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Understanding the role of the Vid30c in the nutrient-dependent turnover of hexose transporters in Saccharomyces cerevisiae

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Title: Understanding the role of the Vid30c in the nutrient-dependent turnover of hexose transporters in Saccharomyces cerevisiae
Author: Snowdon, Christopher
Department: Department of Molecular and Cellular Biology
Program: Molecular and Cellular Biology
Advisor: van der Merwe, George
Abstract: Saccharomyces cerevisiae is confronted with continually changing and diverse nutrient conditions. As such, it has adapted to utilize both a wide variety of nutrient sources and to preferentially use the most nutrient-rich source to obtain a competitive advantage. The transcription, intracellular trafficking and protein turnover of nutrient transporters, including the hexose transporter proteins (Hxts), are strictly regulated in response to nutrient conditions. The low affinity hexose transporter Hxt3p is highly expressed and localizes to the plasma membrane during growth in abundant glucose where it plays a major role in the transport of this sugar. However, following a shift to ethanol as a sole carbon source, Hxt3p is endocytosed and targeted to the vacuole for degradation while its expression is also repressed. In contrast, the high affinity hexose transporter Hxt7p is actively expressed and functional in the plasma membrane when glucose is limiting and nitrogen is abundant. Upon nitrogen starvation or rapamycin treatment, HXT7 transcription decreases and the protein is targeted for degradation. The mechanisms that govern these regulatory steps are poorly understood. The Vid and Gid proteins, several of which compose the Vid30 complex (Vid30c), facilitate the nutrient-dependent degradation of the gluconeogenic enzymes FBPase and Mdh2p when glucose-starved cells are replenished with glucose. Here we show that components of the Vid30c are needed for the ethanol-induced turnover of Hxt3p and the rapamycin or nitrogen starvation-induced degradation of Hxt7p. In addition, we demonstrate that the signals for the ethanol-induced turnover of Hxt3p and the rapamycin-induced turnover of Hxt7p converge on the Vid30c upstream of the Ras/cAMP/PKA pathway, ultimately controlling the degradation of both these hexose transporters. Finally, we provide evidence that the Vid30c controls the localization of the Ras GEF Cdc25p and may therefore directly regulate the activity of the Ras/cAMP/PKA pathway.
URI: http://hdl.handle.net/10214/3606
Date: 2012-04
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