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Abstract
Lowering body temperature extends longevity in various organisms. This study investigates the mechanism behind cold-induced longevity and its effects on protein aggregation, a hallmark of neurodegenerative disorders. Researchers found that cold temperatures selectively induce the trypsin-like activity of the proteasome in *C. elegans* through PSME-3 (PA28γ ortholog). PSME-3 is crucial for cold-induced longevity and improves protein degradation. Cold-induced PSME-3 also reduces protein aggregation in *C. elegans* models of Huntington's and ALS. Similarly, moderate cold temperatures in human cells activate trypsin-like activity via PA28γ/PSME3, reducing aggregation and neurodegeneration. This research suggests a conserved beneficial role of cold temperature in proteasome regulation with implications for aging and age-related diseases.
Publisher
Nature Aging
Published On
May 01, 2023
Authors
Hyun Ju Lee, Hafiza Alirzayeva, Seda Koyuncu, Amirabbas Rueber, Alireza Noormohammadi, David Vilchez
Tags
longevity
cold temperatures
proteasome
protein aggregation
neurodegenerative disorders
C. elegans
aging
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