Abstract
Protein function is controlled by the cellular proteostasis network. Proteostasis is energetically costly and those costs must be balanced with the energy needs of other physiological functions. Hypertonic stress causes widespread protein damage in C. elegans. Suppression and management of protein damage is essential for optimal survival under hypertonic conditions. ASH chemosensory neurons allow C. elegans to detect and avoid strongly hypertonic environments. We demonstrate that mutations in osm-9 and osm-12 that disrupt ASH mediated hypertonic avoidance behavior or genetic ablation of ASH neurons are associated with enhanced survival during hypertonic stress. Improved survival is not due to altered systemic volume homeostasis or organic osmolyte accumulation. Instead, we find that osm-9(ok1677) mutant and osm-9(RNAi) worms exhibit reductions in hypertonicity induced protein damage in non-neuronal cells suggesting that enhanced proteostasis capacity may account for improved hypertonic stress resistance in worms with defects in osmotic avoidance behavior. RNA-seq analysis revealed that genes that play roles in managing protein damage are upregulated in osm-9(ok1677) worms. Our findings are consistent with a growing body of work demonstrating that intercellular communication between neuronal and non-neuronal cells plays a critical role in integrating cellular stress resistance with other organismal physiological demands and associated energy costs.
Highlights
Cellular life requires precise control of protein structure and function, which are determined by protein conformation, concentration, assembly and localization
We demonstrate that disruption of osmotic avoidance behavior via gene mutations or genetic ablation of ASH neurons is associated with enhanced survival in hypertonic environments
All other osm genes are required for the normal function or development of chemosensory neurons. osm-9 and osm-12 encode a TRPV cation channel [20] and a protein required for the biogenesis of sensory neuron cilia [38], respectively
Summary
Cellular life requires precise control of protein structure and function, which are determined by protein conformation, concentration, assembly and localization. The homeostatic mechanisms that maintain protein function are collectively termed proteostasis. The proteostasis network is evolutionarily conserved and comprises the tightly integrated and regulated activities of gene transcription, RNA metabolism and protein synthesis, folding, assembly, trafficking, disassembly, repair and degradation [1,2,3].
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