Adaptive inter-tissue proteostasis networks in aging and neurodegeneration

The maintenance of proteostasis is essential for cellular function and organismal health. Its decline with age is a key contributor to neurodegenerative diseases, metabolic disorders, and other chronic conditions. Eukaryotic cells respond to proteotoxic stress through compartment-specific pathways, including the heat shock response (HSR), the unfolded protein response of the endoplasmic reticulum (UPRER), and the mitochondrial UPR (UPRmt). While these pathways have been extensively studied in cell-autonomous contexts, recent evidence reveals that neurons and glial cells can co-ordinate these responses across tissues through cell-non-autonomous mechanisms. Neuronal signals, including neuropeptides, biogenic amines, and possibly extracellular vesicles, can activate stress responses in distal cells, modulating lipid metabolism and impacting longevity. Emerging data also suggest a role for glial cells in systemic proteostasis regulation, though their mechanisms remain relatively uncharacterized. This review discusses both classical and emerging concepts of proteostasis stress-response pathways, their integration with neural signaling, and how their modulation influences aging and disease. Understanding how intercellular communication governs proteostasis could open new avenues for therapeutic interventions in age-related and neurodegenerative disorders.

Authors

Institutions

Publication Details

Journal
Bioscience Reports
Published
2026-01-01
DOI
https://doi.org/10.1042/bsr20254097
Primary Topic
Endoplasmic Reticulum Stress and Disease
Type
article
Field-Weighted Citation Impact
0.00
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Adaptive inter-tissue proteostasis networks in aging and neurodegeneration

Carlos A. Vergani-Junior, Evandro A. De‐Souza, Matheus Antonio V. de C. Ventura
Bioscience Reports
Endoplasmic Reticulum Stress and Disease
article

Adaptive inter-tissue proteostasis networks in aging and neurodegeneration

Carlos A. Vergani-Junior, Evandro A. De‐Souza, Matheus Antonio V. de C. Ventura
article en

Abstract

The maintenance of proteostasis is essential for cellular function and organismal health. Its decline with age is a key contributor to neurodegenerative diseases, metabolic disorders, and other chronic conditions. Eukaryotic cells respond to proteotoxic stress through compartment-specific pathways, including the heat shock response (HSR), the unfolded protein response of the endoplasmic reticulum (UPRER), and the mitochondrial UPR (UPRmt). While these pathways have been extensively studied in cell-autonomous contexts, recent evidence reveals that neurons and glial cells can co-ordinate these responses across tissues through cell-non-autonomous mechanisms. Neuronal signals, including neuropeptides, biogenic amines, and possibly extracellular vesicles, can activate stress responses in distal cells, modulating lipid metabolism and impacting longevity. Emerging data also suggest a role for glial cells in systemic proteostasis regulation, though their mechanisms remain relatively uncharacterized. This review discusses both classical and emerging concepts of proteostasis stress-response pathways, their integration with neural signaling, and how their modulation influences aging and disease. Understanding how intercellular communication governs proteostasis could open new avenues for therapeutic interventions in age-related and neurodegenerative disorders.

Bioscience ReportsVol. 46(1)
Universidade de São Paulo (BR)
Good health and well-being
Openalex Percentile: Top 93%
Endoplasmic Reticulum Stress and Disease
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.