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Bidirectional Phosphorylation Changes in Opsins Associated With Early Myopia and Hyperopia Signal Regulation by
Yang Yang1,2, Ying Hon Sze2,3, Houjiang Zhou4
1Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hung Hom, Hong Kong.
Phosphorylation changes in visual opsins are linked to lens-induced myopia and hyperopia. These post-translational modifications (PTMs) in retinal opsins may influence ocular growth and adaptation in response to optical stimuli.
Area of Science:
- Ophthalmology
- Molecular Biology
- Proteomics
Background:
- Lens-induced myopia (LIM) and lens-induced hyperopia (LIH) are significant conditions affecting vision.
- Post-translational modifications (PTMs), such as phosphorylation, play crucial roles in cellular signaling.
- Understanding PTMs in ocular development is key to addressing refractive errors.
Purpose of the Study:
- To investigate the role of phosphorylation in the pathogenesis of LIM and LIH.
- To identify specific phosphorylation sites and their modulation in response to induced refractive errors.
Main Methods:
- Utilized an untargeted phosphoproteomics approach to identify phosphorylation sites in chick retinas.
- Quantified phosphorylation level changes using tandem mass tag (TMT) technique.
- Employed targeted mass spectrometry for validation of phosphorylation changes in visual opsins.
Main Results:
- Identified differential phosphorylation at serine residues S334 (rhodopsin), S328 (violet-sensitive opsin), and S342 (blue-sensitive opsin).
- Observed dephosphorylation of these sites during myopia onset and sustained phosphorylation under hyperopic conditions.
- Demonstrated that optical conditions significantly modulate opsin phosphorylation patterns, impacting retinal signaling.
Conclusions:
- Opsin phosphorylation is bidirectionally modulated by optical factors in LIM and LIH.
- This modulation represents a potential mechanism linking optical stimuli to molecular signaling in ocular growth and adaptation.
- Findings provide insights into the molecular basis of refractive error development.
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