Protein phosphatase 2A inhibitors, phoslactomycins. Effects on the cytoskeleton in NIH/3T3 cells

Usui, Takeo ; Marriott, Gerard ; Inagaki, Masaki ; Swarup, Ghanshyam ; Osada, Hiroyuki (1999) Protein phosphatase 2A inhibitors, phoslactomycins. Effects on the cytoskeleton in NIH/3T3 cells Journal of Biochemistry, 125 (5). pp. 960-965. ISSN 0021-924X

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Official URL: http://jb.oxfordjournals.org/content/125/5/960.sho...

Abstract

Protein phosphorylation is a key regulatory mechanism of the organization and dynamics of the actin cytoskeleton during cell motility, differentiation, and cytokinesis. The level of protein phosphorylation is dependent on the relative activities of both protein kinases and protein phosphatases. In this paper, we examined the effect of phoslactomycins (PLMs) on the regulation of the cytoskeleton of NIH/3T3 fibroblasts. Treatment of cells with PLM-F (10 μ M) induced actin filament depolymerization after 4 h. This effect was reversible and actin filaments were reformed 1 h after removal of the inhibitors. As PLM-F had no effect at all on polymerization of purified actin in vitro, it is thought that PLMs induce actin depolymerization through an indirect mechanism. An in vitro assay showed PLMs inhibited protein phosphatase 2A at lower concentrations (IC50 4.7 μ M) than protein phosphatase 1. An in situ phosphorylation assay also revealed that PLM-F treatment stimulated the phosphorylation of intracellular vimentin. These results suggest that phoslactomycins are protein phosphatase 2A-specific inhibitors and that protein phosphatase 2A is involved in regulation of the organization of the actin cytoskeleton.

Item Type:Article
Source:Copyright of this article belongs to Oxford University Press.
Keywords:Actin; Protein Phosphatase 1; Protein Phosphatase 2A Site-specific Phosphorylated Antibodies; Vimentin
ID Code:54451
Deposited On:11 Aug 2011 10:48
Last Modified:11 Aug 2011 10:48

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