and optogenetics researchRetinoids in leukemia and cellular processesRetinal Development and Disorders

Structural biology of 11- cis- retinaldehyde production in the classical visual cycle

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Daruwalla, Anahita, Choi, Elliot H., Palczewski, Krzysztof, Kiser, Philip D.·2018·Biochemical Journal
DOI 10.1042/bcj20180193PMC PMC6440480
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Abstract

The vitamin A derivative 11-cis-retinaldehyde plays a pivotal role in vertebrate vision by serving as the chromophore of rod and cone visual pigments. In the initial step of vision, a photon is absorbed by this chromophore resulting in its isomerization to an all-trans state and consequent activation of the visual pigment and phototransduction cascade. Spent chromophore is released from the pigments through hydrolysis. Subsequent photon detection requires the delivery of regenerated 11-cis-retinaldehyde to the visual pigment. This trans–cis conversion is achieved through a process known as the visual cycle. In this review, we will discuss the enzymes, binding proteins and transporters that enable the visual pigment renewal process with a focus on advances made during the past decade in our understanding of their structural biology.

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  • RDH8 contributes approximately 70% and RDH12 approximately 30% of all-trans-RDH activity.

    “RDH8 contributes to approximately 70% and RDH12 to approximately 30% of all-trans-RDH activity.”

    From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [150]

    The Retinol Dehydrogenases section says RDH8 is the main contributor to all-trans-retinaldehyde reduction in photoreceptors and RDH12 contributes up to 30% of RDH activity. It does not give RDH8 a 70% share, and “up to 30%” does not establish an approximately 30% share in all conditions. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • Pathogenic variants in RLBP1 are associated with autosomal recessive retinal dystrophies including RP, fundus albipunctatus, Bothnia dystrophy, Newfoundland rod-cone dystrophy, and retinitis punctata albescens.

    “They have been associated with a number of autosomal recessive retinal dystrophies, including RP, fundus albipunctatus, Bothnia dystrophy, Newfoundland rod-cone dystrophy and retinitis punctata albescens [150,159,160].”

    From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [150]

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Authors
Daruwalla, A., Choi, E. H., Palczewski, K., & Kiser, P. D.
Affiliations
  • Case Western Reserve University (US)
  • Louis Stokes Cleveland VA Medical Center (US)
Corresponding author
Palczewski, Krzysztof
ORCID
Venue
Biochemical Journal
Publisher
Portland Press Ltd.
Published
2018-10-23
Volume
475
Issue
20
Pages
3171-3188
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
DOI
10.1042/bcj20180193
PMC
PMC6440480
OpenAlex
W2896298468
Cited by
28
References
152
Citations by year
2026: 3 · 2025: 4 · 2024: 4 · 2023: 5 · 2022: 2 · 2021: 4 · 2020: 5 · 2019: 1
FWCI
0.32
Type
journal article
Language
en
Open access
Locations
  • Biochemical Journal (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
  • eScholarship (California Digital Library) (submittedVersion)
Funders
  • U.S. Department of Veterans Affairs (IK2BX002683)
  • National Eye Institute (R24EY027283, U01EY025451, R01EY009339)
  • National Institute of General Medical Sciences (T32GM007250)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Photoreceptor and optogenetics research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinoids in leukemia and cellular processes
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinal Development and Disorders
Keywords
visual cycle, retinal regeneration, visual pigments, chromophores, retinal isomerization, all-trans-retinal, retinal-binding proteins, vitamin A, phototransduction, rod and cone photoreceptors, enzyme structure
MeSH terms
Amino Acid Sequence, Animals, Humans, Retinal Pigments, Retinaldehyde, Vision, Ocular, Protein Structure, Secondary, Crystallography, X-Ray, Retinal Pigment Epithelium

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