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Literature DB >> 2393669

Phalloidin reduces the release of inorganic phosphate during actin polymerization.

Abstract

Phalloidin, an actin-filament stabilizing peptide from Amanita phalloides, did not inhibit ATP hydrolysis during actin polymerization but strongly retarded the release of the hydrolysis product Pi. Thus, the lifetime of the intermediate F-actin-ADP-Pi is significantly increased by phalloidin. The results suggest a close correlation between filament stability and F-actin-ADP-Pi intermediates.

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Year: 1990 PMID： 2393669 DOI： 10.1016/0304-4165(90)90116-e

Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002

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Cited

12 in total

1. Viscoelastic properties of f-actin, microtubules, f-actin/alpha-actinin, and f-actin/hexokinase determined in microliter volumes with a novel nondestructive method.

Authors: O Wagner; J Zinke; P Dancker; W Grill; J Bereiter-Hahn
Journal: Biophys J Date: 1999-05 Impact factor: 4.033

Phalloidin reduces the release of inorganic phosphate during actin polymerization.

1. Viscoelastic properties of f-actin, microtubules, f-actin/alpha-actinin, and f-actin/hexokinase determined in microliter volumes with a novel nondestructive method.

2. The effect of toxins on inorganic phosphate release during actin polymerization.

3. Stability and dynamics of G-actin: back-door water diffusion and behavior of a subdomain 3/4 loop.

4. Position and orientation of phalloidin in F-actin determined by X-ray fiber diffraction analysis.

5. Kinetics of the formation and dissociation of actin filament branches mediated by Arp2/3 complex.

6. Influence of phalloidin on the formation of actin filament branches by Arp2/3 complex.

7. Microinjection of Rap2B protein or RNA induces rearrangement of pigment granules in Xenopus oocytes.

8. Malaria parasite actin polymerization and filament structure.

Review 9. Actin in emerging neurites is recruited from a monomer pool.

10. Formins regulate actin filament flexibility through long range allosteric interactions.