Evidence map›Paper›PMID 34653198›Full record

ArticlePloS one2021

Spectral tuning and deactivation kinetics of marine mammal melanopsins.

Jeffry I Fasick, Haya Algrain, Courtland Samuels, Padmanabhan Mahadevan, Lorian E Schweikert, Zaid J Naffaa, Phyllis R Robinson

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 88% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Spectral Tuning in Mammalian Melanopsins.Molecular biology and evolution · 2025
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 5 institutions in 1 country.

Jeffry I FasickDepartment of Biological Sciences, The University of Tampa, Tampa, Florida, United States of America.ORCID 0000-0002-7657-4196
Haya AlgrainDepartment of Biological Sciences, University of Maryland Baltimore County, Baltimore, Maryland, United States of America.
Courtland SamuelsDepartment of Chemistry, University of South Florida, Tampa, Florida, United States of America.
Padmanabhan MahadevanDepartment of Biological Sciences, The University of Tampa, Tampa, Florida, United States of America.
Lorian E SchweikertDepartment of Biology and Marine Biology, University of North Carolina Wilmington, Wilmington, North Carolina, United States of America.
Zaid J NaffaaDepartment of Biological Sciences, Kean University, Union, New Jersey, United States of America.ORCID 0000-0003-3109-2975
Phyllis R RobinsonDepartment of Biological Sciences, University of Maryland Baltimore County, Baltimore, Maryland, United States of America.
University of Maryland, Baltimore County · USUniversity of Tampa · USKean University · USUniversity of North Carolina Wilmington · USUniversity of South Florida · US

Funding

Regulation of the intrinsic melanopsin-based light response in ipRGCsR01EY027202 · NEI · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI RONALD Lane BROWN, Joseph Leffler · 2017 to 2026
$5.3M
NEI NIH HHS R01 EY027202
6 · The paper itself

Abstract

In mammals, the photopigment melanopsin (Opn4) is found in a subset of retinal ganglion cells that serve light detection for circadian photoentrainment and pupil constriction (i.e., mydriasis). For a given species, the efficiency of photoentrainment and length of time that mydriasis occurs is determined by the spectral sensitivity and deactivation kinetics of melanopsin, respectively, and to date, neither of these properties have been described in marine mammals. Previous work has indicated that the absorbance maxima (λmax) of marine mammal rhodopsins (Rh1) have diversified to match the available light spectra at foraging depths. However, similar to the melanopsin λmax of terrestrial mammals (~480 nm), the melanopsins of marine mammals may be conserved, with λmax values tuned to the spectrum of solar irradiance at the water's surface. Here, we investigated the Opn4 pigments of 17 marine mammal species inhabiting diverse photic environments including the Infraorder Cetacea, as well as the Orders Sirenia and Carnivora. Both genomic and cDNA sequences were used to deduce amino acid sequences to identify substitutions most likely involved in spectral tuning and deactivation kinetics of the Opn4 pigments. Our results show that there appears to be no amino acid substitutions in marine mammal Opn4 opsins that would result in any significant change in λmax values relative to their terrestrial counterparts. We also found some marine mammal species to lack several phosphorylation sites in the carboxyl terminal domain of their Opn4 pigments that result in significantly slower deactivation kinetics, and thus longer mydriasis, compared to terrestrial controls. This finding was restricted to cetacean species previously found to lack cone photoreceptor opsins, a condition known as rod monochromacy. These results suggest that the rod monochromat whales rely on extended pupillary constriction to prevent photobleaching of the highly photosensitive all-rod retina when moving between photopic and scotopic conditions.

Indexed as

Amino Acid SequenceAnimalsAquatic OrganismsCaniformiaCarnivoraCetaceaKineticsMelanopsinModels, MolecularPhylogenyRod OpsinsSequence AlignmentSireniaMelanopsinRod Opsins

Identifiers

PMID34653198
PMCPMC8519484
OpenAlexW3207074110

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.