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J. Biol. Chem., Vol. 282, Issue 7, 4485-4493, February 16, 2007

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Hxk2 Regulates the Phosphorylation State of Mig1 and Therefore Its Nucleocytoplasmic Distribution^*

From the Departamento de Bioquímica y Biología Molecular, Universidad de Oviedo, Campus del Cristo, Edificio Santiago Gascón, 33006 Oviedo, Spain

Mig1 and Hxk2 are two major mediators of glucose repression in Saccharomyces cerevisiae. However, the mechanism by which Hxk2 participates in the glucose repression signaling pathway is not completely understood. Recently, it has been demonstrated that Hxk2 interacts with Mig1 to generate a repressor complex located in the nucleus of S. cerevisiae. However, the mechanism by which Mig1 favors the presence of Hxk2 in the nucleus is not clear, and the function of Hxk2 at the nuclear repressor complex level is still unknown. Here, we report that serine 311 of Mig1 is a critical residue for interaction with Hxk2 and that this interaction is regulated by glucose. Our findings suggest that Snf1 interacts constitutively with the Hxk2 component of the repressor complex at high and low glucose conditions. Furthermore, we show that Snf1 binds to Mig1 under low glucose conditions and that binding is largely abolished after a shift to high glucose medium. We found that phosphorylation of serine 311 of Mig1 by Snf1 kinase is essential for Mig1 protein nuclear export and derepression of the SUC2 gene in glucose-limited cells. These results allow postulating that the Hxk2 operates by interacting both with Mig1 and Snf1 to inhibit the Mig1 phosphorylation at serine 311 during high glucose grown.

Received for publication, July 19, 2006 , and in revised form, December 12, 2006.

^* This work was supported in part by the Ministerio de Educación y Ciencia, Dirección General de Investigación (MEC-DGI), Spain (Grant BFU2004-02855-C0202). 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.

¹ Present address: Departamento de Ingeniería Bioquímica, Escuela Nacional de Ciencias Biológicas, Instituto Politécnico Nacional, 11340 México D.F., México.

² Both authors contributed equally to this work.

³ Supported by the Fundación Carolina (Spain).

⁴ Supported by the MEC-DGI (Spain).

⁵ Supported by the FICYT (Fundación para el Fomento en Asturias de la Investigación Científica Aplicada y la Tecnología), Spain.

⁶ To whom correspondence should be addressed: Tel.: 34-985-103-567; Fax: 34-985-103-157; E-mail: fmoreno{at}uniovi.es.

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