ArticleMolecular vision2008
Protein-protein interactions between lens vimentin and alphaB-crystallin using FRET acceptor photobleaching.
Article in Molecular vision, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- β-synuclein regulates the phase transitions and amyloid conversion of α-synuclein.Nature communications · 2024Article
- Impact of N-Terminal Tags on De Novo Vimentin Intermediate Filament Assembly.International journal of molecular sciences · 2022Article
- Structural and functional studies of D109A human αB-crystallin contributing to the development of cataract and cardiomyopathy diseases.PloS one · 2021Article
- Neuromuscular Diseases Due to Chaperone Mutations: A Review and Some New Results.International journal of molecular sciences · 2020Review
- Vimentin Diversity in Health and Disease.Cells · 2018Review
- Interactome Mapping Guided by Tissue-Specific Phosphorylation in Age-Related Macular Degeneration.International journal of scientific and engineering research · 2017Article
- Differential role of arginine mutations on the structure and functions of α-crystallin.Biochimica et biophysica acta · 2016Review
- Article
- Transcriptional regulation of crystallin, redox, and apoptotic genes by C-Phycocyanin in the selenite-induced cataractogenic rat model.Molecular vision · 2015Article
- Acetylation of lysine 92 improves the chaperone and anti-apoptotic activities of human αB-crystallin.Biochemistry · 2013Article
- The NADPH metabolic network regulates human αB-crystallin cardiomyopathy and reductive stress in Drosophila melanogaster.PLoS genetics · 2013Article
- Molecular and structural analysis of genetic variations in congenital cataract.Molecular vision · 2013Article
- Vimentin in cancer and its potential as a molecular target for cancer therapy.Cellular and molecular life sciences : CMLS · 2011Review
- The common modification in alphaA-crystallin in the lens, N101D, is associated with increased opacity in a mouse model.The Journal of biological chemistry · 2011Article
- A knock-in mouse model for the R120G mutation of αB-crystallin recapitulates human hereditary myopathy and cataracts.PloS one · 2011Article
- Analysis on the alterations of lens proteins by Vitex negundo in selenite cataract models.Molecular vision · 2011Article
- Role of the cytoskeleton in formation and maintenance of angiogenic sprouts.Journal of vascular research · 2011Review
- Structural changes in the cytoplasmic domain of the mechanosensitive channel MscS during opening.Biophysical journal · 2009Article
- Identification of interaction sites between human betaA3- and alphaA/alphaB-crystallins by mammalian two-hybrid and fluorescence resonance energy transfer acceptor photobleaching methods.The Journal of biological chemistry · 2009Article
- Lens intermediate filaments.Experimental eye research · 2009Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
purposeThe R120G mutation of alphaB-crystallin is known to cause desmin-related myopathy, but the mechanisms underlying the formation of cataract are not clearly established. We hypothesize that alteration of protein-protein interaction between R120G alphaB-crystallin and lens intermediate filament proteins is one of the mechanisms of congenital cataract.
methodsProtein-protein interactions were determined by confocal fluorescence resonance energy transfer (FRET) microscopy using green fluorescence protein (GFP) as the donor and red fluorescence protein (RFP) as the acceptor. The lens vimentin gene was fused into a GFP vector and the alphaB-crystallin (WT or R120G mutant) gene was fused into the RFP vector. The donor-acceptor plasmid pairs of intermediate filament (IF)-GFP and alphaB-RFP were co-transfected into HeLa cells. After incubation, confocal fluorescence images of the transfected cells were taken. FRET was estimated by the acceptor photobleaching method. Protein-protein interaction was evaluated by FRET efficiency.
resultsThe confocal fluorescence images showed that the cells expressing vimentin and R120G alphaB-crystallin contained large amounts of protein aggregates while few vimentin fibers were observed. FRET efficiency analyses indicated that vimentin had a significantly greater protein-protein interaction with R120G alphaB-crystallin than with WT alphaB-crystallin.
conclusionsOur results show that the R120G alphaB-crystallin mutant promoted vimentin aggregation through increased protein-protein interaction. This process may contribute to the formation of congenital cataract.
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18618007PMC2447818W2127154055What OpenQuestion holds
Registered trials
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