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J. Biol. Chem., Vol. 282, Issue 5, 3282-3292, February 2, 2007

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YPI1 and SDS22 Proteins Regulate the Nuclear Localization and Function of Yeast Type 1 Phosphatase Glc7^*

Leda Pedelini¹, Maribel Marquina, Joaquin Ariño, Antonio Casamayor, Libia Sanz, Mathieu Bollen^¶, Pascual Sanz², and Maria Adelaida Garcia-Gimeno

From the Instituto de Biomedicina de Valencia, Consejo Superior de Investigaciones Científicas (CSIC), Jaime Roig 11, 46010 Valencia, Spain, the Department Bioquimica i Biologia Molecular, Facultat de Veterinària, Universitat Autònoma de Barcelona, 08193 Bellaterra, Barcelona, Spain, and the ^¶Department of Molecular Cell Biology, Faculty of Medicine, Catholic University of Leuven, Herestraat 49, B-3000 Leuven, Belgium

We have recently characterized Ypi1 as an inhibitory subunit of yeast Glc7 PP1 protein phosphatase. In this work we demonstrate that Ypi1 forms a complex with Glc7 and Sds22, another Glc7 regulatory subunit that targets the phosphatase to substrates involved in cell cycle control. Interestingly, the combination of equimolar amounts of Ypi1 and Sds22 leads to an almost full inhibition of Glc7 activity. Because YPI1 is an essential gene, we have constructed conditional mutants that demonstrate that depletion of Ypi1 leads to alteration of nuclear localization of Glc7 and cell growth arrest in mid-mitosis with aberrant mitotic spindle. These phenotypes mimic those produced upon inactivation of Sds22. The fact that progressive depletion of either Ypi1 or Sds22 resulted in similar physiological phenotypes and that both proteins inhibit the phosphatase activity of Glc7 strongly suggest a common role of these two proteins in regulating Glc7 nuclear localization and function.

Received for publication, July 28, 2006 , and in revised form, October 11, 2006.

The nucleotide sequence(s) reported in this paper has been submitted to the Gen-Bank^TM/EBI Data Bank with accession number(s) CAB11073 [GenBank] .

^* This work was supported in part by Grants BMC2002-00208 (to P. S.), BFU2004-01432 (to Juan Jose Calvete), BMC2002-04011-C05-04, BFU2005_06388-C4-04 (to J. A.), and BFU2004-00014 (to A. C.) from the Spanish Ministry of Education and Science and Fondo Europeo de Desarrollo Regional, an "Ajut de Suport als Grups de Recerca de Catalunya" Grant 2001SGR00193 (to J. A.), the Instituto de Salud Carlos III Network Grants RCMN C03/08 and RGDM G03/212 (to P. S.), Grant PNL2004-8 from Universitat Autònoma de Barcelona, and Grant MIRG-CT-2004-003794 from the European Commission (to A. C.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. 1.

¹ Supported by Predoctoral I3P Fellowship from the CSIC.

² To whom correspondence should be addressed. Tel.: 3496-3391779; Fax: 3496-3690800; E-mail: sanz{at}ibv.csic.es.

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