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J Biol Chem, Vol. 274, Issue 25, 17757-17762, June 18, 1999

Morphological Changes and Detachment of Adherent Cells Induced by p122, a GTPase-activating Protein for Rho

Masayuki SekimataDagger , Yukihito KabuyamaDagger , Yasufumi Emori§, and Yoshimi HommaDagger

From the Dagger  Department of Biomolecular Sciences, Institute of Biomedical Sciences, Fukushima Medical College, 1 Hikariga-oka, Fukushima 960-1295 and the § Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Bunkyo, Tokyo 113-0033, Japan

We recently cloned a novel signaling molecule, p122, that shows a GTPase-activating activity specific for Rho and the ability to enhance the phosphatidylinositol 4,5-bisphosphate-hydrolyzing activity of phospholipase C delta 1 in vitro. Here we analyzed the in vivo function of p122. Microinjection of the GTPase-activating domain of p122 suppressed the formation of stress fibers and focal adhesions induced by lysophosphatidic acid, suggesting a GTPase-activating activity for Rho as in in vitro. Transfection of p122 also induced the disassembly of stress fibers and the morphological rounding of various adherent cells. Analyses using deletion and point mutants demonstrated that the GTPase-activating domain of p122 is responsible for the morphological changes and detachment and that arginine residues at positions 668 and 710 and a lysine residue at position 706 in the GTPase-activating domain are essential. Using Fluo-3-based Ca2+ microscopy, we found that p122 evoked a rapid elevation of intracellular Ca2+ levels, suggesting that p122 stimulates the phosphatidylinositol 4,5-bisphosphate-hydrolyzing activity of phospholipase C delta 1. These results demonstrate that p122 synergistically functions as a GTPase-activating protein specific for Rho and an activator of phospholipase C delta 1 in vivo and induces morphological changes and detachment through cytoskeletal reorganization.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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