Protein Phosphatase 2B of Saccharomyces Cerevisiae is Required for Tolerance to Manganese, in Blocking the Entry of ions into the Cells

Fărcăşanu, Ileana C.; Hirata, Dai; Tsuchiya, Eiko; Nishiyama, Fumitaka; Miyakawa, Tokichi

doi:10.1111/j.1432-1033.1995.712zz.x

Cited by 29 publications

(34 citation statements)

References 20 publications

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“…It is unlikely that ShMTP1 complements the functions defective in the cnb1 mutant, because wild-type CNB1 is a protein phosphatase and not a membrane-bound protein (Farcasanu et al, 1995). Therefore, it is more likely that ShMTP1 acts independently of CNB1 to confer Mn 2ϩ tolerance by some other mechanism.…”

Section: Expression Of Shmtp1 In Yeast Confers Mn 2 ؉ Tolerancementioning

confidence: 97%

“…The cnb1 mutant is defective in Ca homeostasis as a result of inactive calcineurin, and its sensitivity to Mn 2ϩ is thought to be the result of CNB1 also being involved in Mn 2ϩ homeostasis (Farcasanu et al, 1995). The increased sensitivity of pmr1 mutants to Mn 2ϩ has been attributed to the absence of the Ca 2ϩ /Mn 2ϩ -ATPase activity located at the Golgi complex, which normally acts to reduce cytosolic Mn 2ϩ concentrations, with subsequent export of Mn 2ϩ to the external medium by exocytosis (Lapinskas et al, 1995).…”

Section: Expression Of Shmtp1 In Yeast Confers Mn 2 ؉ Tolerancementioning

confidence: 99%

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Genes Encoding Proteins of the Cation Diffusion Facilitator Family That Confer Manganese Tolerance

et al. 2003

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The yeast Saccharomyces cerevisiae expressing a cDNA library prepared from Stylosanthes hamata was screened for enhanced Mn 2 ؉ tolerance. From this screen, we identified four related cDNAs that encode membrane-bound proteins of the cation diffusion facilitator (CDF) family. One of these cDNAs ( ShMTP1 ) was investigated in detail and found to confer Mn 2 ؉ tolerance to yeast by internal sequestration rather than by efflux of Mn 2 ؉ . Expression of ShMTP1 in a range of yeast mutants suggested that it functions as a proton:Mn 2 ؉ antiporter on the membrane of an internal organelle. Similarly, when expressed in Arabidopsis, ShMTP1 conferred Mn 2 ؉ tolerance through internal sequestration. The ShMTP1 protein fused to green fluorescent protein was localized to the tonoplast of Arabidopsis cells but appeared to localize to the endoplasmic reticulum of yeast. We suggest that the ShMTP1 proteins are members of the CDF family involved in conferring Mn 2 ؉ tolerance and that at least one of these proteins (ShMTP1) confers tolerance by sequestering Mn 2 ؉ into internal organelles.

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Section: Expression Of Shmtp1 In Yeast Confers Mn 2 ؉ Tolerancementioning

confidence: 97%

Section: Expression Of Shmtp1 In Yeast Confers Mn 2 ؉ Tolerancementioning

confidence: 99%

Genes Encoding Proteins of the Cation Diffusion Facilitator Family That Confer Manganese Tolerance

et al. 2003

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“…Calcineurin mutants deficient for either the catalytic subunits (CNA1/CNA2; Cyert et al 1991;Liu et al 1991b) or the regulatory subunit (CNB1; Kuno et al 1991;Cyert and Thorner 1992) are viable under standard growth conditions but are sensitive to high concentrations of ions such as Na + , Li + , Mn + , and OH − (Nakamura et al 1993;Mendoza et al 1994;Farcasanu et al 1995;Pozos et al 1996). They also lose viability during sustained treatment with mating pheromone (Moser et al 1996;Withee et al 1997).…”

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confidence: 99%

Calcineurin-dependent regulation of Crz1p nuclear export requires Msn5p and a conserved calcineurin docking site

Boustany¹,

Cyert²

2002

Genes Dev.

112

114

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Calcineurin, a conserved Ca 2+/calmodulin-regulated protein phosphatase, plays a crucial role in Ca 2+ signaling in a wide variety of cell types. In Saccharomyces cerevisiae, calcineurin positively regulates transcription in response to stress by dephosphorylating the transcription factor Crz1p/Tcn1p. Dephosphorylation promotes Crz1p nuclear localization in part by increasing the efficiency of its nuclear import. In this work, we show that calcineurin-dependent dephosphorylation of Crz1p also down-regulates its nuclear export. Using a genetic approach, we identify Msn5p as the exportin for Crz1p. In addition, we define the Crz1p nuclear export signal (NES) and show that it interacts with Msn5p in a phosphorylation-dependent manner. This indicates that calcineurin regulates Crz1p nuclear export by dephosphorylating and inactivating its NES. Finally, we define a motif in Crz1p, PIISIQ, similar to the PxIxIT docking site for calcineurin on the mammalian transcription factor NFAT, that mediates the in vivo interaction between calcineurin and Crz1p and is required for calcineurin-dependent regulation of Crz1p nuclear export and activity. Therefore, in yeast as in mammals, a docking site is required to target calcineurin to its substrate such that it can dephosphorylate it efficiently.

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“…Calcineurin, essential only under specific environmental conditions, is an important mediator of the Ca 2ϩ signal. Calcineurin is required for the recovery from the G 1 arrest induced by mating pheromones and for homeostasis of ions, including Na ϩ /Li ϩ , Mn 2ϩ , and OH Ϫ (13)(14)(15)(16). Calcineurin regulates the expression of ion transporter genes by a mechanism mediated by Crz1, a calcineurin-dependent transcription factor (17,18).…”

mentioning

confidence: 99%

Evidence for Antagonistic Regulation of Cell Growth by the Calcineurin and High Osmolarity Glycerol Pathways in Saccharomyces cerevisiae

Shitamukai

Hirata

Sonobe

et al. 2004

Journal of Biological Chemistry

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Because Ca 2؉ signaling of budding yeast, through the activation of calcineurin and the Mpk1/Slt2 mitogenactivated protein kinase cascade, performs redundant function(s) in the events essential for growth, the simultaneous deletion of both these pathways (⌬cnb1 ⌬mpk1) leads to lethality. A PTC4 cDNA that encodes a protein phosphatase belonging to the PP2C family was obtained as a high dosage suppressor of the lethality of ⌬cnb1 ⌬mpk1 strain. Overexpression of PTC4 led to a decrease in the high osmolarity-induced Hog1 phosphorylation, and HOG1 deletion remarkably suppressed the synthetic lethality, indicating an antagonistic role of the high osmolarity glycerol (HOG) pathway and the Ca 2؉ signaling pathway in growth regulation. The calcineurin-Crz1 pathway was required for the down-regulation of the HOG pathway. Analysis of the time course of actin polarization, bud formation, and the onset of mitosis in synchronous cell cultures demonstrated that calcineurin negatively regulates actin polarization at the bud site, whereas the HOG pathway positively regulates bud formation at a later step after actin has polarized.

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Protein Phosphatase 2B of Saccharomyces Cerevisiae is Required for Tolerance to Manganese, in Blocking the Entry of ions into the Cells

Cited by 29 publications

References 20 publications

Genes Encoding Proteins of the Cation Diffusion Facilitator Family That Confer Manganese Tolerance

Genes Encoding Proteins of the Cation Diffusion Facilitator Family That Confer Manganese Tolerance

Calcineurin-dependent regulation of Crz1p nuclear export requires Msn5p and a conserved calcineurin docking site

Evidence for Antagonistic Regulation of Cell Growth by the Calcineurin and High Osmolarity Glycerol Pathways in Saccharomyces cerevisiae

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