PMID: 8944781Nov 1, 1996Paper

In vivo phosphorylation of actin in Physarum polycephalum. Study of the substrate specificity of the actin-fragmin kinase

European Journal of Biochemistry
V De CorteJ Vandekerckhove

Abstract

Actin-fragmin is a heterodimeric protein complex from Physarum polycephalum microplasmodia that is phosphorylated in vitro at residues Thr203 and Thr202 of the actin subunit by the endogenous actin-fragmin kinase. Following phosphorylation, the F-actin capping activity of the complex becomes Ca(2+)-dependent, suggesting a fundamental regulatory role in controlling F-actin growth [Gettemans, J., De Ville, Y., Waelkens E. and Vandekerckhove, J. (1995) J. Biol. Chem. 270, 2644-2651]. In this study we analysed actin phosphorylation in vivo. We demonstrate that the actin-fragmin complex constitutes the only substrate of the actin-fragmin kinase in plasmodia. Monomeric actin is not phosphorylated. Immunoprecipitation of actin-fragmin reveals that approximately 40% of the actin subunit of the complex is phosphorylated in vivo. However, using purified substrate and kinase, the complex can be quantitatively phosphorylated as judged by two-dimensional gel electrophoresis. Through comparative phosphopeptide fingerprinting, we show that the phosphorylation sites in vivo are identical to those identified in vitro. We additionally characterized a complex of actin and the NH2-terminal half of fragmin (residues 1-168) that is also phosphorylat...Continue Reading

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Citations

Oct 26, 2005·PLoS Computational Biology·Eric D Scheeff, Philip E Bourne
Feb 26, 2003·Cell Motility and the Cytoskeleton·Luo GuJing Chen
Dec 24, 2005·Cell Motility and the Cytoskeleton·Yuki ShiraiKimiko Murakami-Murofushi
Feb 17, 1998·Biochemical and Biophysical Research Communications·K FuruhashiK Titani

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