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Reciprocal regulation of Target of Rapamycin Complex 1 and potassium accumulation

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Reciprocal regulation of Target of Rapamycin Complex 1 and potassium accumulation

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dc.contributor.author Primo Planta, Cecilia es_ES
dc.contributor.author Ferri-Blazquez, Alba es_ES
dc.contributor.author Loewith, Robbie es_ES
dc.contributor.author Yenush, Lynne es_ES
dc.date.accessioned 2018-09-25T07:07:54Z
dc.date.available 2018-09-25T07:07:54Z
dc.date.issued 2017 es_ES
dc.identifier.issn 0021-9258 es_ES
dc.identifier.uri http://hdl.handle.net/10251/108052
dc.description.abstract [EN] The proper maintenance of potassium homeostasis is crucial for cell viability. Among the major determinants of potassium uptake in the model organism Saccharomyces cerevisiae are the Trk1 high affinity potassium transporter and the functionally redundant Hal4 (Sat4) and Hal5 protein kinases. These kinases are required for the plasma membrane accumulation of not only Trk1, but also several nutrient permeases. Here, we show that overexpression of the Target of Rapamycin Complex 1 (TORC1) effector NPR1 improves hal4 hal5 growth defects by stabilizing nutrient permeases at the plasma membrane. We subsequently found that internal potassium levels and TORC1 activity are linked. Specifically, growth under limiting potassium alters the activities of Npr1 and another TORC1 effector kinase, Sch9; hal4 hal5 and trk1 trk2 mutants display hypersensitivity to rapamycin; and, reciprocally, TORC1 inhibition reduces potassium accumulation. Our results demonstrate that in addition to carbon and nitrogen, TORC1 also responds to and regulates potassium fluxes. es_ES
dc.description.sponsorship This work was supported by Spanish Ministry of Science and Innovation (Madrid, Spain) Grant BFU2011-30197-C03-03 (to L. Y.). The authors declare that they have no conflicts of interest with the contents of this article. Supported by a pre-doctoral fellowship from the Spanish Research Council (Consejo Superior de Investigaciones Cientificas). Supported by the Swiss National Science Foundation, the European Research Council, and the Canton of Geneva.
dc.language Inglés es_ES
dc.publisher American Society for Biochemistry and Molecular Biology es_ES
dc.relation MINECO/BFU2011-30197-C03-03 es_ES
dc.relation.ispartof Journal of Biological Chemistry es_ES
dc.rights Reserva de todos los derechos es_ES
dc.subject Target of Rapamycin es_ES
dc.subject Potassium ion transport es_ES
dc.subject Membrane trafficking, Endocytosis es_ES
dc.subject.classification BIOQUIMICA Y BIOLOGIA MOLECULAR es_ES
dc.title Reciprocal regulation of Target of Rapamycin Complex 1 and potassium accumulation es_ES
dc.type Artículo es_ES
dc.identifier.doi 10.1074/jbc.M116.746982 es_ES
dc.rights.accessRights Abierto es_ES
dc.contributor.affiliation Universitat Politècnica de València. Departamento de Biotecnología - Departament de Biotecnologia es_ES
dc.contributor.affiliation Universitat Politècnica de València. Instituto Universitario Mixto de Biología Molecular y Celular de Plantas - Institut Universitari Mixt de Biologia Molecular i Cel·lular de Plantes es_ES
dc.description.bibliographicCitation Primo Planta, C.; Ferri-Blazquez, A.; Loewith, R.; Yenush, L. (2017). Reciprocal regulation of Target of Rapamycin Complex 1 and potassium accumulation. Journal of Biological Chemistry. 292(2):563-574. doi:10.1074/jbc.M116.746982 es_ES
dc.description.accrualMethod S es_ES
dc.relation.publisherversion http://doi.org/10.1074/jbc.M116.746982 es_ES
dc.description.upvformatpinicio 563 es_ES
dc.description.upvformatpfin 574 es_ES
dc.type.version info:eu repo/semantics/publishedVersion es_ES
dc.description.volume 292 es_ES
dc.description.issue 2 es_ES
dc.identifier.pmid 27895122
dc.identifier.pmcid PMC5241732
dc.relation.pasarela 331155 es_ES
dc.contributor.funder Ministerio de Economía, Industria y Competitividad (MINECO) es_ES


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