To maintain protein homoeostasis, animals have developed stress response pathways such as the ubiquitin proteasome system (UPS). Joshi and colleagues have demonstrated that in Caenorhabditis elegans, dopamine release from neurons acts on receptors in the epithelia to modulate protein turnover, by controlling the expression of regulators of the xenobiotic stress response. Dopamine receptor mutants challenged with pathogenic bacteria were defective in protein turnover and were also more sensitive to infection thus highlighting a role for monoamine signalling in innate immunity and stress responses.
See also: KK Joshi et al
Protein homoeostasis, or proteostasis, is the process by which an organism regulates its cellular proteome. The proteome is in a constant state of flux due to perturbations from the environment, such as extremes of temperature, toxins and pathogen exposure. To maintain proteostasis when confronted with these environmental challenges, animals have evolved cellular stress response pathways to either guide proper folding, or to remove damaged or incorrectly folded proteins (Vilchez et al, 2014). The ubiquitin proteasome system (UPS), by which proteins are flagged for removal by the covalent addition of chains of ubiquitin (Ub) and degraded via the 26S proteasome, is critical in mediating these processes. This cellular stress response pathway is tightly regulated within individual cells (Labbadia & Morimoto, 2015), but it is unclear how multicellular organisms are able to coordinate such pathways over multiple tissues.
The recent work of Joshi et al (2016) reveals that in Caenorhabditis elegans, a neuronal signal modulates …
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