ArticleBiophysical journal2000
Thymosin-beta(4) changes the conformation and dynamics of actin monomers.
Article in Biophysical journal, 2000. 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, 70 citations in OpenAlex.
- SH3BGRL proteins are thioredoxin fold-containing actin filament pointed end capping proteins (TPECs).Scientific reports · 2026Article
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- The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022Review
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- The Function of Oncogene B-Cell Lymphoma 6 in the Regulation of the Migration and Invasion of Trophoblastic Cells.International journal of molecular sciences · 2020Article
- Profilin choreographs actin and microtubules in cells and cancer.International review of cell and molecular biology · 2020Article
- Global Proteomics-based Identification and Validation of Thymosin Beta-4 X-Linked as a Prognostic Marker for Head and Neck Squamous Cell Carcinoma.Scientific reports · 2017Article
- Steric Effects Induce Geometric Remodeling of Actin Bundles in Filopodia.Biophysical journal · 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
- 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
- Dimeric WH2 domains in Vibrio VopF promote actin filament barbed-end uncapping and assisted elongation.Nature structural & molecular biology · 2013Article
- Interactions of isolated C-terminal fragments of neural Wiskott-Aldrich syndrome protein (N-WASP) with actin and Arp2/3 complex.The Journal of biological chemistry · 2012Article
- How a single residue in individual β-thymosin/WH2 domains controls their functions in actin assembly.The EMBO journal · 2012Article
- Molecular mechanism of Ena/VASP-mediated actin-filament elongation.The EMBO journal · 2011Article
- Conformational dynamics of actin: effectors and implications for biological function.Cytoskeleton (Hoboken, N.J.) · 2010Review
- The effects of ADF/cofilin and profilin on the conformation of the ATP-binding cleft of monomeric actin.Biophysical journal · 2009Article
- Effects of solution crowding on actin polymerization reveal the energetic basis for nucleotide-dependent filament stability.Journal of molecular biology · 2008Article
- Article
- Nucleotide-mediated conformational changes of monomeric actin and Arp3 studied by molecular dynamics simulations.Journal of molecular biology · 2008Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Thymosin-beta(4) (Tbeta(4)) binds actin monomers stoichiometrically and maintains the bulk of the actin monomer pool in metazoan cells. Tbeta(4) binding quenches the fluorescence of N-iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine (AEDANS) conjugated to Cys(374) of actin monomers. The K(d) of the actin-Tbeta(4) complex depends on the cation and nucleotide bound to actin but is not affected by the AEDANS probe. The different stabilities are determined primarily by the rates of dissociation. At 25 degrees C, the free energy of Tbeta(4) binding MgATP-actin is primarily enthalpic in origin but entropic for CaATP-actin. Binding is coupled to the dissociation of bound water molecules, which is greater for CaATP-actin than MgATP-actin monomers. Proteolysis of MgATP-actin, but not CaATP-actin, at Gly(46) on subdomain 2 is >12 times faster when Tbeta(4) is bound. The C terminus of Tbeta(4) contacts actin near this cleavage site, at His(40). By tritium exchange, Tbeta(4) slows the exchange rate of approximately eight rapidly exchanging amide protons on actin. We conclude that Tbeta(4) changes the conformation and structural dynamics ("breathing") of actin monomers. The conformational change may reflect the unique ability of Tbeta(4) to sequester actin monomers and inhibit nucleotide exchange.
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