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EPLIN (Epithelial Protein Lost in Neoplasm) (Chang et al, 1998; Maul & Chang, 1999) has two or more actin-binding sites. EPLIN binds G- and F-actin (Maul et al, 2003). The actin-binding sites When over-expressed in culture cells stress fibres are increased in both number and size (Maul et al, 2003). EPLIN has no effect on the rate of spontaneous polymerization of pure actin not does it affect the on rate at the barbed ends, but it does inhibit depolymerization and the branching nucleation of the Arp2/3 complex (Maul et al, 2003).  The inhibition of depolymerization is in common with other actin bundling proteins such as p30kDa (Zigmond et al, 1992).
EPLIN contains a central LIM domain 



Chang, D. D., Park, N. H., Denny, C. T., Nelson, S. F. & Pe, M. (1998) Characterization of transformation related genes in oral cancer cells. Oncogene. 16, 1921-1930.

Maul, R. S. & Chang, D. D. (1999) EPLIN, epithelial protein lost in neoplasm. Oncogene. 18, 7838-7841.

Maul, R. S., Song, Y., Amann, K. J., Gerbin, S. C., Pollard, T. D. & Chang, D. D. (2003) EPLIN regulates actin dynamics by cross-linking and stabilizing filaments. J. Cell Biol. 160, 399-407.

Song, Y., Maul, R. S., Gerbin, C. S. & Chang, D. D. (2002) Inhibition of anchorage independent growth of transformed NIH3T3 cells by EPLIN is dependent on localization of EPLIN to the actin cytoskeleton. Mol Biol Cell. 13, 1408-1416.

Zigmond, S. H., Furukawa, R. & Fechheimer, M. (1992) Inhibition of Actin Filament Depolymerization by the Dictyostelium 30,000-D Actin-bundling Protein.  J.Cell Biol. 119, 559-567.

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