ArticleInternational journal of molecular sciences2013
Disease-causing mutations in BEST1 gene are associated with altered sorting of bestrophin-1 protein.
Article in International journal of molecular sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 19 citations in OpenAlex.
- Review of the clinical electrooculogram - Part 2: the bestrophinopathies and modified protocols.Documenta ophthalmologica. Advances in ophthalmology · 2026Review
- Novel BEST1 Variant Characterization in a Large French Cohort in Light of Updated Bestrophin-1 Structure-Function Correlation.Investigative ophthalmology & visual science · 2025Article
- Design and Biological Evaluation of hBest1-Containing Bilayer Nanostructures.Molecules (Basel, Switzerland) · 2025Article
- Clinical and Genetic Features of Autosomal Recessive Bestrophinopathy: A Case Series from a Vietnamese Cohort.Biomedicines · 2025Article
- Best Disease: Global Mutations Review, Genotype-Phenotype Correlation, and Prevalence Analysis in the Israeli Population.Investigative ophthalmology & visual science · 2024Article
- Impaired Bestrophin Channel Activity in an iPSC-RPE Model of Best Vitelliform Macular Dystrophy (BVMD) from an Early Onset Patient Carrying the P77S Dominant Mutation.International journal of molecular sciences · 2022Article
- Functional assays of non-canonical splice-site variants in inherited retinal dystrophies genes.Scientific reports · 2022Article
- Pathogenicity of new BEST1 variants identified in Italian patients with best vitelliform macular dystrophy assessed by computational structural biology.Journal of translational medicine · 2019Article
- BEST1 protein stability and degradation pathways differ between autosomal dominant Best disease and autosomal recessive bestrophinopathy accounting for the distinct retinal phenotypes.Human molecular genetics · 2018Article
- Restoration of mutant bestrophin-1 expression, localisation and function in a polarised epithelial cell model.Disease models & mechanisms · 2016Article
- Mislocalisation of BEST1 in iPSC-derived retinal pigment epithelial cells from a family with autosomal dominant vitreoretinochoroidopathy (ADVIRC).Scientific reports · 2016Article
- Transepithelial resistance in human bestrophin-1 stably transfected Madin-Darby canine kidney cells.Biotechnology, biotechnological equipment · 2015Article
- Changes in the functional characteristics of tumor and normal cells after treatment with extracts of white dead-nettle.Biotechnology, biotechnological equipment · 2015Article
- Bestrophin-1 influences transepithelial electrical properties and Ca2+ signaling in human retinal pigment epithelium.Molecular vision · 2015Article
- Disease-causing mutations associated with four bestrophinopathies exhibit disparate effects on the localization, but not the oligomerization, of Bestrophin-1.Experimental eye research · 2014Article
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Authors and funding
12 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mutations in BEST1 gene, encoding the bestrophin-1 (Best1) protein are associated with macular dystrophies. Best1 is predominantly expressed in the retinal pigment epithelium (RPE), and is inserted in its basolateral membrane. We investigated the cellular localization in polarized MDCKII cells of disease-associated Best1 mutant proteins to study specific sorting motifs of Best1. Real-time PCR and western blots for endogenous expression of BEST1 in MDCK cells were performed. Best1 mutant constructs were generated using site-directed mutagenesis and transfected in MDCK cells. For protein sorting, confocal microscopy studies, biotinylation assays and statistical methods for quantification of mislocalization were used. Analysis of endogenous expression of BEST1 in MDCK cells revealed the presence of BEST1 transcript but no protein. Confocal microscopy and quantitative analyses indicate that transfected normal human Best1 displays a basolateral localization in MDCK cells, while cell sorting of several Best1 mutants (Y85H, Q96R, L100R, Y227N, Y227E) was altered. In contrast to constitutively active Y227E, constitutively inactive Y227F Best1 mutant localized basolaterally similar to the normal Best1 protein. Our data suggest that at least three basolateral sorting motifs might be implicated in proper Best1 basolateral localization. In addition, non-phosphorylated tyrosine 227 could play a role for basolateral delivery.
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