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Molecular and Cellular Biology, May 2003, p. 3116-3125, Vol. 23, No. 9
0270-7306/03/$08.00+0 DOI: 10.1128/MCB.23.9.3116-3125.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
Department of Pharmacology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213
Received 31 October 2002/ Returned for modification 11 December 2002/ Accepted 6 February 2003
In Saccharomyces cerevisiae, the Tor proteins mediate a wide spectrum of growth-related cellular processes in response to nutrients. The pleiotropic role of the Tor proteins is mediated, at least in part, by type 2A protein phosphatases (PP2A) and 2A-like protein phosphatases. Tor-mediated signaling activity promotes the interaction of phosphatase-interacting protein Tap42 with PP2A and 2A-like protein phosphatases. The distinct complexes formed between Tap42 and different phosphatases mediate various cellular events and modulate phosphorylation levels of many downstream factors in the Tor pathway in a Tor-dependent and rapamycin-sensitive manner. In this study, we demonstrate that the interaction between Tap42 and the catalytic subunits of PP2A (PP2Ac) is required for cell cycle-dependent distribution of actin. We show that mutations in PP2Ac and Tap42 that perturb the interaction cause random distribution of actin during the cell cycle and that overexpression of the Rho2 GTPase suppresses the actin defects associated with the mutants. Our findings suggest that the Tap42-PP2Ac complex regulates the actin cytoskeleton via a Rho GTPase-dependent mechanism. In addition, we provide evidence that PP2A activity plays a negative role in controlling the actin cytoskeleton and, possibly, in regulation of the G2/M transition of the cell cycle.
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