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MBC in Press, published online ahead of print February 22, 2002
Mol. Biol. Cell 10.1091/mbc.01-08-0414

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Submitted on August 20, 2001
Revised on January 17, 2002
Accepted on January 18, 2002

Inhibition of anchorage independent growth of transformed NIH3T3 cells by EPLIN requires localization of EPLIN to the actin cytoskeleton

Yuhong Song1, Raymond S. Maul1, C. Sachi Gerbin1, and David D. Chang2*

1 Department of Medicine, Microbiology, Immunology and Molecular Genetics, Jonsson Comprehensive Cancer Center, and Molecular Biology Institute, UCLA School of Medicine, 10833 Le Conte Avenue, Los Angeles, California 90095
2 UCLA School of Medicine, Division of Heme-Onc, Factor 11-934, 10833 Le Conte Avenue, Los Angeles, CA 90095-1678

* Corresponding author. E-mail address: ddchang{at}mednet.ucla.edu.

EPLIN is a cytoskeleton-associated protein characterized by the presence of a single centrally located LIM domain. We have reported previously that EPLIN is down regulated in transformed cells. In this study, we have investigated whether ectopic expression of EPLIN affects transformation. In untransformed NIH3T3 cells, retroviral-mediated transduction of EPLIN did not alter the cell morphology or growth. NIH3T3 cells expressing EPLIN, however, failed to form colonies when transformed by the activated Cdc42 or the chimeric nuclear oncogene EWS/Fli-1. This suppression of anchorage independent growth was not universal as EPLIN failed to inhibit the colony formation of Ras transformed cells. Interestingly, the localization of EPLIN to the actin cytoskeleton was maintained in the EWS/Fli-1 or Cdc42 transformed cells, but not in Ras transformed cells where it was distributed heterogeneously in the cytoplasm. Using truncated EPLIN constructs, we demonstrated that the NH2-terminal region of EPLIN is necessary for both the localization of EPLIN to the actin cytoskeleton and suppression of anchorage independent growth of EWS/Fli-1 transformed cells. The LIM domain or the COOH-terminal region of EPLIN could be deleted without affecting its cytoskeletal localization or ability to suppress anchorage dependent growth. Our study indicates EPLIN may function in growth control by associating with and regulating the actin cytoskeleton.




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R. S. Maul, Y. Song, K. J. Amann, S. C. Gerbin, T. D. Pollard, and D. D. Chang
EPLIN regulates actin dynamics by cross-linking and stabilizing filaments
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