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Mol Cell Biol, August 1998, p. 4761-4771, Vol. 18, No. 8
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

RhoE Regulates Actin Cytoskeleton Organization and Cell Migration

Rosa M. Guasch,1 2 Peter Scambler,3 Gareth E. Jones,2 and Anne J. Ridley1 4 *

The Ludwig Institute for Cancer Research, London W1P 8BT,1 Muscle and Motility Research Centre, The Randall Institute, King's College London, London, WC2B 5RL,2 Institute of Child Health, London, WC1N 1EH,3 and Department of Biochemistry and Molecular Biology, University College London, London WC1E 6BT,4 United Kingdom

Received 29 December 1997/Returned for modification 5 February 1998/Accepted 3 May 1998

The actin cytoskeleton is regulated by Rho family proteins: in fibroblasts, Rho mediates the formation of actin stress fibers, whereas Rac regulates lamellipodium formation and Cdc42 controls filopodium formation. We have cloned the mouse RhoE gene, whose product is a member of the Rho family that shares (except in one amino acid) the conserved effector domain of RhoA, RhoB, and RhoC. RhoE is able to bind GTP but does not detectably bind GDP and has low intrinsic GTPase activity compared with Rac. The role of RhoE in regulating actin organization was investigated by microinjection in Bac1.2F5 macrophages and MDCK cells. In macrophages, RhoE induced actin reorganization, leading to the formation of extensions resembling filopodia and pseudopodia. In MDCK cells, RhoE induced the complete disappearance of stress fibers, together with cell spreading. However, RhoE did not detectably affect the actin bundles that run parallel to the outer membranes of cells at the periphery of colonies, which are known to be dependent on RhoA. In addition, RhoE induced an increase in the speed of migration of hepatocyte growth factor/scatter factor-stimulated MDCK cells, in contrast to the previously reported inhibition produced by activated RhoA. The subcellular localization of RhoE at the lateral membranes of MDCK cells suggests a role in cell-cell adhesion, as has been shown for RhoA. These results suggest that RhoE may act to inhibit signalling downstream of RhoA, altering some RhoA-regulated responses, such as stress fiber formation, but not affecting others, such as peripheral actin bundle formation.

* Corresponding author. Mailing address: The Ludwig Institute for Cancer Research, 91 Riding House St., London W1P 8BT, United Kingdom. Phone: (44)-171-878-4088. Fax: (44)-171-878-4040. E-mail: anne{at}ludwig.ucl.ac.uk.

Mol Cell Biol, August 1998, p. 4761-4771, Vol. 18, No. 8
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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