FLP-17 links glial stress sensing to remote UPR activation
The neuropeptide FLP-17 activates the Unfolded Protein Response in distant C. elegans tissues through glial signaling, a cell-nonautonomous proteostasis mechanism linked to Jennifer Garrison's research on brain-organ communication.
The neuropeptide FLP-17 activates the Unfolded Protein Response (UPRER, a stress-response program of the endoplasmic reticulum) in tissues far from the signal source. In C. elegans (a nematode) experiments, glial UPRER activation induces transcriptomic changes, FLP-17 triggers the same response in other tissues, and XBP-1 and PERK contribute to maximal activation.
The UPRER is activated when the endoplasmic reticulum (an intracellular organelle) is under stress. The program adjusts protein-folding capacity, translation, and degradation. In these experiments, the response is coordinated at the organism level through neuropeptide signaling from glia.
Jennifer Garrison (Buck Institute for Research on Aging) studies communication between the brain and reproductive organs and the mechanisms of ovarian aging. One plausible interpretation is that organism-wide proteostasis coordination through a glial neuropeptide relates to her work on inter-organ communication. Whether this result directly concerns ovarian aging is not established from the available data, and the source publication has not been identified.
This edge connects a researcher whose focus is brain–reproductive organ signaling to a cell-nonautonomous stress-response pathway demonstrated to act at a distance via a neuropeptide signal from glia, offering a concrete mechanistic angle on how the nervous system may coordinate organism-wide proteostasis during aging.