Ref2, a regulatory subunit of the yeast protein phosphatase 1, is a novel component of cation homoeostasis

Ferrer-Dalmau, Jofre; González, Asier; Platara, Maria; Navarrete, Clara; Martínez, José Luis; Barreto, Lina; Ramos, José; Ariño, Joaquı́n; Casamayor, Antonio

doi:10.1042/bj20091909

Cited by 13 publications

(11 citation statements)

References 62 publications

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“…The ref2 mutation prevents growth in the presence of lithium, sodium, and calcium cations, as well as under alkaline conditions. These cells display a significant decrease in lithium efflux, which can be explained by the inability of these cells to fully induce the ENA1 gene (Ferrer‐Dalmau et al, ). The effects were not mediated by the calcineurin pathway, likely involved Glc7, and appeared to be unrelated to the known function of Ref2 as a component of the APT complex (Ferrer‐Dalmau et al, ).…”

Section: The Ena Efflux Systemmentioning

confidence: 99%

Monovalent cation transporters at the plasma membrane in yeasts

Ariño

Ramos

Sychrová

2018

Yeast

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Maintenance of proper intracellular concentrations of monovalent cations, mainly sodium and potassium, is a requirement for survival of any cell. In the budding yeast Saccharomyces cerevisiae, monovalent cation homeostasis is determined by the active extrusion of protons through the Pma1 H -ATPase (reviewed in another chapter of this issue), the influx and efflux of these cations through the plasma membrane transporters (reviewed in this chapter), and the sequestration of toxic cations into the vacuoles. Here, we will describe the structure, function, and regulation of the plasma membrane transporters Trk1, Trk2, Tok1, Nha1, and Ena1, which play a key role in maintaining physiological intracellular concentrations of Na , K , and H , both under normal growth conditions and in response to stress.

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Section: The Ena Efflux Systemmentioning

confidence: 99%

Monovalent cation transporters at the plasma membrane in yeasts

Ariño

Ramos

Sychrová

2018

Yeast

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“…The effect of lack of Ref2 was shown to be additive to that of blockage of the calcineurin pathway and might disrupt multiple mechanisms controlling ENA1 expression. Remarkably, this role seems to be unrelated to the previously identified function of Ref2 as a component of the APT complex (75).…”

Section: Regulation Of Ena1mentioning

confidence: 87%

“…Very recently, a role for Ref2 (a regulatory subunit of the Glc7 type 1 protein phosphatase) in cation homeostasis has been proposed (75). The ref2 deletion mutant displays a marked decrease in lithium efflux, which can be explained by 110 ARIÑ O ET AL.…”

Section: Regulation Of Ena1mentioning

confidence: 99%

Alkali Metal Cation Transport and Homeostasis in Yeasts

Ariño

Ramos

Sychrová

2010

Microbiol Mol Biol Rev

261

299

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SUMMARY The maintenance of appropriate intracellular concentrations of alkali metal cations, principally K+ and Na+, is of utmost importance for living cells, since they determine cell volume, intracellular pH, and potential across the plasma membrane, among other important cellular parameters. Yeasts have developed a number of strategies to adapt to large variations in the concentrations of these cations in the environment, basically by controlling transport processes. Plasma membrane high-affinity K+ transporters allow intracellular accumulation of this cation even when it is scarce in the environment. Exposure to high concentrations of Na+ can be tolerated due to the existence of an Na+, K+-ATPase and an Na+, K+/H+-antiporter, which contribute to the potassium balance as well. Cations can also be sequestered through various antiporters into intracellular organelles, such as the vacuole. Although some uncertainties still persist, the nature of the major structural components responsible for alkali metal cation fluxes across yeast membranes has been defined within the last 20 years. In contrast, the regulatory components and their interactions are, in many cases, still unclear. Conserved signaling pathways (e.g., calcineurin and HOG) are known to participate in the regulation of influx and efflux processes at the plasma membrane level, even though the molecular details are obscure. Similarly, very little is known about the regulation of organellar transport and homeostasis of alkali metal cations. The aim of this review is to provide a comprehensive and up-to-date vision of the mechanisms responsible for alkali metal cation transport and their regulation in the model yeast Saccharomyces cerevisiae and to establish, when possible, comparisons with other yeasts and higher plants.

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“…Vacuolar staining and visualization was carried out using the lipophilic styryl dye FM4-64 (Molecular Probes) as described in [39].…”

Section: Methodsmentioning

confidence: 99%

Ptc6 Is Required for Proper Rapamycin-Induced Down-Regulation of the Genes Coding for Ribosomal and rRNA Processing Proteins in S. cerevisiae

et al. 2013

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Ptc6 is one of the seven components (Ptc1-Ptc7) of the protein phosphatase 2C family in the yeast Saccharomyces cerevisiae. In contrast to other type 2C phosphatases, the cellular role of this isoform is poorly understood. We present here a comprehensive characterization of this gene product. Cells lacking Ptc6 are sensitive to zinc ions, and somewhat tolerant to cell-wall damaging agents and to Li+. Ptc6 mutants are sensitive to rapamycin, albeit to lesser extent than ptc1 cells. This phenotype is not rescued by overexpression of PTC1 and mutation of ptc6 does not reproduce the characteristic genetic interactions of the ptc1 mutation with components of the TOR pathway, thus suggesting different cellular roles for both isoforms. We show here that the rapamycin-sensitive phenotype of ptc6 cells is unrelated to the reported role of Pt6 in controlling pyruvate dehydrogenase activity. Lack of Ptc6 results in substantial attenuation of the transcriptional response to rapamycin, particularly in the subset of repressed genes encoding ribosomal proteins or involved in rRNA processing. In contrast, repressed genes involved in translation are Ptc6-independent. These effects cannot be attributed to the regulation of the Sch9 kinase, but they could involve modulation of the binding of the Ifh1 co-activator to specific gene promoters.

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Ref2, a regulatory subunit of the yeast protein phosphatase 1, is a novel component of cation homoeostasis

Cited by 13 publications

References 62 publications

Monovalent cation transporters at the plasma membrane in yeasts

Monovalent cation transporters at the plasma membrane in yeasts

Alkali Metal Cation Transport and Homeostasis in Yeasts

Ptc6 Is Required for Proper Rapamycin-Induced Down-Regulation of the Genes Coding for Ribosomal and rRNA Processing Proteins in S. cerevisiae

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