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Abstract Conventional type I dendritic cells (cDC1s) undergo homeostatic maturation upon apoptotic cell engulfment, hallmarked by the activation of the transcription factor LXRβ, which mediates cholesterol efflux and dampens interferon-stimulated gene expression. Here, we identify the unfolded protein response sensor IRE1 as an essential regulator of this process. Loss of IRE1 impairs cDC1, but not cDC2, homeostatic maturation and survival.
Abstract Protein-protein interactions play an important biological role in every aspect of cellular homeostasis and functioning. Proximity labeling mass spectrometry-based proteomics overcomes challenges typically associated with other methods, and has quickly become the current state-of-the-art in the field. Nevertheless, tight control of proximity labeling enzymatic activity and expression levels is crucial to accurately identify protein interactors.
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