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Originally published In Press as doi:10.1074/jbc.M007039200 on October 16, 2000

J. Biol. Chem., Vol. 276, Issue 2, 875-883, January 12, 2001
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A New Family of Cdc42 Effector Proteins, CEPs, Function in Fibroblast and Epithelial Cell Shape Changes*

Dianne Snow Hirsch, Dana M. Pirone, and Peter D. BurbeloDagger

From the Department of Oncology, Lombardi Cancer Center, Georgetown University Medical Center, Washington, DC 20007

Cdc42, a Rho GTPase, regulates the organization of the actin cytoskeleton by its interaction with several distinct families of downstream effector proteins. Here, we report the identification of four new Cdc42-binding proteins that, along with MSE55, constitute a new family of effector proteins. These molecules, designated CEPs, contain three regions of homology, including a Cdc42 binding domain and two unique domains called CI and CII. Experimentally, we have verified that CEP2 and CEP5 bind Cdc42. Expression of CEP2, CEP3, CEP4, and CEP5 in NIH-3T3 fibroblasts induced pseudopodia formation. Fibroblasts coexpressing dominant negative Cdc42 with CEP2 or expressing a Cdc42/Rac interactive binding domain mutant of CEP2 did not induce pseudopodia formation. In primary keratinocytes, CEP2- and CEP5-expressing cells showed reduced F-actin localization at the adherens junctions with an increase in thin stress fibers that extended the length of the cell body. Keratinocytes expressing CEPs also showed an altered vinculin distribution and a loss of E-cadherin from adherens junctions. Similar effects were observed in keratinocytes expressing constitutively active Cdc42, but were not seen with a Cdc42/Rac interactive binding domain mutant of CEP2. These results suggest that CEPs act downstream of Cdc42 to induce actin filament assembly leading to cell shape changes.

* This work was supported by Grant R29-CA77459-01 (to P. D. B.) from the National Cancer Institute, by a predoctoral scholarship from the ARCs Foundation (to D. S. H.), and by a Department of Defense breast cancer predoctoral fellowship (to D. M. P.). The DNA sequencing and Microscopy core facilities of the Lombardi Cancer Center were funded by Grant P30-CA51008 from the National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF098290, AF104857, AF099664, and AF102773.

Dagger To whom correspondence should be addressed: Georgetown University Medical Center, Rm. EG16, New Research Bldg., Lombardi Cancer Center, 3970 Reservoir Rd., NW, Washington, DC 20007. Tel.: 202-687-1444; Fax: 202-687-7505; E-mail: burbelpd@gunet.georgetown.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.