ArticleMolecular biology of the cell2020
F-actin-bundling sites are conserved in proteins with villin-type headpiece domains.
Article in Molecular biology of the cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 8 citations in OpenAlex.
- GSK3β-driven phosphorylation of ABLIM1 regulates its interactions with titin cardiac muscle.The Journal of general physiology · 2025Article
- Bsp1, a fungal CPI motif protein, regulates actin filament capping in endocytosis and cytokinesis.Molecular biology of the cell · 2024Article
- The Potential for Targeting AVIL and Other Actin-Binding Proteins in Rhabdomyosarcoma.International journal of molecular sciences · 2023Article
- Targeting AVIL, a New Cytoskeleton Regulator in Glioblastoma.International journal of molecular sciences · 2021Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Villin is a major actin-bundling protein that assembles the brush border of intestinal and renal epithelial cells. The villin "headpiece" domain and the actin-binding residues within it regulate its actin-bundling function. Substantial experimental and theoretical information about the three-dimensional structure of the isolated villin headpiece, including a description of the actin-binding residues within the headpiece, is available. Despite that, the actin-bundling site in the full-length (FL) villin protein remains unidentified. We used this existing villin headpiece nuclear magnetic resonance data and performed mutational analysis and functional assays to identify the actin-bundling site in FL human villin protein. By careful evaluation of these conserved actin-binding residues in human advillin protein, we demonstrate their functional significance in the over 30 proteins that contain a villin-type headpiece domain. Our study is the first that combines the available structural data on villin headpiece with functional assays to identify the actin-binding residues in FL villin that regulate its filament-bundling activity. Our findings could have wider implications for other actin-bundling proteins that contain a villin-type headpiece domain.
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Registered trials
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