Cofilin is a Component of Intranuclear and Cytoplasmic Actin Rods Induced in Cultured Cells

Incubation of cultured cells under specific conditions induces a dramatic change in the actin organization: induction of intranuclear and/or cytoplasmic actin rods (actin paracrystal-like intracellular structures). We have found that cofilin, a 21-kDa actin-binding protein, is a component of these r...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1987-08, Vol.84 (15), p.5262-5266
Main Authors: Nishida, Eisuke, Iida, Kazuko, Yonezawa, Naoto, Koyasu, Shigeo, Yahara, Ichiro, Sakai, Hikoichi
Format: Article
Language:English
Subjects:
Actin Depolymerizing Factors
Actins
Actins - analysis
Actins - metabolism
Analytical, structural and metabolic biochemistry
Animals
Antibodies
Binding and carrier proteins
Binding, Competitive
Biological and medical sciences
Carrier Proteins - analysis
Cells
Cells, Cultured
Cultured cells
Cytoplasm - ultrastructure
Dimethyl Sulfoxide - pharmacology
Fibroblasts - ultrastructure
Fluorescent antibody techniques
Fundamental and applied biological sciences. Psychology
Gels
Gelsolin
Hot Temperature
Mice
Microfilament Proteins
Molecular Weight
Molecules
Nerve Tissue Proteins - analysis
Nerve Tissue Proteins - metabolism
Phalloidine - metabolism
Proteins
Stress fibers
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Summary:Incubation of cultured cells under specific conditions induces a dramatic change in the actin organization: induction of intranuclear and/or cytoplasmic actin rods (actin paracrystal-like intracellular structures). We have found that cofilin, a 21-kDa actin-binding protein, is a component of these rods. Antibodies directed against cofilin labeled intranuclear actin rods induced in cells treated with dimethyl sulfoxide or exposed to heat shock and also labeled cytoplasmic actin rods induced in cells incubated in specific salt buffers. Moreover, we found that these actin rods are not stained with fluorescent phalloidin derivatives at all and appear to be right-handed helices, different from straight bundles of F-actin such as stress fibers. In vitro experiments revealed that cofilin and phalloidin compete with each other for binding to F-actin. Since cofilin and phalloidin have the ability to stoichiometrically bind actin molecule in the filament in vitro, the above results seem to suggest that cofilin directly binds to actin molecule in nearly an equimolar ratio in these rods. We call these rods ``actin/cofilin rods.''
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.84.15.5262