Thermosensation in Caenorhabditis elegans is linked to ubiquitin-dependent protein turnover via insulin and calcineurin signalling
Alexandra Segref (),
Kavya L. Vakkayil,
Tsimafei Padvitski,
Qiaochu Li,
Virginia Kroef,
Jakob Lormann,
Lioba Körner,
Fabian Finger and
Thorsten Hoppe ()
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Alexandra Segref: University of Cologne
Kavya L. Vakkayil: University of Cologne
Tsimafei Padvitski: University of Cologne
Qiaochu Li: University of Cologne
Virginia Kroef: University of Cologne
Jakob Lormann: University of Cologne
Lioba Körner: University of Cologne
Fabian Finger: University of Cologne
Thorsten Hoppe: University of Cologne
Nature Communications, 2022, vol. 13, issue 1, 1-17
Abstract:
Abstract Organismal physiology and survival are influenced by environmental conditions and linked to protein quality control. Proteome integrity is achieved by maintaining an intricate balance between protein folding and degradation. In Caenorhabditis elegans, acute heat stress determines cell non-autonomous regulation of chaperone levels. However, how the perception of environmental changes, including physiological temperature, affects protein degradation remains largely unexplored. Here, we show that loss-of-function of dyf-1 in Caenorhabditis elegans associated with dysfunctional sensory neurons leads to defects in both temperature perception and thermal adaptation of the ubiquitin/proteasome system centered on thermosensory AFD neurons. Impaired perception of moderate temperature changes worsens ubiquitin-dependent proteolysis in intestinal cells. Brain-gut communication regulating protein turnover is mediated by upregulation of the insulin-like peptide INS-5 and inhibition of the calcineurin-regulated forkhead-box transcription factor DAF-16/FOXO. Our data indicate that perception of ambient temperature and its neuronal integration is important for the control of proteome integrity in complex organisms.
Date: 2022
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-33467-7
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DOI: 10.1038/s41467-022-33467-7
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