ArticleBiophysical journal2009
The effects of ADF/cofilin and profilin on the conformation of the ATP-binding cleft of monomeric actin.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 28 citations in OpenAlex.
- FGF-Mediated Axon Guidance: Role of Downstream Signaling Pathways in Cytoskeletal Control.Cells · 2025Review
- Cdk12 maintains the integrity of adult axons by suppressing actin remodeling.Cell death discovery · 2023Article
- Mammalian and malaria parasite cyclase-associated proteins catalyze nucleotide exchange on G-actin through a conserved mechanism.The Journal of biological chemistry · 2013Article
- Actin-binding Rho activating protein is expressed in the central nervous system of normal adult rats.Neural regeneration research · 2012Article
- Crystal structures explain functional differences in the two actin depolymerization factors of the malaria parasite.The Journal of biological chemistry · 2011Article
- Conformational dynamics of actin: effectors and implications for biological function.Cytoskeleton (Hoboken, N.J.) · 2010Review
- A nucleotide state-sensing region on actin.The Journal of biological chemistry · 2010Article
- Actin remodeling by ADF/cofilin is required for cargo sorting at the trans-Golgi network.The Journal of cell biology · 2009Article
- Profilin is associated with transcriptionally active genes.Nucleus (Austin, Tex.)Article
- Actin Filament Barbed-End Depolymerization by Combined Action of Profilin, Cofilin, and Twinfilin.PRX lifeArticle
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Actin depolymerizing factor (ADF)/cofilin and profilin are small actin-binding proteins, which have central roles in cytoskeletal dynamics in all eukaryotes. When bound to an actin monomer, ADF/cofilins inhibit the nucleotide exchange, whereas most profilins accelerate the nucleotide exchange on actin monomers. In this study the effects of ADF/cofilin and profilin on the accessibility of the actin monomer's ATP-binding pocket was investigated by a fluorescence spectroscopic method. The fluorescence of the actin bound epsilon-ATP was quenched with a neutral quencher (acrylamide) in steady-state and time dependent experiments, and the data were analyzed with a complex form of the Stern-Volmer equation. The experiments revealed that in the presence of ADF/cofilin the accessibility of the bound epsilon-ATP decreased, indicating a closed and more compact ATP-binding pocket induced by the binding of ADF/cofilin. In the presence of profilin the accessibility of the bound epsilon-ATP increased, indicating a more open and approachable protein matrix around the ATP-binding pocket. The results of the fluorescence quenching experiments support a structural mechanism regarding the regulation of the nucleotide exchange on actin monomers by ADF/cofilin and profilin.
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