ArticleEukaryotic cell2010
Differential roles of the glycogen-binding domains of beta subunits in regulation of the Snf1 kinase complex.
Article in Eukaryotic cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- SNF1/AMPK controls its own localization by phosphorylating its activating kinase Sak1.iScience · 2026Article
- Integrative Phosphoproteomic and Proteomic Analysis ofJournal of proteome research · 2025Article
- A Suppressor Mutation in the β-Subunit Kis1 Restores Functionality of the SNF1 Complex inmSphere · 2021Article
- Drug resistance in diploid yeast is acquired through dominant alleles, haploinsufficiency, gene duplication and aneuploidy.PLoS genetics · 2021Article
- Integrated transcriptome and miRNA analysis uncovers molecular regulators of aerial stem-to-rhizome transition in the medical herb Gynostemma pentaphyllum.BMC genomics · 2019Article
- Laboratory evolution for forced glucose-xylose co-consumption enables identification of mutations that improve mixed-sugar fermentation by xylose-fermenting Saccharomyces cerevisiae.FEMS yeast research · 2018Article
- The β subunit of yeast AMP-activated protein kinase directs substrate specificity in response to alkaline stress.Cellular signalling · 2016Article
- Activation and inhibition of Snf1 kinase activity by phosphorylation within the activation loop.Biochimica et biophysica acta · 2016Article
- Structural and functional basis for starch binding in the SnRK1 subunits AKINβ2 and AKINβγ.Frontiers in plant science · 2014Article
- The hybrid four-CBS-domain KINβγ subunit functions as the canonical γ subunit of the plant energy sensor SnRK1.The Plant journal : for cell and molecular biology · 2013Article
- The β-subunit of the SnRK1 complex is phosphorylated by the plant cell death suppressor Adi3.Plant physiology · 2012Article
- Subunit and domain requirements for adenylate-mediated protection of Snf1 kinase activation loop from dephosphorylation.The Journal of biological chemistry · 2011Article
- Reg1 protein regulates phosphorylation of all three Snf1 isoforms but preferentially associates with the Gal83 isoform.Eukaryotic cell · 2011Article
- Transcriptional responses to glucose in Saccharomyces cerevisiae strains lacking a functional protein kinase A.BMC genomics · 2011Article
- Ubp8 and SAGA regulate Snf1 AMP kinase activity.Molecular and cellular biology · 2011Article
- Regulation of glycogen metabolism in yeast and bacteria.FEMS microbiology reviews · 2010Review
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5 authors at 1 institution in 1 country.
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Abstract
Members of the AMP-activated protein kinase family, including the Snf1 kinase of Saccharomyces cerevisiae, are activated under conditions of nutrient stress. AMP-activated protein kinases are heterotrimeric complexes composed of a catalytic alpha subunit and regulatory beta and gamma subunits. In this study, the role of the beta subunits in the regulation of Snf1 activity was examined. Yeasts express three isoforms of the AMP-activated protein kinase consisting of Snf1 (alpha), Snf4 (gamma), and one of three alternative beta subunits, either Sip1, Sip2, or Gal83. The Gal83 isoform of the Snf1 complex is the most abundant and was analyzed in the greatest detail. All three beta subunits contain a conserved domain referred to as the glycogen-binding domain. The deletion of this domain from Gal83 results in a deregulation of the Snf1 kinase, as judged by a constitutive activity independent of glucose availability. In contrast, the deletion of this homologous domain from the Sip1 and Sip2 subunits had little effect on Snf1 kinase regulation. Therefore, the different Snf1 kinase isoforms are regulated through distinct mechanisms, which may contribute to their specialized roles in different stress response pathways. In addition, the beta subunits are subjected to phosphorylation. The responsible kinases were identified as being Snf1 and casein kinase II. The significance of the phosphorylation is unclear since the deletion of the region containing the phosphorylation sites in Gal83 had little effect on the regulation of Snf1 in response to glucose limitation.
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