ArticleBiochimica et biophysica acta2016
Activation and inhibition of Snf1 kinase activity by phosphorylation within the activation loop.
Article in Biochimica et biophysica acta, 2016. 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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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Phosphorylation of Golgin Imh1 by AMPK/Snf1 compromises Golgi compartmentalization by releasing Arl1-Imh1 axis.Molecular biology of the cell · 2025Article
- Proteomic consequences of TDA1 deficiency in Saccharomyces cerevisiae: Protein kinase Tda1 is essential for Hxk1 and Hxk2 serine 15 phosphorylation.Scientific reports · 2022Article
- SCP4-STK35/PDIK1L complex is a dual phospho-catalytic signaling dependency in acute myeloid leukemia.Cell reports · 2022Article
- Kog1/Raptor mediates metabolic rewiring during nutrient limitation by controlling SNF1/AMPK activity.Science advances · 2021Article
- Septin Assembly and Remodeling at the Cell Division Site During the Cell Cycle.Frontiers in cell and developmental biology · 2021Review
- Spontaneous mutations that confer resistance to 2-deoxyglucose act through Hxk2 and Snf1 pathways to regulate gene expression and HXT endocytosis.PLoS genetics · 2020Article
- A Snf1-related nutrient-responsive kinase antagonizes endocytosis in yeast.PLoS genetics · 2020Article
- Fine-Tuning of Energy Levels RegulatesFrontiers in physiology · 2020Article
- Regulation and metabolic engineering strategies for permeases of Saccharomyces cerevisiae.World journal of microbiology & biotechnology · 2019Review
- Conventional and emerging roles of the energy sensor Snf1/AMPK inMicrobial cell (Graz, Austria) · 2018Review
- Article
- Compensatory Internalization of Pma1 in V-ATPase Mutants inGenetics · 2018Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The AMP-activated protein kinase is a metabolic regulator that transduces information about energy and nutrient availability. In yeast, the AMP-activated protein kinase, called Snf1, is activated when energy and nutrients are scarce. Earlier studies have demonstrated that activation of Snf1 requires the phosphorylation of the activation loop on threonine 210. Here we examined the regulation of Snf1 kinase activity in response to phosphorylation at other sites. Phosphoproteomic studies have identified numerous phosphorylation sites within the Snf1 kinase enzyme. We made amino acid substitutions in the Snf1 protein that were either non-phosphorylatable (serine to alanine) or phospho-mimetic (serine to glutamate) and examined the effects of these changes on Snf1 kinase function in vivo and on its catalytic activity in vitro. We found that changes to most of the phosphorylation sites had no effect on Snf1 kinase function. However, changes to serine 214, a site within the kinase activation loop, inhibited Snf1 kinase activity. Snf1-activating kinase 1 still phosphorylates Snf1-S214E on threonine 210 but the S214E enzyme is non-functional in vivo and catalytically inactive in vitro. We conclude that yeast have developed two distinct pathways for down-regulating Snf1 activity. The first is through direct dephosphorylation of the conserved activation loop threonine. The second is through phosphorylation of serine 214.
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