Structure of cone photoreceptors

Mustafi, Debarshi; Engel, Andreas H.; Palczewski, Krzysztof

doi:10.1016/j.preteyeres.2009.05.003

Cited by 275Retinal Development and DisordersRetinal Diseases and TreatmentsPhotoreceptor and optogenetics research

Structure of cone photoreceptors

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Mustafi, Debarshi, Engel, Andreas H., Palczewski, Krzysztof·2009·Progress in Retinal and Eye Research

DOI 10.1016/j.preteyeres.2009.05.003PMC PMC2740621

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Abstract

Although outnumbered more than 20:1 by rod photoreceptors, cone cells in the human retina mediate daylight vision and are critical for visual acuity and color discrimination. A variety of human diseases are characterized by a progressive loss of cone photoreceptors but the low abundance of cones and the absence of a macula in non-primate mammalian retinas have made it difficult to investigate cones directly. Conventional rodents (laboratory mice and rats) are nocturnal rod-dominated species with few cones in the retina, and studying other animals with cone-rich retinas presents various logistic and technical difficulties. Originating in the early 1900s, past research has begun to provide insights into cone ultrastructure but has yet to afford an overall perspective of cone cell organization. This review summarizes our past progress and focuses on the recent introduction of special mammalian models (transgenic mice and diurnal rats rich in cones) that together with new investigative techniques such as atomic force microscopy and cryo-electron tomography promise to reveal a more unified concept of cone photoreceptor organization and its role in retinal diseases.

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Rhodopsin is the main protein of ROS disk and plasma membranes, making up 90% and 75% of their protein content respectively.
“Rhodopsin is the main component of disk and plasma membranes of ROS, accounting for 90 and 75% of their protein content.”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [235]
Section 2.2 states that rhodopsin comprises approximately 90% of the protein in rod disc membranes. It does not give the claimed 75% figure for rod outer-segment plasma membranes (page not provided). (LLM, conf=0.89)
Experimental — accuracy not yet measured
The opsin binding pocket modulates the photosensitivity of the 11-cis-retinylidene chromophore, producing visual pigments with different wavelength maxima and enabling color discrimination.
“The extreme photosensitivity of the 11-cis-retinylidene chromophore is modulated by the chemical environment of the opsin chromophore binding pocket, yielding different visual pigments that respond maximally to light at different wavelengths, causing the so-called “opsin shift” that allows us to discern differences in color.”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [235]

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“2; for review, see Mustafi et al., 2009) and make synaptic associations with secondary neurons such as bipolar cells in the outer plexiform layer (OPL).”
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Authors: Mustafi, D., Engel, A. H., & Palczewski, K.
Affiliations: Case Western Reserve University (US)
University of Basel (CH)
Corresponding author: Palczewski, Krzysztof
ORCID: Mustafi, Debarshi
Engel, Andreas H.
Palczewski, Krzysztof
Venue: Progress in Retinal and Eye Research
Publisher: Elsevier BV
Published: 2009-07
Volume: 28
Issue: 4
Pages: 289-302
ISSN: 1350-9462 (ISSN-L)
DOI: 10.1016/j.preteyeres.2009.05.003
PMC: PMC2740621
OpenAlex: W2153150479
Cited by: 275
References: 149
Citations by year: 2026: 20 · 2025: 27 · 2024: 30 · 2023: 33 · 2022: 12 · 2021: 20 · 2020: 15 · 2019: 14 · 2018: 14 · 2017: 13 · 2016: 14 · 2015: 13 · 2014: 9 · 2013: 13 · 2012: 8
FWCI: 0.71
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Progress in Retinal and Eye Research (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: Amgen
Case Western Reserve University
Medical College of Wisconsin
National Institutes of Health
National Eye Institute (EY 09339, EY019478-01, R01EY019478, T32EY007157, R01EY009339)
National Institute of General Medical Sciences (GM 079191, T32GM007250, R01GM079191)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinal Development and Disorders
Health Sciences › Medicine › Ophthalmology › Retinal Diseases and Treatments
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Photoreceptor and optogenetics research
Keywords: cone photoreceptors, photoreceptor ultrastructure, transgenic mice, retinal disease, color vision, visual acuity, cryo-electron tomography, atomic force microscopy
MeSH terms: Animals, Humans, Mice, Transgenic, Retinal Diseases, Vision, Ocular, Retinal Rod Photoreceptor Cells, Retinal Cone Photoreceptor Cells, Microscopy, Atomic Force, Models, Animal, Mice, Rats, Electron Microscope Tomography

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