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Hyperactive TORC 1 sensitizes yeast cells to endoplasmic reticulum stress by compromising cell wall integrity
Author(s) -
Ahmed Khadija,
Carter David E.,
Lajoie Patrick
Publication year - 2019
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13463
Subject(s) - unfolded protein response , endoplasmic reticulum , microbiology and biotechnology , saccharomyces cerevisiae , cell , chemistry , crosstalk , yeast , biology , biochemistry , physics , optics
Accumulation of misfolded proteins in the endoplasmic reticulum ( ER ) activates the unfolded protein response ( UPR ). Here, we investigated how the target of rapamycin complex 1 ( TORC 1) signaling cascade acts in parallel with the UPR to regulate ER stress sensitivity. Using Saccharomyces cerevisiae , we found that TORC 1 signaling is attenuated during ER stress and constitutive activation of TORC 1 increases sensitivity to ER stressors independently of the UPR . Transcriptome analysis revealed that TORC 1 hyperactivation results in cell wall remodelling. Conversely, hyperactive TORC 1 sensitizes cells to cell wall stressors, including the antifungal caspofungin. Elucidating the crosstalk between the UPR , cell wall integrity, and TORC 1 signaling may uncover new paradigms through which the response to protein misfolding is regulated.