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Journal ArticleDOI

Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I

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TLDR
A simple and selective assay for monomeric and filamentous actin is presented, based on the inhibition of DNAase I by actin, which is rapid enough to detect changes in the polymerization state of actin in vitro over time intervals as short as 3 min.
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This article is published in Cell.The article was published on 1978-11-01. It has received 536 citations till now. The article focuses on the topics: Filamentous actin & Actin-binding protein.

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Actin Depolymerizing Factor (ADF/Cofilin) Enhances the Rate of Filament Turnover: Implication in Actin-based Motility

TL;DR: The function of ADF is not to sequester G-actin, but uses ATP hydrolysis in actin assembly to enhance filament dynamics and increase in the rate of actin-based motile processes.
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Proteins of the ADF/Cofilin Family: Essential Regulators of Actin Dynamics

TL;DR: Although vertebrate ADF/cofilins contain a nuclear localization sequence, they are usually concentrated in regions containing dynamic actin pools, such as the leading edge of migrating cells and neuronal growth cones.
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Mechanism of action of cytochalasin B on actin

TL;DR: 2 microM CB strongly reduces the low shear viscosity of actin filaments alone and actin Filaments cross-linked by a variety of macromolecules, which may be due to inhibition of act in filament-filament interactions which normally contribute to network formation.
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DNase expression allows the pathogen group A Streptococcus to escape killing in neutrophil extracellular traps.

TL;DR: A significant role for NETs in neutrophil-mediated innate immunity is demonstrated, and a novel therapeutic target against invasive GAS infection is identified.
References
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Journal ArticleDOI

Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells.

TL;DR: It is proposed that reversible association of actin with profilin in the cell may provide a mechanism for storage of monomeric actin and controlled turnover of microfilaments.
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Actin Is the Naturally Occurring Inhibitor of Deoxyribonuclease I

TL;DR: The observation that actin can be isolated by DNase-agarose affinity chromatography provides a useful tool for the biochemical study of actin under different physiological conditions.
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Immunological characterization of the subunit of the 100 A filaments from muscle cells.

TL;DR: It is believed that this new protein functions in muscle primarily as a three dimensional matrix which interconnects individual myofibrils to one another and to the plasma membrane at the level of their Z lines.
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Studies on the function and composition of the 10-NM(100-A) filaments of vertebrate smooth muscle.

TL;DR: Data indicate that the 10-nm filaments are not essential for contraction, but rather form a specialized intracellular cytoskeleton in smooth muscle and, as appears likely, in other cell types the filament protein has been tentatively termed 'skeletin'.
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The polymerization of actin: its role in the generation of the acrosomal process of certain echinoderm sperm.

TL;DR: The sperm actin was shown to be localized in the microfilaments in the acrosomal processes by heavy meromyosin binding in situ, and when unreacted sperm were lysed with the detergent Triton X-100 and the state of the actin in the sperm extract was analyzed by centrifugation, it was determined that at least 80% of the acting sperm was in the monomeric state.
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