UNIGE document Scientific Article
previous document  unige:103220  next document
add to browser collection
Title

Reciprocal Regulation of Target of Rapamycin Complex 1 and Potassium Accumulation

Authors
Primo, Cecilia
Ferri-Blázquez, Alba
Yenush, Lynne
Published in Journal of Biological Chemistry. 2017, vol. 292, no. 2, p. 563-574
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/metabolismIntracellular Signaling Peptides and Proteins/genetics/metabolismMechanistic Target of Rapamycin Complex 1Multiprotein Complexes/genetics/metabolismPotassium/metabolismProtein Kinases/geneticsProtein-Serine-Threonine Kinases/genetics/metabolismSaccharomyces cerevisiae/genetics/metabolismSaccharomyces cerevisiae Proteins/genetics/metabolismTOR Serine-Threonine Kinases/genetics/metabolism
Identifiers
PMID: 27895122
Full text
Structures
Research group Groupe Loewith
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. https://archive-ouverte.unige.ch/unige:103220

14 hits

2 downloads

Update

Deposited on : 2018-03-27

Export document
Format :
Citation style :