ArticleThe Journal of biological chemistry2013
Ligand binding to the AMP-activated protein kinase active site mediates protection of the activation loop from dephosphorylation.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 33 citations in OpenAlex.
- Identification of kinase modulators as host-directed therapeutics against intracellular methicillin-resistantFrontiers in cellular and infection microbiology · 2024Article
- BAY-3827 and SBI-0206965: Potent AMPK Inhibitors That Paradoxically Increase Thr172 Phosphorylation.International journal of molecular sciences · 2023Article
- Review
- Article
- Nuclear UHRF1 is a gate-keeper of cellular AMPK activity and function.Cell research · 2022Article
- Mig1 localization exhibits biphasic behavior which is controlled by both metabolic and regulatory roles of the sugar kinases.Molecular genetics and genomics : MGG · 2020Article
- The Regulatory Role of Key Metabolites in the Control of Cell Signaling.Biomolecules · 2020Review
- Fine-Tuning of Energy Levels RegulatesFrontiers in physiology · 2020Article
- Coordinated regulation of intracellular pH by two glucose-sensing pathways in yeast.The Journal of biological chemistry · 2018Article
- Single-cell study links metabolism with nutrient signaling and reveals sources of variability.BMC systems biology · 2017Article
- The yeast Hsp70 homolog Ssb: a chaperone for general de novo protein folding and a nanny for specific intrinsically disordered protein domains.Current genetics · 2017Review
- The β subunit of yeast AMP-activated protein kinase directs substrate specificity in response to alkaline stress.Cellular signalling · 2016Article
- The Hsp70 homolog Ssb and the 14-3-3 protein Bmh1 jointly regulate transcription of glucose repressed genes in Saccharomyces cerevisiae.Nucleic acids research · 2016Article
- Regulation of AMP-activated protein kinase by natural and synthetic activators.Acta pharmaceutica Sinica. B · 2016Review
- Snf1 Phosphorylates Adenylate Cyclase and Negatively Regulates Protein Kinase A-dependent Transcription in Saccharomyces cerevisiae.The Journal of biological chemistry · 2015Article
- Less is more: Nutrient limitation induces cross-talk of nutrient sensing pathways with NADFrontiers in biology · 2015Article
- Genetic analysis of resistance and sensitivity to 2-deoxyglucose in Saccharomyces cerevisiae.Genetics · 2014Article
- Yeast AMP-activated protein kinase monitors glucose concentration changes and absolute glucose levels.The Journal of biological chemistry · 2014Article
- Nutrient sensing and signaling in the yeast Saccharomyces cerevisiae.FEMS microbiology reviews · 2014Review
- Mechanisms of regulation of SNF1/AMPK/SnRK1 protein kinases.Frontiers in plant science · 2014Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The AMP-activated protein kinase (AMPK) is a conserved signaling molecule in a pathway that maintains adenosine triphosphate homeostasis. Recent studies have suggested that low energy adenylate ligands bound to one or more sites in the γ subunit of AMPK promote the formation of an active, phosphatase-resistant conformation. We propose an alternative model in which the kinase domain association with the heterotrimer core results in activation of the kinase catalytic activity, whereas low energy adenylate ligands bound in the kinase active site promote phosphatase resistance. Purified Snf1 α subunit with a conservative, single amino acid substitution in the kinase domain is protected from dephosphorylation by adenosine diphosphate in the complete absence of the β and γ subunits. Staurosporine, a compound known to bind to the active site of many protein kinases, mediates strong protection from dephosphorylation to yeast and mammalian AMPK enzymes. The analog-sensitive Snf1-I132G protein but not wild type Snf1 exhibits protection from dephosphorylation when bound by the adenosine analog 2NM-PP1 in vitro and in vivo. These data demonstrate that ligand binding to the Snf1 active site can mediate phosphatase resistance. Finally, Snf1 kinase with an amino acid substitution at the interface of the kinase domain and the heterotrimer core exhibits normal regulation of phosphorylation in vivo but greatly reduced Snf1 kinase activity, supporting a model in which kinase domain association with the heterotrimer core is needed for kinase activation.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.