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Chromatin regulates IL-33 release and extracellular cytokine activity
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Chromatin regulates IL-33 release and extracellular cytokine activity
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Journal Article
Chromatin regulates IL-33 release and extracellular cytokine activity
2018
Overview
IL-33 is an epithelium-derived, pro-inflammatory alarmin with enigmatic nuclear localization and chromatin binding. Here we report the functional properties of nuclear IL-33. Overexpression of IL-33 does not alter global gene expression in transduced epithelial cells. Fluorescence recovery after photobleaching data show that the intranuclear mobility of IL-33 is ~10-fold slower than IL-1α, whereas truncated IL-33 lacking chromatin-binding activity is more mobile. WT IL-33 is more resistant to necrosis-induced release than truncated IL-33 and has a relatively slow, linear release over time after membrane dissolution as compared to truncated IL-33 or IL-1α. Lastly, IL-33 and histones are released as a high-molecular weight complex and synergistically activate receptor-mediated signaling. We thus propose that chromatin binding is a post-translational mechanism that regulates the releasability and ST2-mediated bioactivity of IL-33 and provide a paradigm to further understand the enigmatic functions of nuclear cytokines.
Interleukin-33 (IL-33) can be released as a cytokine or transported into the nucleus, but the significance of this nuclear shuttling is not fully understood. Here the authors show that chromatin-binding of IL-33 alters, unexpectedly, the activity of IL-33 both in alarmin release kinetics and receptor signaling capacity.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 13/109
/ 13/21
/ 14/19
/ 14/35
/ 14/63
/ 38/91
/ 42/44
/ 82/16
/ 82/80
/ Binding
/ Extracellular Space - metabolism
/ Fluorescence recovery after photobleaching
/ Heterochromatin - metabolism
/ Histones
/ Humanities and Social Sciences
/ Humans
/ Interleukin-1 Receptor-Like 1 Protein
/ Kinetics
/ Necrosis
/ Science
