ArticleThe Journal of biological chemistry2011
Subunit and domain requirements for adenylate-mediated protection of Snf1 kinase activation loop from dephosphorylation.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 33 citations in OpenAlex.
- Article
- Modelling of glucose repression signalling in yeast Saccharomyces cerevisiae.FEMS yeast research · 2022Review
- D-Xylose Sensing inInternational journal of molecular sciences · 2021Review
- Article
- Conventional and emerging roles of the energy sensor Snf1/AMPK inMicrobial cell (Graz, Austria) · 2018Review
- Single-cell study links metabolism with nutrient signaling and reveals sources of variability.BMC systems biology · 2017Article
- Quantitative proteomics reveals novel protein interaction partners of PP2A catalytic subunit in pancreatic β-cells.Molecular and cellular endocrinology · 2016Article
- Cross-Talk between Carbon Metabolism and the DNA Damage Response in S. cerevisiae.Cell reports · 2015Article
- Network reconstruction and validation of the Snf1/AMPK pathway in baker's yeast based on a comprehensive literature review.NPJ systems biology and applications · 2015Article
- Mechanisms of regulation of SNF1/AMPK/SnRK1 protein kinases.Frontiers in plant science · 2014Review
- Ptc1 protein phosphatase 2C contributes to glucose regulation of SNF1/AMP-activated protein kinase (AMPK) in Saccharomyces cerevisiae.The Journal of biological chemistry · 2013Article
- SUMOylation regulates the SNF1 protein kinase.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Ligand binding to the AMP-activated protein kinase active site mediates protection of the activation loop from dephosphorylation.The Journal of biological chemistry · 2013Article
- Reciprocal phosphorylation of yeast glycerol-3-phosphate dehydrogenases in adaptation to distinct types of stress.Molecular and cellular biology · 2012Article
- PAS kinase: integrating nutrient sensing with nutrient partitioning.Seminars in cell & developmental biology · 2012Review
- Heterotrimer-independent regulation of activation-loop phosphorylation of Snf1 protein kinase involves two protein phosphatases.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- AMPK: a nutrient and energy sensor that maintains energy homeostasis.Nature reviews. Molecular cell biology · 2012Review
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Members of the AMP-activated protein kinase (AMPK) family are activated by phosphorylation at a conserved threonine residue in the activation loop of the kinase domain. Mammalian AMPK adopts a phosphatase-resistant conformation that is stabilized by binding low energy adenylate molecules. Similarly, binding of ADP to the Snf1 complex, yeast AMPK, protects the kinase from dephosphorylation. Here, we determined the nucleotide specificity of the ligand-mediated protection from dephosphorylation and demonstrate the subunit and domain requirements for this reaction. Protection from dephosphorylation was highly specific for adenine nucleotides, with ADP being the most effective ligand for mediating protection. The full-length α subunit (Snf1) was not competent for ADP-mediated protection, confirming the requirement for the regulatory β and γ subunits. However, Snf1 heterotrimeric complexes that lacked either the glycogen-binding domain of Gal83 or the linker region of the α subunit were competent for ADP-mediated protection. In contrast, adenylate-mediated protection of recombinant human AMPK was abolished when a portion of the linker region containing the α-hook domain was deleted. Therefore, the exact means by which the different adenylate nucleotides are distinguished by the Snf1 enzyme may differ compared with its mammalian ortholog.
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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.