# Bidirectional Phosphorylation Changes in Opsins Associated With Early Myopia and Hyperopia Signal Regulation by Phosphoproteomics

**Authors:** Yang Yang, Ying Hon Sze, Houjiang Zhou, Winky Wing Man Ko, Yuanliang Zhang, Kecheng Li, Qi Zhang, King Kit Li, Trevor C. Charles, Chi-ho To, Qian Zhao, Thomas Chuen Lam

PMC · DOI: 10.1167/iovs.66.9.70 · Investigative Ophthalmology & Visual Science · 2025-07-30

## TL;DR

This study explores how phosphorylation changes in retinal opsins are linked to myopia and hyperopia, revealing a potential molecular mechanism for eye adaptation to optical changes.

## Contribution

The study identifies specific phosphorylation sites in opsins that are modulated during myopia and hyperopia, offering new insights into retinal signaling.

## Key findings

- Phosphorylation at S334 in rhodopsin, S328 in violet-sensitive opsin, and S342 in blue-sensitive opsin changes with optical conditions.
- Dephosphorylation at these sites occurs during myopia, while phosphorylation is maintained in hyperopia.
- These phosphorylation patterns suggest a bidirectional signaling mechanism in retinal adaptation to vision changes.

## Abstract

The study aimed to investigate the role of post-translational modifications (PTMs), specifically phosphorylation, in the pathogenesis of lens-induced myopia (LIM) and lens-induced hyperopia (LIH).

This study used an untargeted phosphoproteomics approach to identify more than 12,000 phosphorylation sites in chick retinas. The changes in phosphorylation levels were quantified using the tandem mass tag (TMT) technique. Furthermore, targeted mass spectrometry was employed to characterize and validate the phosphorylation changes in visual opsins.

The analysis identified differential phosphorylation at specific sites: S334 in rhodopsin, S328 in violet-sensitive opsin, and S342 in blue-sensitive opsin. Notably, these serine residues were dephosphorylated during the onset of myopia, but they remained phosphorylated under hyperopic conditions. This finding indicates that phosphorylation patterns in opsins are significantly modulated by changes in optical conditions, potentially influencing retinal signaling pathways.

The findings highlight the bidirectional modulation of phosphorylation in opsins as a potential mechanism linking optical factors from induced myopia and hyperopia to the molecular signaling processes that regulate ocular growth and adaptation.

## Linked entities

- **Proteins:** rhodopsin (rhodopsin-like)
- **Diseases:** myopia (MONDO:0001384), hyperopia (MONDO:0004891)

## Full-text entities

- **Genes:** OPN5 (opsin 5) [NCBI Gene 428670] {aka GPR136, GRP136, Opn5m, PGR12, TMEM13, cOpn5m}, OXER1 (oxoeicosanoid receptor 1) [NCBI Gene 165140] {aka GPCR, GPR170, TG1019}, RHO (rhodopsin) [NCBI Gene 751791] {aka CSNBAD1, OPN2, RDP1, RP4, opsin-2}, OPNP (opsin, pineal) [NCBI Gene 396377] {aka opsin}, ARR3 (arrestin 3) [NCBI Gene 407] {aka ARRX, MYP26, cArr}, HIF1A (hypoxia inducible factor 1 alpha subunit) [NCBI Gene 374177], RHO (rhodopsin) [NCBI Gene 6010] {aka CSNBAD1, OPN2, RP4}, OPN1SW (opsin 1 (cone pigments), short-wave-sensitive (violet cone opsin)) [NCBI Gene 396419] {aka SWS1, opsin}
- **Diseases:** VCD (MESH:D007222), refractive error (MESH:D012030), Hyperopia (MESH:D006956), glaucoma (MESH:D005901), retinal detachment (MESH:D012163), cataracts (MESH:D002386), overdose (MESH:D062787), Myopia (MESH:D009216), blurred vision (MESH:D014786), diabetic retinopathy (MESH:D003930), axial elongation (MESH:C537791), LIM (MESH:D007905)
- **Chemicals:** urea (MESH:D014508), dithiothreitol (MESH:D004229), phosphate (MESH:D010710), Phosphopeptides (MESH:D010748), MgCl2 (MESH:D015636), tyrosine (MESH:D014443), lipid (MESH:D008055), aspartic acid (MESH:D001224), lysine (MESH:D008239), FA (MESH:C030544), PMMA (MESH:D019904), lactic acid (MESH:D019344), Peptide (MESH:D010455), TiO2 (MESH:C009495), water (MESH:D014867), iodoacetamide (MESH:D007460), TEAB (MESH:C041737), cysteine (MESH:D003545), epoxy (MESH:D004853), pSer (MESH:D010768), ACN (MESH:C032159), calcium (MESH:D002118), PBS (MESH:D007854), nitrogen (MESH:D009584), Saline (MESH:D012965), adenosine triphosphate (MESH:D000255), EDTA (MESH:D004492), carbon dioxide (MESH:D002245), Lys-C (-), serine (MESH:D012694), HCl (MESH:D006851), dopamine (MESH:D004298), threonine (MESH:D013912), methionine (MESH:D008715), TFA (MESH:D014269), H3PO4 (MESH:C030242)
- **Species:** Gallus gallus (bantam, species) [taxon 9031], Mus musculus (house mouse, species) [taxon 10090], Cavia porcellus (domestic guinea pig, species) [taxon 10141], Homo sapiens (human, species) [taxon 9606]
- **Mutations:** threonine at position +6, aspartic acid at positions -4

## Full text

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## Figures

5 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12315934/full.md

## References

69 references — full list in the complete paper: https://tomesphere.com/paper/PMC12315934/full.md

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Source: https://tomesphere.com/paper/PMC12315934