ArticleEukaryotic cell2011
Interaction of SNF1 protein kinase with its activating kinase Sak1.
Article in Eukaryotic cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 30 citations in OpenAlex.
- SNF1/AMPK controls its own localization by phosphorylating its activating kinase Sak1.iScience · 2026Article
- Nutrient sensing and transceptor-mediated metabolic control in yeast.FEMS yeast research · 2026Review
- Nitrogen limitation causes a seismic shift in redox state and phosphorylation of proteins implicated in carbon flux and lipidome remodeling in Rhodotorula toruloides.Biotechnology for biofuels and bioproducts · 2025Article
- Glucose metabolism in the pathogenic free-living amoebae: Tempting targets for treatment development.Chemical biology & drug design · 2024Review
- The polyHIS Tract of Yeast AMPK Coordinates Carbon Metabolism with Iron Availability.International journal of molecular sciences · 2023Article
- Article
- Protein kinases Elm1 and Sak1 of Saccharomyces cerevisiae exerted different functions under high-glucose and heat shock stresses.Applied microbiology and biotechnology · 2022Article
- The regulation of Saccharomyces cerevisiae Snf1 protein kinase on glucose utilization is in a glucose-dependent manner.Current genetics · 2021Review
- Role of Elm1, Tos3, and Sak1 Protein Kinases in the Maltose Metabolism of Baker's Yeast.Frontiers in microbiology · 2021Article
- Increased mitochondrial respiration promotes survival from endoplasmic reticulum stress.Cell death and differentiation · 2019Article
- Article
- Hexokinase 2 Is an Intracellular Glucose Sensor of Yeast Cells That Maintains the Structure and Activity of Mig1 Protein Repressor Complex.The Journal of biological chemistry · 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
- Protein kinase A is part of a mechanism that regulates nuclear reimport of the nuclear tRNA export receptors Los1p and Msn5p.Eukaryotic cell · 2014Article
- Crosstalk between SNF1 pathway and the peroxisome-mediated lipid metabolism in Magnaporthe oryzae.PloS one · 2014Article
- 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
- 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
- Protein kinase A contributes to the negative control of Snf1 protein kinase in Saccharomyces cerevisiae.Eukaryotic cell · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The Saccharomyces cerevisiae SNF1 protein kinase, a member of the SNF1/AMP-activated protein kinase (AMPK) family, is activated by three kinases, Sak1, Tos3, and Elm1, which phosphorylate the Snf1 catalytic subunit on Thr-210 in response to glucose limitation and other stresses. Sak1 is the primary Snf1-activating kinase and is associated with Snf1 in a complex. Here we examine the interaction of Sak1 with SNF1. We report that Sak1 coimmunopurifies with the Snf1 catalytic subunit from extracts of both glucose-replete and glucose-limited cultures and that interaction occurs independently of the phosphorylation state of Snf1 Thr-210, Snf1 catalytic activity, and other SNF1 subunits. Sak1 interacts with the Snf1 kinase domain, and nonconserved sequences C terminal to the Sak1 kinase domain mediate interaction with Snf1 and augment the phosphorylation and activation of Snf1. The Sak1 C terminus is modified in response to glucose depletion, dependent on SNF1 activity. Replacement of the C terminus of Elm1 (or Tos3) with that of Sak1 enhanced the ability of the Elm1 kinase domain to interact with and phosphorylate Snf1. These findings indicate that the C terminus of Sak1 confers its function as the primary Snf1-activating kinase and suggest that the physical association of Sak1 with SNF1 facilitates responses to environmental change.
Indexed as
Identifiers
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.