ArticleInvestigative ophthalmology & visual science2011
Interaction of arrestin with enolase1 in photoreceptors.
Article in Investigative ophthalmology & visual science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 33 citations in OpenAlex.
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- Modulation of Aerobic Glycolysis Genes During the Progression of Retinitis Pigmentosa.Investigative ophthalmology & visual science · 2026Article
- Arrestins as Possible Drug Targets.Biomolecules & therapeutics · 2025Review
- GPCR-dependent and -independent arrestin signaling.Trends in pharmacological sciences · 2024Review
- Arrestins: A Small Family of Multi-Functional Proteins.International journal of molecular sciences · 2024Review
- Do arrestin oligomers have specific functions?Cell signaling · 2023Article
- [Relationship between anti-ENO1 antibody and systemic lupus erythematosus patients with retinopathy].Beijing da xue xue bao. Yi xue ban = Journal of Peking University. Health sciences · 2022Article
- A Modified Arrestin1 Increases Lactate Production in the Retina and Slows Retinal Degeneration.Human gene therapy · 2022Article
- Functional compartmentalization of photoreceptor neurons.Pflugers Archiv : European journal of physiology · 2021Review
- Compartmentalization of Photoreceptor Sensory Cilia.Frontiers in cell and developmental biology · 2021Review
- An arrestin-1 surface opposite of its interface with photoactivated rhodopsin engages with enolase-1.The Journal of biological chemistry · 2020Article
- Impact of Autoantibodies against Glycolytic Enzymes on Pathogenicity of Autoimmune Retinopathy and Other Autoimmune Disorders.Frontiers in immunology · 2017Review
- Arrestin 1 and Cone Arrestin 4 Have Unique Roles in Visual Function in an All-Cone Mouse Retina.Investigative ophthalmology & visual science · 2015Article
- Light-dependent phosphorylation of Bardet-Biedl syndrome 5 in photoreceptor cells modulates its interaction with arrestin1.Cellular and molecular life sciences : CMLS · 2013Article
- Rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant.Cellular signalling · 2013Article
- Protein sorting, targeting and trafficking in photoreceptor cells.Progress in retinal and eye research · 2013Review
- Alterations in energy metabolism, neuroprotection and visual signal transduction in the retina of Parkinsonian, MPTP-treated monkeys.PloS one · 2013Article
- Transport and localization of signaling proteins in ciliated cells.Vision research · 2012Review
- Redox proteomic identification of visual arrestin dimerization in photoreceptor degeneration after photic injury.Investigative ophthalmology & visual science · 2012Article
- Steric volume exclusion sets soluble protein concentrations in photoreceptor sensory cilia.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
purposeArrestin is in disequilibrium in photoreceptors, translocating between inner and outer segments in response to light. The purpose of this project was to identify the cellular component with which arrestin associates in the dark-adapted retina.
methodsRetinas were cross-linked with 2.5 mM dithiobis(succinimidylpropionate) (DSP), and arrestin-containing complexes purified by anion-exchange chromatography. Tandem mass spectrometric analysis was used to identify the protein components in the complex. Enolase localization in photoreceptors was assessed by immunohistochemistry. Confirmation of interacting components was performed using immunoprecipitation and surface plasmon resonance (SPR). Enolase activity was also assessed in the presence of arrestin1.
resultsIn retinas treated with DSP, arrestin cross-linked in a 125-kDa complex. The principal components of this complex were arrestin1 and enolase1. Both arrestin1 and -4 were pulled down with enolase1 when enolase1 was immunoprecipitated. In the dark-adapted retina, enolase1 co-localized with arrestin1 in the inner segments and outer nuclear layer, but remained in the inner segments when arrestin1 translocated in response to light adaptation. SPR of purified arrestin1 and enolase1 demonstrated direct binding between arrestin1 and enolase1. Arrestin1 modulated the catalytic activity of enolase1, slowing it by as much as 24%.
conclusionsThe results show that in the dark-adapted retina, arrestin1 and -4 interact with enolase1. The SPR data show that the interaction between arrestin1 and enolase1 was direct, not requiring a third element to form the complex. Arrestin1 slowed the catalytic activity of enolase1, suggesting that light-driven translocation of arrestin1 may modulate the metabolic activity of photoreceptors.
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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.