Nucleosomal association and altered interactome underlie the mechanism of cataract caused by the R54C mutation of αA-crystallin

Ahsan, Saad M.; Raman, Bakthisaran; Tangirala, Ramakrishna; Rao, Ch. Mohan

doi:10.1016/j.bbagen.2021.129846

Cited by 4 publications

(2 citation statements)

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“…SUMOylation can promote α-crystallin expression by activating PAX6 in the lens [ 109 ]. , whereas the R54C mutation in alpha A-crystallin causes cataracts, and its molecular basis is the alteration of interactome and nucleosomal association [ 110 ]. P-benzoquinone(p-BQ) induces α-crystallin aggregation and affects the structure and chaperone function of α-crystallin, which is one of the causes of smoking-related cataracts [ 111 ].…”

Section: Discussionmentioning

confidence: 99%

A bibliometric and visualized analysis of the pathogenesis of cataracts from 1999 to 2023

Shu,

Liu,

et al. 2024

Heliyon

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Section: Discussionmentioning

confidence: 99%

A bibliometric and visualized analysis of the pathogenesis of cataracts from 1999 to 2023

Shu,

Liu,

et al. 2024

Heliyon

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“…The small heat shock protein, α-crystallins, which consist of αA- and αB-crystallin, function as molecular chaperones to inhibit the misfolding and aggregation of β/γ-crystallins ( Roskamp et al, 2019 ). In addition, α-crystallin also protects the lens cells against apoptosis ( Ahsan et al, 2021 ). Previous studies have reported that cataract pathogenesis is correlated with aberrant changes in the ratio of crystallin subunits and apoptosis of lens epithelial cells ( Li et al, 2008 ).…”

Section: Introductionmentioning

confidence: 99%

Cataract-causing allele in CRYAA (Y118D) proceeds through endoplasmic reticulum stress in mouse model

Jia

Wang

et al. 2021

Zoological Research

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As small heat shock proteins, α-crystallins function as molecular chaperones and inhibit the misfolding and aggregation of β/γ-crystallins. Genetic mutations of CRYAA are associated with protein aggregation and cataract occurrence. One possible process underlying cataract formation is that endoplasmic reticulum stress (ERS) induces the unfolded protein response (UPR), leading to apoptosis. However, the pathogenic mechanism related to this remains unexplored. Here, we successfully constructed a cataract-causing CRYAA (Y118D) mutant mouse model, in which the lenses of the CRYAA-Y118D mutant mice showed severe posterior rupture, abnormal morphological changes, and aberrant arrangement of crystallin fibers. Histological analysis was consistent with the clinical pathological characteristics. We also explored the pathogenic factors involved in cataract development through transcriptome analysis. In addition, based on key pathway analysis, up-regulated genes in CRYAA-Y118D mutant mice were implicated in the ERS-UPR pathway. This study showed that prolonged activation of the UPR pathway and severe stress response can cause proteotoxic and ERS-induced cell death in CRYAA-Y118D mutant mice.

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Crystallin gene expression: Insights from studies of transcriptional bursting

Cvekl

Eliscovich

2021

Experimental Eye Research

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Nucleosomal association and altered interactome underlie the mechanism of cataract caused by the R54C mutation of αA-crystallin

Cited by 4 publications

References 71 publications

A bibliometric and visualized analysis of the pathogenesis of cataracts from 1999 to 2023

A bibliometric and visualized analysis of the pathogenesis of cataracts from 1999 to 2023

Cataract-causing allele in CRYAA (Y118D) proceeds through endoplasmic reticulum stress in mouse model

Crystallin gene expression: Insights from studies of transcriptional bursting

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