Conventional and emerging roles of the energy sensor Snf1/AMPK in Saccharomyces cerevisiae
| Autor: | Raffaele Nicastro, Paola Coccetti, Farida Tripodi |
|---|---|
| Přispěvatelé: | Coccetti, P, Nicastro, R, Tripodi, F |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Cell physiology Anabolism Saccharomyces cerevisiae Biochemistry Genetics and Molecular Biology (miscellaneous) Microbiology Applied Microbiology and Biotechnology Energy homeostasis 03 medical and health sciences Virology Genetics endocytosis budding yeast lcsh:QH301-705.5 Molecular Biology Endocytosi biology Effector aging fungi AMPK stress response Cell Biology biology.organism_classification Yeast Cell biology carbohydrates (lipids) 030104 developmental biology lcsh:Biology (General) DNA damage cell cycle Parasitology Signal transduction transcription signaling glucose repression metabolism |
| Zdroj: | Microbial Cell, Vol 5, Iss 11, Pp 482-494 (2018) |
| ISSN: | 2311-2638 |
| DOI: | 10.15698/mic2018.11.655 |
| Popis: | All proliferating cells need to match metabolism, growth and cell cycle progression with nutrient availability to guarantee cell viability in spite of a changing environment. In yeast, a signaling pathway centered on the effector kinase Snf1 is required to adapt to nutrient limitation and to utilize alternative carbon sources, such as sucrose and ethanol. Snf1 shares evolutionary conserved functions with the AMP-activated Kinase (AMPK) in higher eukaryotes which, activated by energy depletion, stimulates catabolic processes and, at the same time, inhibits anabolism. Although the yeast Snf1 is best known for its role in responding to a number of stress factors, in addition to glucose limitation, new unconventional roles of Snf1 have recently emerged, even in glucose repressing and unstressed conditions. Here, we review and integrate available data on conventional and non-conventional functions of Snf1 to better understand the complexity of cellular physiology which controls energy homeostasis. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|