ArticleOpen biology2018
It takes two transducins to activate the cGMP-phosphodiesterase 6 in retinal rods.
Article in Open biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 39 citations in OpenAlex.
- A highly dynamic active state for transducin-bound phosphodiesterase-6 in vertebrate phototransduction.bioRxiv : the preprint server for biology · 2026Article
- Effective AAV-mediated gene replacement therapy in retinal organoids modeling AIPL1-associated LCA4.Molecular therapy. Nucleic acids · 2024Article
- A marine cryptochrome with an inverse photo-oligomerization mechanism.Nature communications · 2023Article
- Photoreceptor physiology and evolution: cellular and molecular basis of rod and cone phototransduction.The Journal of physiology · 2022Review
- 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
- New focus on regulation of the rod photoreceptor phosphodiesterase.Current opinion in structural biology · 2021Review
- Pre-mRNA Processing Factors and Retinitis Pigmentosa: RNA Splicing and Beyond.Frontiers in cell and developmental biology · 2021Review
- A hybrid stochastic/deterministic model of single photon response and light adaptation in mouse rods.Computational and structural biotechnology journal · 2021Article
- Structure of the Visual Signaling Complex between Transducin and Phosphodiesterase 6.Molecular cell · 2020Article
- Structural Analysis of the Regulatory GAF Domains of cGMP Phosphodiesterase Elucidates the Allosteric Communication Pathway.Journal of molecular biology · 2020Article
- A kinetic analysis of mouse rod and cone photoreceptor responses.The Journal of physiology · 2020Article
- A quantitative account of mammalian rod phototransduction with PDE6 dimeric activation: responses to bright flashes.Open biology · 2020Article
- Article
- The molecular architecture of photoreceptor phosphodiesterase 6 (PDE6) with activated G protein elucidates the mechanism of visual excitation.The Journal of biological chemistry · 2019Article
- Therapeutic targeting of 3',5'-cyclic nucleotide phosphodiesterases: inhibition and beyond.Nature reviews. Drug discovery · 2019Review
- Allosteric Regulation of Rod Photoreceptor Phosphodiesterase 6 (PDE6) Elucidated by Chemical Cross-Linking and Quantitative Mass Spectrometry.Journal of molecular biology · 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
- Transducin activates cGMP phosphodiesterase by trapping inhibitory γ subunit freed reversibly from the catalytic subunit in solution.Scientific reports · 2019Article
- Reply to Heck et al.: Signal amplification at the rhodopsin-to-transducin·phosphodiesterase step in rod phototransduction.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Among cyclic nucleotide phosphodiesterases (PDEs), PDE6 is unique in serving as an effector enzyme in G protein-coupled signal transduction. In retinal rods and cones, PDE6 is membrane-bound and activated to hydrolyse its substrate, cGMP, by binding of two active G protein α-subunits (Gα*). To investigate the activation mechanism of mammalian rod PDE6, we have collected functional and structural data, and analysed them by reaction-diffusion simulations. Gα* titration of membrane-bound PDE6 reveals a strong functional asymmetry of the enzyme with respect to the affinity of Gα* for its two binding sites on membrane-bound PDE6 and the enzymatic activity of the intermediary 1 : 1 Gα* · PDE6 complex. Employing cGMP and its 8-bromo analogue as substrates, we find that Gα* · PDE6 forms with high affinity but has virtually no cGMP hydrolytic activity. To fully activate PDE6, it takes a second copy of Gα* which binds with lower affinity, forming Gα* · PDE6 · Gα*. Reaction-diffusion simulations show that the functional asymmetry of membrane-bound PDE6 constitutes a coincidence switch and explains the lack of G protein-related noise in visual signal transduction. The high local concentration of Gα* generated by a light-activated rhodopsin molecule efficiently activates PDE6, whereas the low density of spontaneously activated Gα* fails to activate the effector enzyme.
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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.