Scientific article
OA Policy
English

Reciprocal Regulation of Target of Rapamycin Complex 1 and Potassium Accumulation

Published inJournal of Biological Chemistry, vol. 292, no. 2, p. 563-574
Publication date2017
Abstract

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.

Keywords
  • Cation Transport Proteins/genetics/metabolism
  • Intracellular Signaling Peptides and Proteins/genetics/metabolism
  • Mechanistic Target of Rapamycin Complex 1
  • Multiprotein Complexes/genetics/metabolism
  • Potassium/metabolism
  • Protein Kinases/genetics
  • Protein-Serine-Threonine Kinases/genetics/metabolism
  • Saccharomyces cerevisiae/genetics/metabolism
  • Saccharomyces cerevisiae Proteins/genetics/metabolism
  • TOR Serine-Threonine Kinases/genetics/metabolism
Research groups
Citation (ISO format)
PRIMO, Cecilia et al. Reciprocal Regulation of Target of Rapamycin Complex 1 and Potassium Accumulation. In: Journal of Biological Chemistry, 2017, vol. 292, n° 2, p. 563–574. doi: 10.1074/jbc.M116.746982
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Article (Published version)
accessLevelPublic
Identifiers
Additional URL for this publicationhttp://www.jbc.org/content/292/2/563
Journal ISSN0021-9258
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191downloads

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