{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRhodopsin is the prototypical G protein–coupled receptor responsible for initiating vision by absorbing photons and undergoing a conformational change that transforms its 11‐cis retinal chromophore into the all‐trans form. This photoisomerization triggers a cascade of structural rearrangements—including changes in key motifs such as NPxxY and transitions in cytoplasmic helix 8—that open cytosolic cavities for selective coupling of downstream transducers. High‐resolution crystallography, nuclear magnetic resonance, and molecular dynamics studies have revealed how rhodopsin dynamically organizes its internal water channels and nanodomains in the disc membranes to achieve arrestin– and G protein–biased signaling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nA wide spectrum of disease‐linked mutations in the RHO gene disrupts its precise folding, post‐translational modifications, and interactions with both chaperones and signal‐regulatory proteins. Such mutations can impair correct chromophore binding, promote misfolding and aberrant oligomerization, or alter the kinetics of receptor deactivation through abnormal phosphorylation and arrestin recruitment. These deficiencies underlie severe retinal degenerations such as autosomal–dominant retinitis pigmentosa and congenital stationary night blindness. In experimental animal models and cell‐based systems, studies have detailed how point mutations (including those affecting residues in the active site and elsewhere in the extracellular and cytoplasmic domains) interfere with rhodopsin’s maturation, trafficking, and downstream G protein activation, ultimately compromising photoreceptor cell viability."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "23"}, {"type": "fg_f", "ref": "3"}, {"type": "fg_fs", "start_ref": "24", "end_ref": "40"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its central role in phototransduction, rhodopsin expression and trafficking are subject to a multilayered regulatory network that ensures proper folding in the endoplasmic reticulum, efficient incorporation of its chromophore, and accurate targeting to the specialized outer segment and primary cilia of rod photoreceptors. Recent studies have demonstrated that translational control mechanisms—including association with specific polyribosomes and microRNAs—as well as dedicated chaperones and trafficking effectors, are critical for maintaining the balance between receptor synthesis and turnover. Intriguingly, rhodopsin‐related opsins have also been detected in extraretinal tissues such as human epidermis, highlighting broader roles for these receptors in peripheral light sensing. Comparative analyses with light‐gated microbial rhodopsins further provide insights into the general principles of receptor activation by light."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "41", "end_ref": "43"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Pere Garriga, Joan Manyosa "}, {"type": "b", "children": [{"type": "t", "text": "The eye photoreceptor protein rhodopsin. Structural implications for retinal disease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/s0014-5793(02)03241-6"}], "href": "https://doi.org/10.1016/s0014-5793(02"}, {"type": "t", "text": "03241-6) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12297272"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12297272"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Olaf Fritze, Sławomir Filipek, Vladimir Kuksa, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Role of the conserved NPxxY(x)5,6F motif in the rhodopsin ground state and during activation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0435715100"}], "href": "https://doi.org/10.1073/pnas.0435715100"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12601165"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12601165"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Shivani Ahuja, Markus Eilers, Amiram Hirshfeld, et al. 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