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Convergence of TOR-nitrogen and Snf1-glucose signaling pathways onto Gln3.
Bertram, Paula G; Choi, Jae H; Carvalho, John; Chan, Ting-Fung; Ai, Wandong; Zheng, X F Steven.
Afiliação
  • Bertram PG; Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110, USA.
Mol Cell Biol ; 22(4): 1246-52, 2002 Feb.
Article em En | MEDLINE | ID: mdl-11809814
ABSTRACT
Carbon and nitrogen are two basic nutrient sources for cellular organisms. They supply precursors for energy metabolism and metabolic biosynthesis. In the yeast Saccharomyces cerevisiae, distinct sensing and signaling pathways have been described that regulate gene expression in response to the quality of carbon and nitrogen sources, respectively. Gln3 is a GATA-type transcription factor of nitrogen catabolite-repressible (NCR) genes. Previous observations indicate that the quality of nitrogen sources controls the phosphorylation and cytoplasmic retention of Gln3 via the target of rapamycin (TOR) protein. In this study, we show that glucose also regulates Gln3 phosphorylation and subcellular localization, which is mediated by Snf1, the yeast homolog of AMP-dependent protein kinase and a cytoplasmic glucose sensor. Our data show that glucose and nitrogen signaling pathways converge onto Gln3, which may be critical for both nutrient sensing and starvation responses.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas Repressoras / Proteínas Fúngicas / Transdução de Sinais / Proteínas Serina-Treonina Quinases / Fosfatidilinositol 3-Quinases / Proteínas de Saccharomyces cerevisiae / Proteínas de Ligação a DNA / Glucose / Nitrogênio Idioma: En Revista: Mol Cell Biol Ano de publicação: 2002 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas Repressoras / Proteínas Fúngicas / Transdução de Sinais / Proteínas Serina-Treonina Quinases / Fosfatidilinositol 3-Quinases / Proteínas de Saccharomyces cerevisiae / Proteínas de Ligação a DNA / Glucose / Nitrogênio Idioma: En Revista: Mol Cell Biol Ano de publicação: 2002 Tipo de documento: Article País de afiliação: Estados Unidos