Cited by 975Circadian rhythm and melatoninmelanin and skin pigmentationPhotoreceptor and optogenetics research

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Melanopsin: An opsin in melanophores, brain, and eye

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Provencio, Ignacio, Jiang, Guisen, De Grip, Willem J., Hayes, William Pär, Rollag, Mark D.·1998·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.95.1.340PMC PMC18217

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Abstract

We have identified an opsin, melanopsin, in photosensitive dermal melanophores of Xenopus laevis . Its deduced amino acid sequence shares greatest homology with cephalopod opsins. The predicted secondary structure of melanopsin indicates the presence of a long cytoplasmic tail with multiple putative phosphorylation sites, suggesting that this opsin’s function may be finely regulated. Melanopsin mRNA is expressed in hypothalamic sites thought to contain deep brain photoreceptors and in the iris, a structure known to be directly photosensitive in amphibians. Melanopsin message is also localized in retinal cells residing in the outermost lamina of the inner nuclear layer where horizontal cells are typically found. Its expression in retinal and nonretinal tissues suggests a role in vision and nonvisual photoreceptive tasks, such as photic control of skin pigmentation, pupillary aperture, and circadian and photoperiodic physiology.

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Authors: Provencio, I., Jiang, G., De Grip, W. J., Hayes, W. P., & Rollag, M. D.
Affiliations: Uniformed Services University of the Health Sciences (US)
Department of Anatomy and Cell Biology, Uniformed Services University of the Health Sciences, Bethesda, MD 20814; Institute of Cellular Signaling, University of Nijmegen, 6500 HB Nijmegen, The Netherlands; and Department of Biology, The Catholic University of America, Washington, DC 20064
ORCID: Provencio, Ignacio
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1998-01-06
Volume: 95
Issue: 1
Pages: 340-345
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.95.1.340
PMC: PMC18217
OpenAlex: W1971524741
Semantic Scholar: 65bdc3eb7e2fb5d60b2f8f75ea76a9d735399611
Cited by: 975
References: 43
Citations by year: 2026: 20 · 2025: 42 · 2024: 27 · 2023: 50 · 2022: 43 · 2021: 46 · 2020: 48 · 2019: 28 · 2018: 39 · 2017: 52 · 2016: 47 · 2015: 36 · 2014: 48 · 2013: 41 · 2012: 41
FWCI: 6.98
Type: journal article
Language: en
Open access: green
europepmc.org
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Radboud Repository (Radboud University) (submittedVersion)
Topics: Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Circadian rhythm and melatonin
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › melanin and skin pigmentation
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Photoreceptor and optogenetics research
Keywords: melanopsin, opsin, melanophores, Xenopus laevis, amino acid sequence homology, cytoplasmic tail, phosphorylation sites, retinal horizontal cells, inner nuclear layer, non-visual photoreception, circadian physiology
MeSH terms: Melanopsin, Amino Acid Sequence, Animals, Brain Chemistry, Cells, Cultured, Eye, Melanophores, Molecular Sequence Data, Xenopus laevis, Sequence Alignment, Rod Opsins, In Situ Hybridization, Protein Structure, Secondary, DNA, Complementary

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Melanopsin: An opsin in melanophores, brain, and eye

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