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Updated: Mar 3, 2026

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans
Published on: September 7, 2021
Proteostasis or Aging: Let the CHIPs Fall Where They May
Robyn Branicky1, Siegfried Hekimi1
1Department of Biology, McGill University, Montreal H3A 1B1, Canada.
Abstract:
The conserved E3 ubiquitin ligase CHIP/CHN-1 contributes to proteostasis by ubiquitylating HSP70 and HSP90-interacting proteins. In a recent issue of Cell,Tawo et al. (2017) show that CHIP/CHN-1 also directly ubiquitylates the insulin receptor INSR/DAF-2 to regulate its turnover. These findings suggest an unexpected interpretation of the effects of altered proteostasis on survival.
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