Rod PDE6 complex: molecular mechanisms & dependencies

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

Human evidence only

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What it acts on

Image analysis of purified bovine rod phosphodiesterase 6 revealed the three-dimensional dimeric arrangement of the alpha-beta-delta complex and the internal organization of each catalytic subunit into three distinct domains corresponding to the catalytic and two GAF domains, and the three-dimensional molecular organization of human platelet phosphodiesterase type 5 appears highly homologous to that of bovine rod phosphodiesterase 6 as predicted by similarities in their primary sequences.
Rod PDE6 complex → Phosphodiesterase 5 family source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sildenafil-research/11453687.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "54fdc1cf336b81568055fa21b19ad21600db5bf276dc5dc9e1dcb490cb63de30", "start_char": 0, "end_char": 1312, "text_sha256": "54fdc1cf336b81568055fa21b19ad21600db5bf276dc5dc9e1dcb490cb63de30"}
experimental_model
Electron microscopy and single-particle image analysis of purified bovine rod phosphodiesterase 6
exposure
Solubilised rod PDE6 depleted of its gamma subunits, with immunolabelling
limitations
A structural comparison at 2.8 nanometre resolution rather than atomic detail. The comparison with PDE5 is inferred from sequence similarity and the reconstructed organisation.
nutrient_topic
Sildenafil research collection; topical membership is not evidence of a direct clinical effect, and the drug is recorded separately from its N-desmethyl metabolite and its target enzyme from the homologous retinal PDE6. · Sildenafil
organism
Cattle
plain_language
The retinal enzyme and the target enzyme are built to the same plan, which is why a drug for one reaches the other.
primary_references
[sil-p11453687] Molecular organization of bovine rod cGMP-phosphodiesterase 6. (2001). https://pubmed.ncbi.nlm.nih.gov/11453687/ DOI: 10.1006/jmbi.2001.4813
tissue_or_cell_type
Retinal rod outer segment
Sildenafil: the enzyme it occupies instead of the substrate, why it cannot start a signal it can only preserve, the organic nitrate interaction that follows from that, the homologous retinal enzyme ten-fold away, and the pulmonary circulation where the same mechanism became a second indication (2026-09-22) · lines 249–260
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Electron microscopy and single-particle image analysis of purified bovine rod phosphodiesterase 6 · source_derived_draft · unverified_draft
### sil-pde5-and-pde6-are-built-alike Image analysis of purified bovine rod phosphodiesterase 6 revealed the three-dimensional dimeric arrangement of the alpha-beta-delta complex and the internal organization of each catalytic subunit into three distinct domains corresponding to the catalytic and two GAF domains, and the three-dimensional molecular organization of human platelet phosphodiesterase type 5 appears highly homologous to that of bovine rod phosphodiesterase 6 as predicted by similarities in their primary sequences. Condition category: normal nutrient_topic: Sildenafil research collection; topical membership is not evidence of a direct clinical effect, and the drug is recorded separately from its N-desmethyl metabolite and its target enzyme from the homologous retinal PDE6. plain_language: The retinal enzyme and the target enzyme are built to the same plan, which is why a drug for one reaches the other. organism: Cattle tissue_or_cell_type: Retinal rod outer segment experimental_model: Electron microscopy and single-particle image analysis of purified bovine rod phosphodiesterase 6 limitations: A structural comparison at 2.8 nanometre resolution rather than atomic detail. The comparison with PDE5 is inferred from sequence similarity and the reconstructed organisation. exposure: Solubilised rod PDE6 depleted of its gamma subunits, with immunolabelling evidence_span: {"source_cache": "artifacts/sildenafil-research/11453687.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "54fdc1cf336b81568055fa21b19ad21600db5bf276dc5dc9e1dcb490cb63de30", "start_char": 0, "end_char": 1312, "text_sha256": "54fdc1cf336b81568055fa21b19ad21600db5bf276dc5dc9e1dcb490cb63de30"} [sil-p11453687] Molecular organization of bovine rod cGMP-phosphodiesterase 6. (2001). https://pubmed.ncbi.nlm.nih.gov/11453687/ DOI: 10.1006/jmbi.2001.4813
Complete structured claim and evidence
Activated rod phosphodiesterase hydrolyzed cyclic GMP in the phototransduction reconstitution.
Rod PDE6 complex → Cyclic guanosine monophosphate source_derived_draftungraded
Experimental context and source evidence
experimental_model
Biochemical phosphodiesterase assay
limitations
The channel step was tested in a separate experiment.
nutrient_topic
Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
organism
Bos taurus
plain_language
cGMP destruction passes the light signal toward channel closure.
primary_references
[fung-1981] Flow of information in the light-triggered cyclic nucleotide cascade of vision (1981). https://pubmed.ncbi.nlm.nih.gov/6264430/ DOI: 10.1073/pnas.78.1.152
tissue_or_cell_type
Rod outer-segment proteins
Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 927–936
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Biochemical phosphodiesterase assay · source_derived_draft · unverified_draft
### a-vision-pde6-cgmp Activated rod phosphodiesterase hydrolyzed cyclic GMP in the phototransduction reconstitution. Condition category: normal nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: cGMP destruction passes the light signal toward channel closure. organism: Bos taurus tissue_or_cell_type: Rod outer-segment proteins experimental_model: Biochemical phosphodiesterase assay limitations: The channel step was tested in a separate experiment. [fung-1981] Flow of information in the light-triggered cyclic nucleotide cascade of vision (1981). https://pubmed.ncbi.nlm.nih.gov/6264430/ DOI: 10.1073/pnas.78.1.152
Complete structured claim and evidence

What acts on it

Activated transducin stimulated rod cyclic-GMP phosphodiesterase in the reconstituted signaling system.
GTP-bound rod transducin alpha → Rod PDE6 complex source_derived_draftungraded
Experimental context and source evidence
experimental_model
Reconstituted transducin/PDE assays
limitations
Rod PDE6 complex identity is kept separate from cone PDE6.
nutrient_topic
Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
organism
Bos taurus
plain_language
Transducin turns on the enzyme that removes cGMP.
primary_references
[fung-1981] Flow of information in the light-triggered cyclic nucleotide cascade of vision (1981). https://pubmed.ncbi.nlm.nih.gov/6264430/ DOI: 10.1073/pnas.78.1.152
tissue_or_cell_type
Rod outer-segment proteins
Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 916–925
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Reconstituted transducin/PDE assays · source_derived_draft · unverified_draft
### a-vision-transducin-pde6 Activated transducin stimulated rod cyclic-GMP phosphodiesterase in the reconstituted signaling system. Condition category: normal nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: Transducin turns on the enzyme that removes cGMP. organism: Bos taurus tissue_or_cell_type: Rod outer-segment proteins experimental_model: Reconstituted transducin/PDE assays limitations: Rod PDE6 complex identity is kept separate from cone PDE6. [fung-1981] Flow of information in the light-triggered cyclic nucleotide cascade of vision (1981). https://pubmed.ncbi.nlm.nih.gov/6264430/ DOI: 10.1073/pnas.78.1.152
Complete structured claim and evidence

The events it takes part in

A mechanism often involves more than two components. These are the full events, with every participant and its role.

Situations it appears in

Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

Open hypotheses

Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.

This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

Rod PDE6 complex