title: The AMPK/SNF1/SnRK1 fuel gauge and energy regulator: structure, function and regulation.
abstract: All life forms on earth require a continuous input and monitoring of carbon and energy supplies. The AMP-activated kinase (AMPK)/sucrose non-fermenting1 (SNF1)/Snf1-related kinase1 (SnRK1) protein kinases are evolutionarily conserved metabolic sensors found in all eukaryotic organisms from simple unicellular fungi (yeast SNF1) to animals (AMPK) and plants (SnRK1). Activated by starvation and energy-depleting stress conditions, they enable energy homeostasis and survival by up-regulating energy-conserving and energy-producing catabolic processes, and by limiting energy-consuming anabolic metabolism. In addition, they control normal growth and development as well as metabolic homeostasis at the organismal level. As such, the AMPK/SNF1/SnRK1 kinases act in concert with other central signaling components to control carbohydrate uptake and metabolism, fatty acid and lipid biosynthesis and the storage of carbon energy reserves. Moreover, they have a tremendous impact on developmental processes that are triggered by environmental changes such as nutrient depletion or stress. Although intensive research by many groups has partly unveiled the factors that regulate AMPK/SNF1/SnRK1 kinase activity as well as the pathways and substrates they control, several fundamental issues still await to be clarified. In this review, we will highlight these issues and focus on the structure, function and regulation of the AMPK/SNF1/SnRK1 kinases.
authors: Department of Biology, Laboratory for Functional Biology, Katholieke Universiteit Leuven, Heverlee, Belgium.
authors: Ruben
authors: R
authors: Ghillebert
authors: Erwin
authors: E
authors: Swinnen
authors: Jing
authors: J
authors: Wen
authors: Lies
authors: L
authors: Vandesteene
authors: Matthew
authors: M
authors: Ramon
authors: Koen
authors: K
authors: Norga
authors: Filip
authors: F
authors: Rolland
authors: Joris
authors: J
authors: Winderickx
mesh_terms: D000091162:AMP-Activated Protein Kinase Kinases; D000494:Allosteric Regulation; D020134:Catalytic Domain; D004734:Energy Metabolism; D006706:Homeostasis; D010766:Phosphorylation; D011487:Protein Conformation; D011494:Protein Kinases / Q000737:chemistry / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D011494:Protein Kinases; C490994:SNRK protein, human; D017346:Protein Serine-Threonine Kinases; D000091162:AMP-Activated Protein Kinase Kinases