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Open Access Research article

Role of casein kinase 1 in the glucose sensor-mediated signaling pathway in yeast

Satish Pasula13, Samujjwal Chakraborty1, Jae H Choi2 and Jeong-Ho Kim1*

Author affiliations

1 The Mississippi Functional Genomics Network, Department of Biological Sciences, The University of Southern Mississippi, 118 College Dr, Hattiesburg, MS 39406, USA

2 University of Illinois at Chicago College of Pharmacy, Department of Medicinal Chemistry and Pharmacognosy, Rockford Regional Program, 1601 Parkview Avenue, Rockford, IL 61107, USA

3 Oklahoma Medical Research Foundation, 825 N.E. 13th Street, Oklahoma City, Oklahoma 73104, USA

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Citation and License

BMC Cell Biology 2010, 11:17  doi:10.1186/1471-2121-11-17

Published: 7 March 2010

Abstract

Background

In yeast, glucose-dependent degradation of the Mth1 protein, a corepressor of the glucose transporter gene (HXT) repressor Rgt1, is a crucial event enabling expression of several HXT. This event occurs through a signaling pathway that involves the Rgt2 and Snf3 glucose sensors and yeast casein kinase 1 and 2 (Yck1/2). In this study, we examined whether the glucose sensors directly couple with Yck1/2 to convert glucose binding into an intracellular signal that leads to the degradation of Mth1.

Results

High levels of glucose induce degradation of Mth1 through the Rgt2/Snf3 glucose signaling pathway. Fluorescence microscopy analysis indicates that, under glucose-limited conditions, GFP-Mth1 is localized in the nucleus and does not shuttle between the nucleus and cytoplasm. If glucose-induced degradation is prevented due to disruption of the Rgt2/Snf3 pathway, GFP-Mth1 accumulates in the nucleus. When engineered to be localized to the cytoplasm, GFP-Mth1 is degraded regardless of the presence of glucose or the glucose sensors. In addition, removal of Grr1 from the nucleus prevents degradation of GFP-Mth1. These results suggest that glucose-induced, glucose sensor-dependent Mth1 degradation occurs in the nucleus. We also show that, like Yck2, Yck1 is localized to the plasma membrane via C-terminal palmitoylation mediated by the palmitoyl transferase Akr1. However, glucose-dependent degradation of Mth1 is not impaired in the absence of Akr1, suggesting that a direct interaction between the glucose sensors and Yck1/2 is not required for Mth1 degradation.

Conclusion

Glucose-induced, glucose sensor-regulated degradation of Mth1 occurs in the nucleus and does not require direct interaction of the glucose sensors with Yck1/2.