ArticleThe Journal of biological chemistry2010
Rod phosphodiesterase-6 PDE6A and PDE6B subunits are enzymatically equivalent.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 53 citations in OpenAlex.
- Compact transcriptional activators: Therapeutic gene regulation in ocular disease.Neural regeneration research · 2026Article
- Zebrafish knockout models of atxn1a, atxn1b, and atxn1l reveal distinct and shared phenotypic and transcriptomic alterations.Human molecular genetics · 2026Article
- Review
- dCasMINI-mediated therapy rescues photoreceptors degeneration in a mouse model of retinitis pigmentosa.Science advances · 2024Article
- Mechanism investigation of highly selective inhibitors toward phosphodiesterase 5 and 6 via theFrontiers in chemistry · 2024Article
- Identification of Human Retinal Organoid Cell Differentiation-Related Genes via Single-Cell Sequencing Data Analysis.Computational and mathematical methods in medicine · 2022Article
- Photoreceptor Phosphodiesterase (PDE6): Structure, Regulatory Mechanisms, and Implications for Treatment of Retinal Diseases.Advances in experimental medicine and biology · 2022Review
- Photoreceptor phosphodiesterase (PDE6): activation and inactivation mechanisms during visual transduction in rods and cones.Pflugers Archiv : European journal of physiology · 2021Review
- A quantitative account of mammalian rod phototransduction with PDE6 dimeric activation: responses to bright flashes.Open biology · 2020Article
- The molecular architecture of photoreceptor phosphodiesterase 6 (PDE6) with activated G protein elucidates the mechanism of visual excitation.The Journal of biological chemistry · 2019Article
- Longitudinal Clinical Follow-up and Genetic Spectrum of Patients With Rod-Cone Dystrophy Associated With Mutations in PDE6A and PDE6B.JAMA ophthalmology · 2019Article
- The N termini of the inhibitory γ-subunits of phosphodiesterase-6 (PDE6) from rod and cone photoreceptors differentially regulate transducin-mediated PDE6 activation.The Journal of biological chemistry · 2019Article
- Elementary response triggered by transducin in retinal rods.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Deep Genome Resequencing Reveals Artificial and Natural Selection for Visual Deterioration, Plateau Adaptability and High Prolificacy in Chinese Domestic Sheep.Frontiers in genetics · 2019Article
- It takes two transducins to activate the cGMP-phosphodiesterase 6 in retinal rods.Open biology · 2018Article
- Implications of dimeric activation of PDE6 for rod phototransduction.Open biology · 2018Article
- Mechanisms of mutant PDE6 proteins underlying retinal diseases.Cellular signalling · 2017Article
- Elevated cAMP improves signal-to-noise ratio in amphibian rod photoreceptors.The Journal of general physiology · 2017Article
- Origins of the phototransduction delay as inferred from stochastic and deterministic simulation of the amplification cascade.Molecular vision · 2017Article
- Evolution and expression of the phosphodiesterase 6 genes unveils vertebrate novelty to control photosensitivity.BMC evolutionary biology · 2016Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Phosphodiesterase-6 (PDE6) is the key effector enzyme of the phototransduction cascade in rods and cones. The catalytic core of rod PDE6 is a unique heterodimer of PDE6A and PDE6B catalytic subunits. The functional significance of rod PDE6 heterodimerization and conserved differences between PDE6AB and cone PDE6C and the individual properties of PDE6A and PDE6B are unknown. To address these outstanding questions, we expressed chimeric homodimeric enzymes, enhanced GFP (EGFP)-PDE6C-A and EGFP-PDE6C-B, containing the PDE6A and PDE6B catalytic domains, respectively, in transgenic Xenopus laevis. Similar to EGFP-PDE6C, EGFP-PDE6C-A and EGFP-PDE6C-B were targeted to the rod outer segments and concentrated at the disc rims. PDE6C, PDE6C-A, and PDE6C-B were isolated following selective immunoprecipitation of the EGFP fusion proteins. All three enzymes, PDE6C, PDE6C-A, and PDE6C-B, hydrolyzed cGMP with similar K(m) (20-23 μM) and k(cat) (4200-5100 s(-1)) values. Likewise, the K(i) values for PDE6C, PDE6C-A, and PDE6C-B inhibition by the cone- and rod-specific PDE6 γ-subunits (Pγ) were comparable. Recombinant cone transducin-α (Gα(t2)) and native rod Gα(t1) fully and potently activated PDE6C, PDE6C-A, and PDE6C-B. In contrast, the half-maximal activation of bovine rod PDE6 required markedly higher concentrations of Gα(t2) or Gα(t1). Our results suggest that PDE6A and PDE6B are enzymatically equivalent. Furthermore, PDE6A and PDE6B are similar to PDE6C with respect to catalytic properties and the interaction with Pγ but differ in the interaction with transducin. This study significantly limits the range of mechanisms by which conserved differences between PDE6A, PDE6B, and PDE6C may contribute to remarkable differences in rod and cone physiology.
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