ArticleMolecular biology of the cell2016
Glutathione depletion activates the yeast vacuolar transient receptor potential channel, Yvc1p, by reversible glutathionylation of specific cysteines.
Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 10 papers.
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10 citing papers in PubMed, 29 citations in OpenAlex.
- Characterizing heterologous protein burden in Komagataella phaffii.FEMS yeast research · 2025Article
- The versatility of the putative transient receptor potential ion channels in regulating the calcium signaling inmSphere · 2023Article
- Intermittent dietary methionine deprivation facilitates tumoral ferroptosis and synergizes with checkpoint blockade.Nature communications · 2023Article
- Calcium Ion Channels inJournal of fungi (Basel, Switzerland) · 2023Review
- Calmodulin kinase 2 genetically interacts with Rch1p to negatively regulate calcium import into Saccharomyces cerevisiae after extracellular calcium pulse.Archives of microbiology · 2022Article
- A Systematic Survey of Characteristic Features of Yeast Cell Death Triggered by External Factors.Journal of fungi (Basel, Switzerland) · 2021Review
- Oxidative Stress Responses and Nutrient Starvation in MCHM TreatedG3 (Bethesda, Md.) · 2020Article
- In Vivo Imaging with Genetically Encoded Redox Biosensors.International journal of molecular sciences · 2020Review
- Phosphatidylinositol 3,5-bisphosphate regulates CaTraffic (Copenhagen, Denmark) · 2020Article
- Article
Corrections and comments
- Erratum issuedCorrection.2019
Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glutathione depletion and calcium influx into the cytoplasm are two hallmarks of apoptosis. We have been investigating how glutathione depletion leads to apoptosis in yeast. We show here that glutathione depletion in yeast leads to the activation of two cytoplasmically inward-facing channels: the plasma membrane, Cch1p, and the vacuolar calcium channel, Yvc1p. Deletion of these channels partially rescues cells from glutathione depletion-induced cell death. Subsequent investigations on the Yvc1p channel, a homologue of the mammalian TRP channels, revealed that the channel is activated by glutathionylation. Yvc1p has nine cysteine residues, of which eight are located in the cytoplasmic regions and one on the transmembrane domain. We show that three of these cysteines, Cys-17, Cys-79, and Cys-191, are specifically glutathionylated. Mutation of these cysteines to alanine leads to a loss in glutathionylation and a concomitant loss in calcium channel activity. We further investigated the mechanism of glutathionylation and demonstrate a role for the yeast glutathione S-transferase Gtt1p in glutathionylation. Yvc1p is also deglutathionylated, and this was found to be mediated by the yeast thioredoxin, Trx2p. A model for redox activation and deactivation of the yeast Yvc1p channel is presented.
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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.