Stress granules at the crossroads of the proteostasis network.
- 1Center for RNA Biomedicine and Department of Biological Chemistry, University of Michigan, Ann Arbor, MI, USA.
- 2Department of Biological Chemistry, University of Michigan, Ann Arbor, MI, USA.
- 3Department of Human Genetics, University of Michigan, Ann Arbor, MI, USA.
Abstract
The proteostasis network maintains cell function by safeguarding the proteome through the coordinated actions of protein synthesis, quality control, and degradation machinery including chaperones and the ubiquitin-proteasome system. Proteostasis collapse and activation of the integrated stress response (ISR) occur in ageing and neurodegeneration. Upon proteotoxic stress, translation suppression during the ISR drives the assembly of non-translating mRNAs into biomolecular condensates called stress granules. Stress granules act as a double-edged sword in the proteostasis network, serving beneficial or detrimental roles through their effects on translation, protein quality control, and protein aggregation. In this review, we discuss how protein synthesis, quality control, and degradation factors regulate stress granule dynamics, and conversely how stress granules impact proteostasis. While stress granules may initially protect cells by sequestering misfolded, aggregation-prone proteins and regulating translation, they may evolve into sites of pathological aggregation. Clarifying these intersections may reveal therapeutic strategies for neurodegeneration and other disease processes.
Related
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- Loss of the UFM-1 pathway enhances the ER Unfolded Protein Response under stress to improve proteostasis and organismal health in Caenorhabditis elegans
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- Spatially Constrained Monte Carlo Permutation Test Reveals Diffusion Changes Near Stress Granules
BibTeX
@article{kim2026stress,
title = {{Stress granules at the crossroads of the proteostasis network.}},
author = {Rachel Kim and Erika N Calle Urgiles and Stephanie L Moon},
journal = {RNA biology},
year = {2026},
month = oct,
doi = {10.1080/15476286.2026.2731904},
url = {https://europepmc.org/article/MED/42861938},
note = {CC BY-NC},
}
RIS
TY - JOUR
TI - Stress granules at the crossroads of the proteostasis network.
AU - Rachel Kim
AU - Erika N Calle Urgiles
AU - Stephanie L Moon
PY - 2026
DA - 2026/10/12
JO - RNA biology
DO - 10.1080/15476286.2026.2731904
UR - https://europepmc.org/article/MED/42861938
AB - The proteostasis network maintains cell function by safeguarding the proteome through the coordinated actions of protein synthesis, quality control, and degradation machinery including chaperones and the ubiquitin-proteasome system. Proteostasis collapse and activation of the integrated stress response (ISR) occur in ageing and neurodegeneration. Upon proteotoxic stress, translation suppression during the ISR drives the assembly of non-translating mRNAs into biomolecular condensates called stress granules. Stress granules act as a double-edged sword in the proteostasis network, serving beneficial or detrimental roles through their effects on translation, protein quality control, and protein aggregation. In this review, we discuss how protein synthesis, quality control, and degradation factors regulate stress granule dynamics, and conversely how stress granules impact proteostasis. While stress granules may initially protect cells by sequestering misfolded, aggregation-prone proteins and regulating translation, they may evolve into sites of pathological aggregation. Clarifying these intersections may reveal therapeutic strategies for neurodegeneration and other disease processes.
SN - 1547-6286
SN - 1555-8584
ER -