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Updated: Oct 10, 2025

Measurement of Protein Turnover Rates in Senescent and Non-Dividing Cultured Cells with Metabolic Labeling and Mass Spectrometry
Published on: April 6, 2022
p62 works as a hub modulation in the ageing process.
Xiaolan Fan1, Tiantian Huang2, Yingdong Tong2
1Institute of Animal Genetics and Breeding, Sichuan Agricultural University, Chengdu, Sichuan 611130, PR China; Farm Animal Genetic Resources Exploration and Innovation Key Laboratory of Sichuan Province, Sichuan Agricultural University, Chengdu, Sichuan, PR China.
p62 protein regulates cellular processes like autophagy and stress resistance, and new research shows its direct involvement in aging. This review details how p62 influences aging, offering insights for future studies.
Area of Science:
- Cellular Biology
- Molecular Biology
- Aging Research
Background:
- p62 (SQSTM1) is a key indicator of autophagic flux, essential for maintaining protein homeostasis.
- It functions as a stress-induced scaffold protein, crucial for resisting oxidative stress.
- p62 interacts with signaling pathways, autophagy, and the ubiquitin-proteasome system (UPS), impacting cell proliferation, apoptosis, and survival.
Purpose of the Study:
- To review and detail the mechanisms by which p62 regulates aging.
- To explore p62's role in various aging-related phenotypes.
- To provide novel insights into p62's function in the aging process.
Main Methods:
- Literature review of recent studies on p62 and aging.
- Analysis of p62's involvement in cellular stress responses.
- Examination of p62's interactions with key cellular pathways.
Main Results:
- p62 is implicated in multiple aging-related signs.
- Its regulatory functions extend to cellular survival and homeostasis.
- Evidence suggests a direct or indirect role of p62 in the aging process.
Conclusions:
- p62 plays a significant role in regulating aging.
- Understanding p62's function offers new avenues for aging research.
- Further investigation into p62 is warranted for its implications in age-related decline.
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