PMID:15247235

Citation	Crespo, JL, Helliwell, SB, Wiederkehr, C, Demougin, P, Fowler, B, Primig, M and Hall, MN (2004) NPR1 kinase and RSP5-BUL1/2 ubiquitin ligase control GLN3-dependent transcription in Saccharomyces cerevisiae. J. Biol. Chem. 279:37512-7
Abstract	The GATA transcription factors GLN3 and GAT1 activate nitrogen-regulated genes in Saccharomyces cerevisiae. NPR1 is a protein kinase that controls post-Golgi sorting of amino acid permeases. In the presence of a good nitrogen source, TOR (target of rapamycin) maintains GLN3 and NPR1 phosphorylated and inactive by inhibiting the type 2A-related phosphatase SIT4. We identified NPR1 as a regulator of GLN3. Specifically, loss of NPR1 causes nuclear translocation and activation of GLN3, but not GAT1, in nitrogen-rich conditions. NPR1-mediated inhibition of GLN3 is independent of the phosphatase SIT4. We also demonstrate that the E3/E4 ubiquitin-protein ligase proteins RSP5 and BUL1/2 are required for GLN3 activation under poor nitrogen conditions. Thus, NPR1 and BUL1/2 antagonistically control GLN3-dependent transcription, suggesting a role for regulated ubiquitination in the control of nutrient-responsive transcription.
Links	PubMed Online version:10.1074/jbc.M407372200
Keywords	Adaptor Proteins, Signal Transducing/physiology; Endosomal Sorting Complexes Required for Transport; Nitrogen/physiology; Proline/metabolism; Protein Kinases/physiology; Repressor Proteins/genetics; Saccharomyces cerevisiae/enzymology; Saccharomyces cerevisiae Proteins/genetics; Saccharomyces cerevisiae Proteins/physiology; Sirolimus/pharmacology; Transcription Factors/genetics; Transcription, Genetic/physiology; Ubiquitin-Protein Ligase Complexes/physiology; Ubiquitin-Protein Ligases
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