ArticlePLoS biology2024
IntAct: A nondisruptive internal tagging strategy to study the organization and function of actin isoforms.
Article in PLoS biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- IntAct-U-ExM enables super-resolution imaging of isoform-specific actin networks across species.PLoS biology · 2026Article
- ALFA nanobody-guided endogenous labeling.Nature chemical biology · 2025Article
- Functional fluorescence labeling of actins in live-cell system using engineered split-GFP technology.Molecular biology of the cell · 2025Article
- The complete absence of cytoplasmic γ-actin results in no discernible phenotype in mice or primary fibroblasts.The FEBS journal · 2025Article
- Intracellular protein editing enables incorporation of noncanonical residues in endogenous proteins.Science (New York, N.Y.) · 2025Article
- Structure of the F-tractin-F-actin complex.The Journal of cell biology · 2025Article
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10 authors at 3 institutions in 2 countries.
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Abstract
Mammals have 6 highly conserved actin isoforms with nonredundant biological functions. The molecular basis of isoform specificity, however, remains elusive due to a lack of tools. Here, we describe the development of IntAct, an internal tagging strategy to study actin isoforms in fixed and living cells. We identified a residue pair in β-actin that permits tag integration and used knock-in cell lines to demonstrate that IntAct β-actin expression and filament incorporation is indistinguishable from wild type. Furthermore, IntAct β-actin remains associated with common actin-binding proteins (ABPs) and can be targeted in living cells. We demonstrate the usability of IntAct for actin isoform investigations by showing that actin isoform-specific distribution is maintained in human cells. Lastly, we observed a variant-dependent incorporation of tagged actin variants into yeast actin patches, cables, and cytokinetic rings demonstrating cross species applicability. Together, our data indicate that IntAct is a versatile tool to study actin isoform localization, dynamics, and molecular interactions.
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