ArticleThe Journal of biological chemistry2016
Aryl Hydrocarbon Receptor-interacting Protein-like 1 Is an Obligate Chaperone of Phosphodiesterase 6 and Is Assisted by the γ-Subunit of Its Client.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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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.
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Who cites it
26 citing papers in PubMed, 40 citations in OpenAlex.
- Redox regulation of PDE6 and cGMP signaling in diabetic retinal neurodegeneration.Biochemistry and biophysics reports · 2026Review
- Structural basis of phosphodiesterase-5 conformational organization revealed by a PDE6/PDE5 chimera.The Journal of biological chemistry · 2026Article
- Restoring Sight: The Journey of AIPL1 from Discovery to Therapy.International journal of molecular sciences · 2025Review
- Structural and functional dynamics of human cone cGMP-phosphodiesterase important for photopic vision.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Cone photoreceptor phosphodiesterase PDE6H inhibition regulates cancer cell growth and metabolism, replicating the dark retina response.Cancer & metabolism · 2024Article
- Evaluation of mesenchymal stem cells as anFrontiers in cell and developmental biology · 2024Review
- Updates on protein-prenylation and associated inherited retinopathies.Frontiers in ophthalmology · 2024Review
- Reconstitution of the phosphodiesterase 6 maturation process important for photoreceptor cell function.The Journal of biological chemistry · 2024Article
- Unique interface and dynamics of the complex of HSP90 with a specialized cochaperone AIPL1.Structure (London, England : 1993) · 2023Article
- The Role of Hsp90 in Retinal Proteostasis and Disease.Biomolecules · 2022Review
- Review
- 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
- Clinical and functional analyses of AIPL1 variants reveal mechanisms of pathogenicity linked to different forms of retinal degeneration.Scientific reports · 2020Article
- Structural Analysis of the Regulatory GAF Domains of cGMP Phosphodiesterase Elucidates the Allosteric Communication Pathway.Journal of molecular biology · 2020Article
- Novel Bi-allelic PDE6C Variant Leads to Congenital Achromatopsia.Iranian biomedical journal · 2020Article
- Review
- Interaction of the tetratricopeptide repeat domain of aryl hydrocarbon receptor-interacting protein-like 1 with the regulatory Pγ subunit of phosphodiesterase 6.The Journal of biological chemistry · 2019Article
- A nonhuman primate model of inherited retinal disease.The Journal of clinical investigation · 2019Article
- FKBP Ligands-Where We Are and Where to Go?Frontiers in pharmacology · 2018Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Phosphodiesterase 6 (PDE6) is the effector enzyme in the phototransduction cascade and is critical for the health of both rod and cone photoreceptors. Its dysfunction, caused by mutations in either the enzyme itself or AIPL1 (aryl hydrocarbon receptor-interacting protein-like 1), leads to retinal diseases culminating in blindness. Progress in research on PDE6 and AIPL1 has been severely hampered by failure to express functional PDE6 in a heterologous expression system. Here, we demonstrated that AIPL1 is an obligate chaperone of PDE6 and that it enables low yield functional folding of cone PDE6C in cultured cells. We further show that the AIPL1-mediated production of folded PDE6C is markedly elevated in the presence of the inhibitory Pγ-subunit of PDE6. As illustrated in this study, a simple and sensitive system in which AIPL1 and Pγ are co-expressed with PDE6 represents an effective tool for probing structure-function relationships of AIPL1 and reliably establishing the pathogenicity of its variants.
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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.