ArticleEuropean biophysics journal : EBJ2011
The effect of toxins on inorganic phosphate release during actin polymerization.
Article in European biophysics journal : EBJ, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Physical confinement modulates the rate-limiting transition in the release of phosphate from actin filaments.Science advances · 2026Article
- Physical Confinement Modulates the Rate-Limiting Transition in the Release of Phosphate from Actin Filaments.bioRxiv : the preprint server for biology · 2026Article
- Molecular mechanisms of inorganic-phosphate release from the core and barbed end of actin filaments.Nature structural & molecular biology · 2023Article
- Structure and function of Plasmodium actin II in the parasite mosquito stages.PLoS pathogens · 2023Article
- Towards a structural understanding of the remodeling of the actin cytoskeleton.Seminars in cell & developmental biology · 2020Review
- Structural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM.Nature structural & molecular biology · 2018Article
- Near-atomic structure of jasplakinolide-stabilized malaria parasite F-actin reveals the structural basis of filament instability.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
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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
During the polymerization of actin, hydrolysis of bound ATP occurs in two consecutive steps: chemical cleavage of the high-energy nucleotide and slow release of the γ-phosphate. In this study the effect of phalloidin and jasplakinolide on the kinetics of P(i) release was monitored during the formation of actin filaments. An enzyme-linked assay based spectrophotometric technique was used to follow the liberation of inorganic phosphate. It was verified that jasplakinolide reduced the P(i) release in the same way as phalloidin. It was not possible to demonstrate long-range allosteric effects of the toxins by release of P(i) from F-actin. The products of ATP hydrolysis were released by denaturation of the actin filaments. HPLC analysis of the samples revealed that the ATP in the toxin-bound region was completely hydrolysed into ADP and P(i). The effect of both toxins can be sufficiently explained by local and mechanical blockade of P(i) dissociation.
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