ArticleVision research2012
The expression of whirlin and Cav1.3α₁ is mutually independent in photoreceptors.
Article in Vision research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 8 citations in OpenAlex.
- Knockout of CaScientific reports · 2021Article
- Circadian regulation in the retina: From molecules to network.The European journal of neuroscience · 2020Review
- Voltage- and calcium-gated ion channels of neurons in the vertebrate retina.Progress in retinal and eye research · 2019Review
- D-cis-Diltiazem Can Produce Oxidative Stress in Healthy Depolarized Rods In Vivo.Investigative ophthalmology & visual science · 2018Article
- Expression of Cav1.3 calcium channel in the human and mouse colon: posttranscriptional inhibition by IFNγ.American journal of physiology. Gastrointestinal and liver physiology · 2017Article
- MRI of rod cell compartment-specific function in disease and treatment in vivo.Progress in retinal and eye research · 2016Review
- Genetic dissection of horizontal cell inhibitory signaling in mice in complete darkness in vivo.Investigative ophthalmology & visual science · 2015Article
- Usher syndrome: Hearing loss, retinal degeneration and associated abnormalities.Biochimica et biophysica acta · 2015Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Whirlin is a gene responsible for Usher syndrome type II (USH2) and congenital deafness. In photoreceptors, it organizes a protein complex through binding to proteins encoded by other USH2 genes, usherin (USH2A) and G-protein-coupled receptor 98 (GPR98). Recently, Ca(v)1.3α(1) (α(1D)) has been discovered to interact with whirlin in vitro and these two proteins are localized to the same subcellular compartments in photoreceptors. Accordingly, it is proposed that Ca(v)1.3α(1) is in the USH2 protein complex and that the USH2 protein complex is involved in regulating Ca(2+) in photoreceptors. To test this hypothesis, we investigated the interdependence of Ca(v)1.3α(1) and whirlin expression in photoreceptors. We found that lack of Ca(v)1.3α(1) did not change the whirlin distribution or expression level in photoreceptors. In the retina, several Ca(v)1.3α(1) splice variants were found at the RNA level. Among them, the whirlin-interacting Ca(v)1.3α(1) long variant had no change in its protein expression level in the absence of whirlin. The localization of Ca(v)1.3α(1) in photoreceptors, published previously, cannot be confirmed. Therefore, the mutual independence of whirlin and Ca(v)1.3α(1) expressions in photoreceptors suggests that Ca(v)1.3α(1) may not be a key member of the USH2 protein complex at the periciliary membrane complex.
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Registered trials
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.