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Distinct TORC1 signalling branches regulate Adc17 proteasome assembly chaperone expression.

Thomas D Williams1,2, Ifeoluwapo Joshua1, Flavie Soubigou1

  • 1MRC-PPU, University of Dundee, Dundee DD1 5EH, UK.

Journal of Cell Science
|July 1, 2024
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Summary
This summary is machine-generated.

Inhibition of TORC1 in yeast cells increases proteasome assembly by activating the cell wall integrity pathway and requires inhibiting S6 kinase Sch9. This enhances cellular adaptation to stress.

Keywords:
Actin cytoskeletonMpk1 kinaseProteasome assembly chaperoneSlt2 kinaseTORC1 signalling

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Cells require proteome adaptation for protein homeostasis under stress, necessitating increased proteasome assembly.
  • Proteasome assembly depends on the production of specific chaperones, regulated by complex signaling networks.

Purpose of the Study:

  • To investigate the signaling pathways regulating proteasome assembly chaperone production in Saccharomyces cerevisiae.
  • To elucidate the role of TORC1 inhibition and downstream effectors in cellular stress response and proteasome biogenesis.

Main Methods:

  • Inhibition of the target of rapamycin complex 1 (TORC1) kinase.
  • Analysis of mitogen-activated protein kinase (MAPK) Mpk1 activation and mRNA relocalization.
  • Investigation of cell wall integrity pathway activation via sensor proteins (Wsc1, Wsc3, Wsc4) and S6 kinase Sch9 inhibition.

Main Results:

  • TORC1 inhibition in yeast activates the cell wall integrity pathway, leading to increased proteasome assembly chaperone translation.
  • This process involves Mpk1 activation and mRNA relocalization to actin patches.
  • Co-inhibition of S6 kinase Sch9 is essential for driving protein expression, indicating a dual requirement beyond cell wall signaling.

Conclusions:

  • TORC1 inhibition triggers proteasome assembly upregulation through cell wall integrity signaling and requires concurrent Sch9 inhibition.
  • This study reveals a novel signaling mechanism coordinating cellular stress adaptation and proteasome biogenesis.
  • Findings expand understanding of the regulatory pathways governing proteasome assembly chaperone production.