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Aging and diet alter the protein ubiquitylation landscape in the mouse brain
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Aging and diet alter the protein ubiquitylation landscape in the mouse brain
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Journal Article
Aging and diet alter the protein ubiquitylation landscape in the mouse brain
2025
Overview
Post-translational modifications (PTMs) regulate protein homeostasis, but how aging impacts PTMs remains unclear. Here, we used mass spectrometry to reveal changes in hundreds of protein ubiquitylation, acetylation, and phosphorylation sites in the mouse aging brain. We show that aging has a major impact on protein ubiquitylation. 29% of the quantified ubiquitylation sites were affected independently of protein abundance, indicating altered PTM stoichiometry. Using iPSC-derived neurons, we estimated that 35% of ubiquitylation changes observed in the aged brain can be attributed to reduced proteasome activity. Finally, we tested whether protein ubiquitylation in the brain can be influenced by dietary intervention. We found that one cycle of dietary restriction and re-feeding modifies the brain ubiquitylome, rescuing some but exacerbating other ubiquitylation changes observed in old brains. Our findings reveal an age-dependent ubiquitylation signature modifiable by dietary intervention, providing insights into mechanisms of protein homeostasis impairment and highlighting potential biomarkers of brain aging.
Post-translational modifications (PTMs) regulate protein homeostasis and function. Here, the authors applied mass spectrometry to uncover extensive changes in protein ubiquitylation in the aging mouse brain and show that dietary intervention can alter protein ubiquitylation in old mice.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
