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Significance The unfolded protein response of the endoplasmic reticulum (UPRER ) is induced by proteotoxic conditions. Lipid disequilibrium also activates the UPRER , but whether this activation is accompanied by disturbed proteostasis in vivo remains controversial. In this study, we show that in the nematodeCaenorhabditis elegans compromised fatty acid desaturation and reduced phosphatidylcholine production activate the UPRER without overt proteostatic imbalance, as assessed by molecular, pharmacological, and genetic analyses. This finding suggests that membrane composition is a direct input able to activate UPRER signaling even when proteostasis in the ER is largely intact. The activation of the UPRER by independent inputs may reflect the central role of the ER in both lipid and protein biosynthesis.

Activation of the endoplasmic reticulum unfolded protein response by lipid disequilibrium without disturbed proteostasis in vivo