ArticleiScience2022
Structurally-discovered KLF4 variants accelerate and stabilize reprogramming to pluripotency.
Article in iScience, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Micropatterned neural induction with heat-inactivated extracellular matrix protein by on-demand high-speed laser.Regenerative therapy · 2026Article
- Analyzing cell-type-specific isoform expression using IsoDiffR and long-read single-cell RNA sequencing.Bioinformatics (Oxford, England) · 2026Article
- Krüppel-Like Factor 4, a Hub Gate for Cell Crosstalk in Tumor Microenvironment.Cancer medicine · 2026Review
- Unmeasured human transcription factor ChIP-seq data shape functional genomics and demand strategic prioritization.Briefings in functional genomics · 2025Article
- Generation of human induced pluripotent stem cell lines derived from patients of cystic biliary atresia.Human cell · 2024Article
- Article
- Opening the "Black Box" Underlying Barriers to the Use of Canine Induced Pluripotent Stem Cells: A Narrative Review.Stem cells and development · 2023Review
- Butterfly eyespots exhibit unique patterns of open chromatin.F1000Research · 2023Article
- Comprehensive comparison of gene expression diversity among a variety of human stem cells.NAR genomics and bioinformatics · 2022Article
- Review
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Authors and funding
16 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Non-genetically modified somatic cells can only be inefficiently and stochastically reprogrammed to pluripotency by exogenous expression of reprogramming factors. Low competence of natural reprogramming factors may prevent the majority of cells to successfully and synchronously reprogram. Here we screened DNA-interacting amino acid residues in the zinc-finger domain of KLF4 for enhanced reprogramming efficiency using alanine-substitution scanning methods. Identified KLF4 L507A mutant accelerated and stabilized reprogramming to pluripotency in both mouse and human somatic cells. By testing all the variants of L507 position, variants with smaller amino acid residues in the KLF4 L507 position showed higher reprogramming efficiency. L507A bound more to promoters or enhancers of pluripotency genes, such as KLF5, and drove gene expression of these genes during reprogramming. Molecular dynamics simulations predicted that L507A formed additional interactions with DNA. Our study demonstrates how modifications in amino acid residues of DNA-binding domains enable next-generation reprogramming technology with engineered reprogramming factors.
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