ArticleNature communications2022
Magic angle spinning NMR structure of human cofilin-2 assembled on actin filaments reveals isoform-specific conformation and binding mode.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
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- Actin isoform-specific interactions revealed byProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Dipolar Recoupling in Rotating Solids.Chemical reviews · 2024Review
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- Stabilization of F-actin by Salmonella effector SipA resembles the structural effects of inorganic phosphate and phalloidin.Structure (London, England : 1993) · 2024Article
- Review
- Stabilization of F-actin bybioRxiv : the preprint server for biology · 2023Article
- Troponin and a Myopathy-Linked Mutation inInternational journal of molecular sciences · 2023Article
- Performance efficient macromolecular mechanics via sub-nanometer shape based coarse graining.Nature communications · 2023Article
- Actin Bundles Dynamics and Architecture.Biomolecules · 2023Review
- Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Actin polymerization dynamics regulated by actin-binding proteins are essential for various cellular functions. The cofilin family of proteins are potent regulators of actin severing and filament disassembly. The structural basis for cofilin-isoform-specific severing activity is poorly understood as their high-resolution structures in complex with filamentous actin (F-actin) are lacking. Here, we present the atomic-resolution structure of the muscle-tissue-specific isoform, cofilin-2 (CFL2), assembled on ADP-F-actin, determined by magic-angle-spinning (MAS) NMR spectroscopy and data-guided molecular dynamics (MD) simulations. We observe an isoform-specific conformation for CFL2. This conformation is the result of a unique network of hydrogen bonding interactions within the α2 helix containing the non-conserved residue, Q26. Our results indicate F-site interactions that are specific between CFL2 and ADP-F-actin, revealing mechanistic insights into isoform-dependent F-actin disassembly.
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