ArticleThe EMBO journal2012
How a single residue in individual β-thymosin/WH2 domains controls their functions in actin assembly.
Article in The EMBO journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 58 citations in OpenAlex.
- Optical Control of G-Actin with a Photoswitchable Latrunculin.Journal of the American Chemical Society · 2024Article
- Functional and structural insights into the multi-step activation and catalytic mechanism of bacterial ExoY nucleotidyl cyclase toxins bound to actin-profilin.PLoS pathogens · 2023Article
- FuzPred: a web server for the sequence-based prediction of the context-dependent binding modes of proteins.Nucleic acids research · 2023Article
- Thymosin β4 is essential for thrombus formation by controlling the G-actin/F-actin equilibrium in platelets.Haematologica · 2022Article
- Folding and self-assembly of short intrinsically disordered peptides and protein regions.Nanoscale advances · 2021Review
- Putative Coiled-Coil Domain-Dependent Autoinhibition and Alternative Splicing Determine SHTN1's Actin-Binding Activity.Journal of molecular biology · 2020Article
- Cloning, Expression and Effects ofInternational journal of molecular sciences · 2019Article
- Long Noncoding RNA CRYBG3 Blocks Cytokinesis by Directly Binding G-Actin.Cancer research · 2018Article
- The activities of the C-terminal regions of the formin protein disheveled-associated activator of morphogenesis (DAAM) in actin dynamics.The Journal of biological chemistry · 2017Article
- Actin activates Pseudomonas aeruginosa ExoY nucleotidyl cyclase toxin and ExoY-like effector domains from MARTX toxins.Nature communications · 2016Article
- Utilization of paramagnetic relaxation enhancements for structural analysis of actin-binding proteins in complex with actin.Scientific reports · 2016Article
- Role of the C-terminal Extension of Formin 2 in Its Activation by Spire Protein and Processive Assembly of Actin Filaments.The Journal of biological chemistry · 2016Article
- Biochemical Activities of the Wiskott-Aldrich Syndrome Homology Region 2 Domains of Sarcomere Length Short (SALS) Protein.The Journal of biological chemistry · 2016Article
- Emerging applications of small angle solution scattering in structural biology.Protein science : a publication of the Protein Society · 2015Review
- Filament assembly by Spire: key residues and concerted actin binding.Journal of molecular biology · 2015Article
- Investigating increasingly complex macromolecular systems with small-angle X-ray scattering.IUCrJ · 2014Review
- Structural basis of thymosin-β4/profilin exchange leading to actin filament polymerization.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Disordered proteinaceous machines.Chemical reviews · 2014Review
- Article
- Structural basis of actin filament nucleation by tandem W domains.Cell reports · 2013Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
β-Thymosin (βT) and WH2 domains are widespread, intrinsically disordered actin-binding peptides that display significant sequence variability and different regulations of actin self-assembly in motile and morphogenetic processes. Here, we reveal the structural mechanisms by which, in their 1:1 stoichiometric complexes with actin, they either inhibit assembly by sequestering actin monomers like Thymosin-β4, or enhance motility by directing polarized filament assembly like Ciboulot βT. We combined mutational, functional or structural analysis by X-ray crystallography, SAXS (small angle X-ray scattering) and NMR on Thymosin-β4, Ciboulot, TetraThymosinβ and the long WH2 domain of WASP-interacting protein. The latter sequesters G-actin with the same molecular mechanisms as Thymosin-β4. Functionally different βT/WH2 domains differ by distinct dynamics of their C-terminal half interactions with G-actin pointed face. These C-terminal interaction dynamics are controlled by the strength of electrostatic interactions with G-actin. At physiological ionic strength, a single salt bridge with actin located next to their central LKKT/V motif induces G-actin sequestration in both isolated long βT and WH2 domains. The results open perspectives for elucidating the functions of βT/WH2 domains in other modular proteins.
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