SNF1/AMPK pathways in yeast.

  title={SNF1/AMPK pathways in yeast.},
  author={Kristina Hedbacker and Marian Carlson},
  journal={Frontiers in bioscience : a journal and virtual library},
The SNF1/AMPK family of protein kinases is highly conserved in eukaryotes and is required for energy homeostasis in mammals, plants, and fungi. SNF1 protein kinase was initially identified by genetic analysis in the budding yeast Saccharomyces cerevisiae. SNF1 is required primarily for the adaptation of yeast cells to glucose limitation and for growth on carbon sources that are less preferred than glucose, but is also involved in responses to other environmental stresses. SNF1 regulates… 

Figures from this paper

Mechanisms of regulation of SNF1/AMPK/SnRK1 protein kinases

Current knowledge on the regulation of SNF1/AMPK/SnRK1 by upstream components, post-translational modifications, various metabolites, hormones, and others are reviewed in an attempt to highlight both the commonalities of these essential eukaryotic kinases and the divergences that have evolved to cope with the particularities of each one of these systems.

Dynamic regulation of the Mig1 transcriptional repressor under glucose de/repression

It is found that regardless of glucose availability Mig1 is present in the cytoplasm and the nucleus as monomer and oligomers, and it is suggested that eukaryotic gene regulation is mediated through transcription factors which act as multimeric clusters, which provides novel concepts in understanding of the AMPK/Snf1 signal transduction pathway.

Phosphoproteomic analysis identifies proteins involved in transcription-coupled mRNA decay as targets of Snf1 signaling

To understand Snf1-mediated signaling, quantitative mass spectrometry was used to identify proteins that were phosphorylated in a Snf 1-dependent manner and identified 210 Snf2-dependent phosphopeptides in 145 proteins, including several proteins involved in mRNA metabolism.

Snf1 Phosphorylates Adenylate Cyclase and Negatively Regulates Protein Kinase A-dependent Transcription in Saccharomyces cerevisiae *

It is shown that Snf1 and adenylate cyclase (Cyr1) interact in a nutrient-independent manner, and this is the first evidence of regulation of PKA pathway by Snf 1/AMPK.

Conventional and emerging roles of the energy sensor Snf1/AMPK in Saccharomyces cerevisiae

Here, available data on conventional and non-conventional functions of Snf1 are reviewed and integrated to better understand the complexity of cellular physiology which controls energy homeostasis.

The regulation of Saccharomyces cerevisiae Snf1 protein kinase on glucose utilization is in a glucose-dependent manner

Exploring the regulatory mechanism of Snf1 in glucose metabolism in different concentrations of glucose can provide insights into the study of the global regulatory mechanism in yeast and can help to better understand the complexity of physiological response of cells to stresses.

The regulation of Saccharomyces cerevisiae Snf1 protein kinase on glucose utilization is in a glucose-dependent manner

Snf1 regulates glucose metabolism in a glucose-dependent manner, which is associated with the different regulation on activation, localization, and signal pathways of Snf1 by varied glucose.

Protein kinase Snf1 is involved in the proper regulation of the unfolded protein response in Saccharomyces cerevisiae.

The results reveal that Snf1 plays an important role in the attenuation of the UPR, as well as identifying the protein kinase and its effectors as possible pharmacological targets for human diseases that are associated with insufficient UPR activation.

Snf1/AMPK promotes S-phase entrance by controlling CLB5 transcription in budding yeast

Novel findings are presented indicating that Snf1, the key regulator of cellular energy, is also involved in yeast cell cycle control, and a previously unrecognized role for Snf 1 in transcriptional modulation of the G1 to S transition is described, differing from the reported AMPK role in controlling the G 1/S transition in multicellular eukaryotes.

Protein Kinase A Contributes to the Negative Control of Snf1 Protein Kinase in Saccharomyces cerevisiae

The results suggest that PKA, which integrates multiple regulatory inputs, could contribute to Snf1 regulation under various conditions via a complex mechanism and support the view that, like its mammalian counterpart, AMP-activated protein kinase (AMPK), yeast Snf 1 participates in metabolic checkpoint control that coordinates growth with nutrient availability.



Nitrogen Availability and TOR Regulate the Snf1 Protein Kinase in Saccharomyces cerevisiae

Evidence is presented that Snf1 is directly involved in nitrogen signaling and negatively regulated by the rapamycin-sensitive TOR kinase which plays essential roles in signaling nitrogen and amino acid availability, and other evidence implicateSnf1 in the integration of signals regarding nitrogen and carbon stress.

Glucose regulates protein interactions within the yeast SNF1 protein kinase complex.

Using the two-hybrid system, it is shown that interaction between SNF1 and SNF4 is strongly regulated by the glucose signal and that homologs of theSNF1 kinase complex respond to regulatory signals by analogous mechanisms.

Elm1p Is One of Three Upstream Kinases for the Saccharomyces cerevisiae SNF1 Complex

Regulation of Snf1 Protein Kinase in Response to Environmental Stress*

It was shown that Snf1 protein kinase is regulated differently during adaptation of cells to NaCl and alkaline pH with respect to both temporal regulation of activation and subcellular localization, which could contribute to specificity of the stress responses.

Regulation of Snf1 Kinase

The data indicate that activation of the Snf1 kinase complex involves two steps, one that requires a distinct upstream kinase and one that is mediated by the γ subunit of the kinase itself.

Yeast SNF1 is functionally related to mammalian AMP-activated protein kinase and regulates acetyl-CoA carboxylase in vivo.

SNF1 undergoes a time-dependent increase in activity during growth in glucose-derepressing conditions, providing the first evidence that SNF1 activity is regulated by the level of available glucose.

Mammalian AMP-activated protein kinase is homologous to yeast and plant protein kinases involved in the regulation of carbon metabolism.

The primary sequence of rat AMPK is reported and antibodies raised against synthetic peptides based on the deduced sequence of AMPK immunoprecipitate AMPK activity from rat liver extracts suggest that AMPK may be involved in the regulation of a wide range of metabolic pathways.

Glucose-regulated interaction of a regulatory subunit of protein phosphatase 1 with the Snf1 protein kinase in Saccharomyces cerevisiae.

A model in which protein phosphatase 1, targeted by Reg1, facilitates the conformational change of the kinase complex from its active state to the autoinhibited state is proposed, indicating that Snf1 negatively regulates its own interaction with Reg1.

Yeast SNF1 protein kinase interacts with SIP4, a C6 zinc cluster transcriptional activator: a new role for SNF1 in the glucose response

Evidence thatSNF1 modulates function of a transcriptional activator, SIP4, which was identified in a two-hybrid screen for interaction with SNF1 is reported, providing the first direct evidence for a role of SNF 1 in activating transcription in response to glucose limitation.