ArticleHuman molecular genetics2013
Differential effects of Best disease causing missense mutations on bestrophin-1 trafficking.
Article in Human molecular genetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 29 citations in OpenAlex.
- Review of the clinical electrooculogram - Part 2: the bestrophinopathies and modified protocols.Documenta ophthalmologica. Advances in ophthalmology · 2026Review
- Allele-specific suppression of pathogenic bestrophin-1 transcripts by CRISPR/Cas9-mediated genome editing.Genome medicine · 2026Article
- From BEST1 mutations to retinal regeneration: integrating stem cell-derived RPE models and gene correction strategies.Frontiers in cell and developmental biology · 2026Review
- Novel BEST1 Variant Characterization in a Large French Cohort in Light of Updated Bestrophin-1 Structure-Function Correlation.Investigative ophthalmology & visual science · 2025Article
- Degradable fibrin hydrogels for transplantation of iPSC-derived retinal pigment epithelial cell monolayers.Frontiers in cell and developmental biology · 2025Article
- Deep learning to distinguish Best vitelliform macular dystrophy (BVMD) from adult-onset vitelliform macular degeneration (AVMD).Scientific reports · 2022Article
- 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
- Sensing through Non-Sensing Ocular Ion Channels.International journal of molecular sciences · 2020Review
- Mutation-Dependent Pathomechanisms Determine the Phenotype in the Bestrophinopathies.International journal of molecular sciences · 2020Article
- The Y227N mutation affects bestrophin-1 protein stability and impairs sperm function in a mouse model of Best vitelliform macular dystrophy.Biology open · 2019Article
- Mutant Best1 Expression and Impaired Phagocytosis in an iPSC Model of Autosomal Recessive Bestrophinopathy.Scientific reports · 2018Article
- Bestrophin 1 and retinal disease.Progress in retinal and eye research · 2017Review
- Directional Fluid Transport across Organ-Blood Barriers: Physiology and Cell Biology.Cold Spring Harbor perspectives in biology · 2017Review
- Restoration of mutant bestrophin-1 expression, localisation and function in a polarised epithelial cell model.Disease models & mechanisms · 2016Article
- Phasing and structure of bestrophin-1: a case study in the use of heavy-atom cluster compounds with multi-subunit transmembrane proteins.Acta crystallographica. Section D, Structural biology · 2016Article
- Pharmacological Modulation of Photoreceptor Outer Segment Degradation in a Human iPS Cell Model of Inherited Macular Degeneration.Molecular therapy : the journal of the American Society of Gene Therapy · 2015Article
- Autosomal Recessive Bestrophinopathy Is Not Associated With the Loss of Bestrophin-1 Anion Channel Function in a Patient With a Novel BEST1 Mutation.Investigative ophthalmology & visual science · 2015Article
- Bestrophin 1 is indispensable for volume regulation in human retinal pigment epithelium cells.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Nonantibestrophin Anti-RPE Antibodies in Paraneoplastic Exudative Polymorphous Vitelliform Maculopathy.Translational vision science & technology · 2015Article
- Bestrophin-1 influences transepithelial electrical properties and Ca2+ signaling in human retinal pigment epithelium.Molecular vision · 2015Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Mutations in bestrophin-1 (Best1) cause Best vitelliform macular dystrophy (BVMD), a dominantly inherited retinal degenerative disease. Best1 is a homo-oligomeric anion channel localized to the basolateral surface of retinal pigment epithelial (RPE) cells. A number of Best1 mutants mislocalize in Madin-Darby canine kidney (MDCK) cells. However, many proteins traffic differently in MDCK and RPE cells, and MDCK cells do not express endogenous Best1. Thus, effects of Best1 mutations on localization in MDCK cells may not translate to RPE cells. To determine whether BVMD causing mutations affect Best1 localization, we compared localization and oligomerization of Best1 with Best1 mutants V9M, W93C, and R218C. In MDCK cells, Best1 and Best1(R218C) were basolaterally localized. Best1(W93C) and Best1(V9M) accumulated in cells. In cultured fetal human retinal pigment epithelium cells (fhRPE) expressing endogenous Best1, Best1(R218C) and Best1(W93C) were basolateral. Best1(V9M) was intracellular. All three mutants exhibited similar fluorescence resonance energy transfer (FRET) efficiencies to, and co-immunoprecipitated with Best1, indicating unimpaired oligomerization. When human Best1 was expressed in RPE in mouse eyes it was basolaterally localized. However, Best1(V9M) accumulated in intracellular compartments in mouse RPE. Co-expression of Best1 and Best1(W93C) in MDCK cells resulted in basolateral localization of both Best1 and Best1(W93C), but co-expression of Best1 with Best1(V9M) resulted in mislocalization of both proteins. We conclude that different mutations in Best1 cause differential effects on its localization and that this effect varies with the presence or absence of wild-type (WT) Best1. Furthermore, MDCK cells can substitute for RPE when examining the effects of BVMD causing mutations on Best1 localization if co-expressed with WT Best1.
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Registered trials
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