ArticleJournal of bacteriology2001
Hyperactive glycogen synthase mutants of Saccharomyces cerevisiae suppress the glc7-1 protein phosphatase mutant.
Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Glycogen synthase activity inmSphere · 2024Article
- Article
- Article
- Genetic Regulators and Physiological Significance of Glycogen Storage inJournal of fungi (Basel, Switzerland) · 2019Article
- Circadian clock regulation of the glycogen synthase (Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Effect of nitrogen availability on the poly-3-D-hydroxybutyrate accumulation by engineered Saccharomyces cerevisiae.AMB Express · 2017Article
- A highly prevalent equine glycogen storage disease is explained by constitutive activation of a mutant glycogen synthase.Biochimica et biophysica acta. General subjects · 2017Article
- Regulation of glycogen metabolism in yeast and bacteria.FEMS microbiology reviews · 2010Review
- Genetic interaction network of the Saccharomyces cerevisiae type 1 phosphatase Glc7.BMC genomics · 2008Article
- Article
- 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
- Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
A yeast glc7-1 mutant expressing a variant of protein phosphatase type 1 fails to accumulate glycogen. This defect is associated with hyperphosphorylated and inactive glycogen synthase, consistent with Glc7p acting directly to dephosphorylate and activate glycogen synthase. To characterize the glycogen synthesis defect of this mutant in more detail, we isolated 26 pseudorevertants of the glc7-1 mutant. All pseudoreversion events were due to missense mutations in GSY2, the gene encoding the major isoform of glycogen synthase. A majority of the mutations responsible for the suppression were in the 3' end of the gene, corresponding to the phosphorylated COOH terminus of Gsy2p. Phosphorylation of the mutant proteins was reduced, suggesting that they are poor substrates for glycogen synthase kinases. Suppressor mutations outside this domain did not decrease the phosphorylation of the resulting proteins, indicating that these proteins are immune to the regulatory effects of phosphorylation. Since no growth defect has been observed for strains with altered glycogen levels, the relative levels of fitness of GSY2 mutants that fail to accumulate glycogen and that hyperaccumulate glycogen were assayed by cocultivation experiments. A wild-type strain outcompeted both hypo- and hyperaccumulating strains, suggesting that glycogen levels contribute substantially to the fitness of yeast.
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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.