ArticleBiophysical journal2014
Nucleotide regulation of the structure and dynamics of G-actin.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- The structure of an actin nucleus stabilized by villin.Science advances · 2025Article
- Histidine 73 methylation coordinates β-actin plasticity in response to key environmental factors.Nature communications · 2025Article
- Mechanisms and therapeutic potential of disulphidptosis in cancer.Cell proliferation · 2025Review
- Quantifying Unbiased Conformational Ensembles from Biased Simulations Using ShapeGMM.Journal of chemical theory and computation · 2024Article
- Effects of Nucleotide and End-Dependent Actin Conformations on Polymerization.Biophysical journal · 2020Article
- Foundations for a Realism-Based Ontology of Protein Aggregates.CEUR workshop proceedings · 2020Article
- D-loop Dynamics and Near-Atomic-Resolution Cryo-EM Structure of Phalloidin-Bound F-Actin.Structure (London, England : 1993) · 2020Article
- ADF/cofilin regulation from a structural viewpoint.Journal of muscle research and cell motility · 2020Review
- Multiscale simulation of actin filaments and actin-associated proteins.Biophysical reviews · 2018Review
- Insights into the Cooperative Nature of ATP Hydrolysis in Actin Filaments.Biophysical journal · 2018Article
- Structural basis for cofilin binding and actin filament disassembly.Nature communications · 2018Article
- Coarse-Grained Directed Simulation.Journal of chemical theory and computation · 2017Article
- Characterization of the flexibility of the peripheral stalk of prokaryotic rotary A-ATPases by atomistic simulations.Proteins · 2016Article
- Exploring Valleys without Climbing Every Peak: More Efficient and Forgiving Metabasin Metadynamics via Robust On-the-Fly Bias Domain Restriction.Journal of chemical theory and computation · 2015Article
- Structural basis of fast- and slow-severing actin-cofilactin boundaries.The Journal of biological chemistryArticle
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Actin, a highly conserved cytoskeletal protein found in all eukaryotic cells, facilitates cell motility and membrane remodeling via a directional polymerization cycle referred to as treadmilling. The nucleotide bound at the core of each actin subunit regulates this process. Although the biochemical kinetics of treadmilling has been well characterized, the atomistic details of how the nucleotide affects polymerization remain to be definitively determined. There is increasing evidence that the nucleotide regulation (and other characteristics) of actin cannot be fully described from the minimum energy structure, but rather depends on a dynamic equilibrium between conformations. In this work we explore the conformational mobility of the actin monomer (G-actin) in a coarse-grained subspace using umbrella sampling to bias all-atom molecular-dynamics simulations along the variables of interest. The results reveal that ADP-bound actin subunits are more conformationally mobile than ATP-bound subunits. We used a multiscale analysis method involving coarse-grained and atomistic representations of these simulations to characterize how the nucleotide affects the low-energy states of these systems. The interface between subdomains SD2-SD4, which is important for polymerization, is stabilized in an actin filament-like (F-actin) conformation in ATP-bound G-actin. Additionally, the nucleotide modulates the conformation of the SD1-SD3 interface, a region involved in the binding of several actin-binding proteins.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.