ArticleNature structural & molecular biology2022
Bound nucleotide can control the dynamic architecture of monomeric actin.
Article in Nature structural & molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Structure and mechanism of an actin-dependent bacterial phosphoryl AMPylase.Nature chemical biology · 2026Article
- Histidine 73 methylation coordinates β-actin plasticity in response to key environmental factors.Nature communications · 2025Article
- Absolute and Relative Binding Free Energy Calculations of Nucleotides to Multiple Protein Classes.Journal of chemical theory and computation · 2025Article
- Cryo-EM structures of cardiac muscle α-actin mutants M305L and A331P give insights into the structural mechanisms of hypertrophic cardiomyopathy.European journal of cell biology · 2024Article
- Spa2 remodels ADP-actin via molecular condensation under glucose starvation.Nature communications · 2024Article
- Structural insights into actin isoforms.eLife · 2023Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Polymerization of actin into cytoskeletal filaments is coupled to its bound adenine nucleotides. The mechanism by which nucleotide modulates actin functions has not been evident from analyses of ATP- and ADP-bound crystal structures of the actin monomer. We report that NMR chemical shift differences between the two forms are globally distributed. Furthermore, microsecond-millisecond motions are spread throughout the molecule in the ATP form, but largely confined to subdomains 1 and 2, and the nucleotide binding site in the ADP form. Through these motions, the ATP- and ADP-bound forms sample different high-energy conformations. A deafness-causing, fast-nucleating actin mutant populates the high-energy conformer of ATP-actin more than the wild-type protein, suggesting that this conformer may be on the pathway to nucleation. Together, the data suggest a model in which differential sampling of a nucleation-compatible form of the actin monomer may contribute to control of actin filament dynamics by nucleotide.
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Registered trials
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