ArticleNature communications2026
Aging-associated modulation of UFMylation impairs proteostasis in C. elegans.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The attachment of Post-Translational Modifications (PTMs) to proteins regulates their activities and stability. Here we utilized the nematode Caenorhabditis elegans to test whether UFMylation, a PTM which affects key biological functions, regulate aging and protein homeostasis (proteostasis). We find that lowering UFMylation extends lifespan and mitigates the toxicity of aggregation-prone proteins that underlie the development of neurodegenerative disorders in humans. Mass spectrometric analysis suggests that UFMylation of aging-regulating proteins, including of the nucleolar FIB-1-NOL-56 complex and the germline-resident proteins CAR-1 and CGH-1, governs proteostasis, probably across tissues. Functional analyses indicate that the proteostasis-regulating transcription factors DAF-16 and SKN-1 are crucial for the protective effects of reduced UFMylation. Counter-proteotoxic effect of reduced UFMylation are mediated by enhanced nascent protein quality control, reduced protein aggregation, and increased protein degradation by the ubiquitin-proteasome system. These insights highlight the important roles of PTMs in the regulation of proteostasis and point at research directions for the development of therapies for neurodegenerative disorders.
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