Thermosensation in Caenorhabditis elegans is linked to ubiquitin-dependent protein turnover via insulin and calcineurin signalling.
Alexandra SegrefKavya L VakkayilTsimafei PadvitskiQiaochu LiVirginia KroefJakob LormannLioba KörnerFabian FingerThorsten HoppePublished in: Nature communications (2022)
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.
Keyphrases
- transcription factor
- type diabetes
- heat stress
- protein protein
- binding protein
- quality control
- amino acid
- signaling pathway
- spinal cord
- multiple sclerosis
- cell proliferation
- liver failure
- white matter
- bone mineral density
- high intensity
- adipose tissue
- poor prognosis
- intensive care unit
- hepatitis b virus
- climate change
- bone marrow
- particulate matter
- machine learning
- artificial intelligence
- human health
- long non coding rna
- aortic dissection