title: The plant energy sensor: evolutionary conservation and divergence of SnRK1 structure, regulation, and function.
abstract: The SnRK1 (SNF1-related kinase 1) kinases are the plant cellular fuel gauges, activated in response to energy-depleting stress conditions to maintain energy homeostasis while also gatekeeping important developmental transitions for optimal growth and survival. Similar to their opisthokont counterparts (animal AMP-activated kinase, AMPK, and yeast Sucrose Non-Fermenting 1, SNF), they function as heterotrimeric complexes with a catalytic (kinase) α subunit and regulatory β and γ subunits. Although the overall configuration of the kinase complexes is well conserved, plant-specific structural modifications (including a unique hybrid βγ subunit) and associated differences in regulation reflect evolutionary divergence in response to fundamentally different lifestyles. While AMP is the key metabolic signal activating AMPK in animals, the plant kinases appear to be allosterically inhibited by sugar-phosphates. Their function is further fine-tuned by differential subunit expression, localization, and diverse post-translational modifications. The SnRK1 kinases act by direct phosphorylation of key metabolic enzymes and regulatory proteins, extensive transcriptional regulation (e.g. through bZIP transcription factors), and down-regulation of TOR (target of rapamycin) kinase signaling. Significant progress has been made in recent years. New tools and more directed approaches will help answer important fundamental questions regarding their structure, regulation, and function, as well as explore their potential as targets for selection and modification for improved plant performance in a changing environment.
authors.affiliation: Laboratory for Molecular Plant Biology, Biology Department, University of Leuven-KU Leuven, Kasteelpark Arenberg 31, 3001 Heverlee-Leuven, Belgium.
authors.forename: Tom
authors.initials: T
authors.lastname: Broeckx
authors.affiliation: Laboratory for Molecular Plant Biology, Biology Department, University of Leuven-KU Leuven, Kasteelpark Arenberg 31, 3001 Heverlee-Leuven, Belgium.
authors.forename: Sander
authors.initials: S
authors.lastname: Hulsmans
authors.affiliation: Laboratory for Molecular Plant Biology, Biology Department, University of Leuven-KU Leuven, Kasteelpark Arenberg 31, 3001 Heverlee-Leuven, Belgium filip.rolland@bio.kuleuven.be.
authors.forename: Filip
authors.initials: F
authors.lastname: Rolland
mesh_terms: D000818:Animals; D005075:Biological Evolution; D004734:Energy Metabolism / Q000235:genetics / Q000502:physiology*; D018506:Gene Expression Regulation, Plant / Q000235:genetics / Q000502:physiology; D006706:Homeostasis / Q000235:genetics / Q000502:physiology; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000502:physiology*
chemical_list: C071570:SNF1-related protein kinases; D017346:Protein Serine-Threonine Kinases
keywords: AMPK; Arabidopsis; SNF1; SnRK1; TOR; energy sensing; trehalose-6-P.