Maintenance of cation homoeostasis is a key process for any living organism. Specific mutations in Glc7, the essential catalytic subunit of yeast protein phosphatase 1, result in salt and alkaline pH sensitivity, suggesting a role for this protein in cation homoeostasis. We screened a collection of Glc7 regulatory subunit mutants for altered tolerance to diverse cations (sodium, lithium and calcium) and alkaline pH. Among 18 candidates, only deletion of REF2 (RNA end formation 2) yielded increased sensitivity to these conditions, as well as to diverse organic toxic cations. The Ref2F374A mutation, which renders it unable to bind Glc7, did not rescue the salt-related phenotypes of the ref2 strain, suggesting that Ref2 function in cation homoeostasis is mediated by Glc7. The ref2 deletion mutant displays a marked decrease in lithium efflux, which can be explained by the inability of these cells to fully induce the Na+-ATPase ENA1 gene. The effect of lack of Ref2 is additive to that of blockage of the calcineurin pathway and might disrupt multiple mechanisms controlling ENA1 expression. ref2 cells display a striking defect in vacuolar morphogenesis, which probably accounts for the increased calcium levels observed under standard growth conditions and the strong calcium sensitivity of this mutant. Remarkably, the evidence collected indicates that the role of Ref2 in cation homoeostasis may be unrelated to its previously identified function in the formation of mRNA via the APT (for associated with Pta1) complex.
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Research Article|
February 24 2010
Ref2, a regulatory subunit of the yeast protein phosphatase 1, is a novel component of cation homoeostasis
Jofre Ferrer-Dalmau;
Jofre Ferrer-Dalmau
*Departament de Bioquímica i Biologia Molecular and Institut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona, Barcelona 08193, Spain
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Asier González;
Asier González
*Departament de Bioquímica i Biologia Molecular and Institut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona, Barcelona 08193, Spain
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Maria Platara;
Maria Platara
*Departament de Bioquímica i Biologia Molecular and Institut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona, Barcelona 08193, Spain
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Clara Navarrete;
Clara Navarrete
†Departamento de Microbiología, Universidad de Córdoba, Córdoba 14071, Spain
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José L. Martínez;
José L. Martínez
†Departamento de Microbiología, Universidad de Córdoba, Córdoba 14071, Spain
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Lina Barreto;
Lina Barreto
*Departament de Bioquímica i Biologia Molecular and Institut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona, Barcelona 08193, Spain
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José Ramos;
José Ramos
†Departamento de Microbiología, Universidad de Córdoba, Córdoba 14071, Spain
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Joaquín Ariño;
Joaquín Ariño
*Departament de Bioquímica i Biologia Molecular and Institut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona, Barcelona 08193, Spain
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Antonio Casamayor
Antonio Casamayor
1
*Departament de Bioquímica i Biologia Molecular and Institut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona, Barcelona 08193, Spain
1To whom correspondence should be addressed (email antonio.casamayor@uab.es).
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Publisher: Portland Press Ltd
Received:
December 16 2009
Accepted:
December 22 2009
Accepted Manuscript online:
December 22 2009
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2010 Biochemical Society
2010
Biochem J (2010) 426 (3): 355–364.
Article history
Received:
December 16 2009
Accepted:
December 22 2009
Accepted Manuscript online:
December 22 2009
Citation
Jofre Ferrer-Dalmau, Asier González, Maria Platara, Clara Navarrete, José L. Martínez, Lina Barreto, José Ramos, Joaquín Ariño, Antonio Casamayor; Ref2, a regulatory subunit of the yeast protein phosphatase 1, is a novel component of cation homoeostasis. Biochem J 15 March 2010; 426 (3): 355–364. doi: https://doi.org/10.1042/BJ20091909
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