ArticleMolecular and cellular biology1996
Pho85p, a cyclin-dependent protein kinase, and the Snf1p protein kinase act antagonistically to control glycogen accumulation in Saccharomyces cerevisiae.
Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 92 citations in OpenAlex.
- TheFrontiers in microbiology · 2022Article
- Conventional and emerging roles of the energy sensor Snf1/AMPK inMicrobial cell (Graz, Austria) · 2018Review
- Article
- Activation and inhibition of Snf1 kinase activity by phosphorylation within the activation loop.Biochimica et biophysica acta · 2016Article
- Coregulated expression of the Na+/phosphate Pho89 transporter and Ena1 Na+-ATPase allows their functional coupling under high-pH stress.Molecular and cellular biology · 2014Article
- Regulation of glycogen metabolism in yeast and bacteria.FEMS microbiology reviews · 2010Review
- The subcellular localization of yeast glycogen synthase is dependent upon glycogen content.Canadian journal of microbiology · 2010Article
- Promoter binding by the Adr1 transcriptional activator may be regulated by phosphorylation in the DNA-binding region.PloS one · 2008Article
- SNF1/AMPK pathways in yeast.Frontiers in bioscience : a journal and virtual library · 2008Review
- The minimum domain of Pho81 is not sufficient to control the Pho85-Rim15 effector branch involved in phosphate starvation-induced stress responses.Current genetics · 2005Article
- The molecular machinery of autophagy: unanswered questions.Journal of cell science · 2005Article
- Combinatorial control by the protein kinases PKA, PHO85 and SNF1 of transcriptional induction of the Saccharomyces cerevisiae GSY2 gene at the diauxic shift.Molecular genetics and genomics : MGG · 2004Article
- Mutations in the gal83 glycogen-binding domain activate the snf1/gal83 kinase pathway by a glycogen-independent mechanism.Molecular and cellular biology · 2004Article
- Regulation of the yeast amphiphysin homologue Rvs167p by phosphorylation.Molecular biology of the cell · 2003Article
- Article
- The GCR1 gene function is essential for glycogen and trehalose metabolism in Saccharomyces cerevisiae.Folia microbiologica · 2002Article
- Antagonistic controls of autophagy and glycogen accumulation by Snf1p, the yeast homolog of AMP-activated protein kinase, and the cyclin-dependent kinase Pho85p.Molecular and cellular biology · 2001Article
- Hyperactive glycogen synthase mutants of Saccharomyces cerevisiae suppress the glc7-1 protein phosphatase mutant.Journal of bacteriology · 2001Article
- The dual-specificity protein phosphatase Yvh1p regulates sporulation, growth, and glycogen accumulation independently of catalytic activity in Saccharomyces cerevisiae via the cyclic AMP-dependent protein kinase cascade.Journal of bacteriology · 2000Article
- Substrate targeting of the yeast cyclin-dependent kinase Pho85p by the cyclin Pcl10p.Molecular and cellular biology · 1999Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
In Saccharomyces cerevisiae, nutrient levels control multiple cellular processes. Cells lacking the SNF1 gene cannot express glucose-repressible genes and do not accumulate the storage polysaccharide glycogen. The impaired glycogen synthesis is due to maintenance of glycogen synthase in a hyperphosphorylated, inactive state. In a screen for second site suppressors of the glycogen storage defect of snf1 cells, we identified a mutant gene that restored glycogen accumulation and which was allelic with PHO85, which encodes a member of the cyclin-dependent kinase family. In cells with disrupted PHO85 genes, we observed hyperaccumulation of glycogen, activation of glycogen synthase, and impaired glycogen synthase kinase activity. In snf1 cells, glycogen synthase kinase activity was elevated. Partial purification of glycogen synthase kinase activity from yeast extracts resulted in the separation of two fractions by phenyl-Sepharose chromatography, both of which phosphorylated and inactivated glycogen synthase. The activity of one of these, GPK2, was inhibited by olomoucine, which potently inhibits cyclin-dependent protein kinases, and contained an approximately 36-kDa species that reacted with antibodies to Pho85p. Analysis of Ser-to-Ala mutations at the three potential Gsy2p phosphorylation sites in pho85 cells implicated Ser-654 and/or Thr-667 in PHO85 control of glycogen synthase. We propose that Pho85p is a physiological glycogen synthase kinase, possibly acting downstream of Snf1p.
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