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Non-muscle myosin heavy chain 9 maintains intestinal homeostasis by preventing epithelium necroptosis and colitis adenoma formation

ABSTRACT: Non-muscle myosin heavy chain 9 maintains intestinal homeostasis by preventing epithelium necroptosis and colitis adenoma formation

PROVIDER: PRJNA715738 | ENA |

REPOSITORIES: ENA

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Non-muscle myosin heavy chain 9 maintains intestinal homeostasis by preventing epithelium necroptosis and colitis adenoma formation

Project description:Non-muscle myosin IIA plays an important role in cell adhesion, cell migration and tissue architecture. We previously showed that low activity of the heavy chain of non-muscle myosin II Myh9 is beneficial to Lgr5+ intestinal stem cell maintenance. However, the function of Myh9 in adult mouse intestinal epithelium is largely unclear. In this study, we used the inducible Villin-creERT2 knockout approach to delete Myh9 in adult mouse intestinal epithelium and observed that homozygous deletion of Myh9 causes colitis-like morphologic changes in intestine, leads to a high sensitivity to dextran sulfate sodium and promotes the colitis related adenomas formation in colon. Myh9 deletion disturbs cell junctions and impairs intestinal lumen barrier integrity, promoting the necroptosis of epithelial cells. Consistently, these changes can be partially rescued by Ripk3 knockout. Our results indicate that Myh9 is required for the maintenance of intestinal epithelium integrity and the prevention of cell necroptosis.

2021-03-20 | GSE169225 | GEO

Non-muscle myosin heavy chain 9 maintains intestinal homeostasis by preventing epithelium necroptosis and colitis adenoma formation.

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Myosin Heavy Chain-embryonic is a crucial regulator of skeletal muscle development and differentiation.

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Necroptosis of intestinal epithelial cells induces innate lymphoid cell-dependent lethal ileitis in preterm mice

Project description:CFLARs encodes short form of cellular FLICE-inhibitory protein that blocks apoptosis, but promotes necroptosis in vitro. Here, we generate transgenic mice expressing CFLARs on the X-chromosome, designated as XCFY or XCFX mice. All XCFY mice die perinatally due to severe ileitis, whereas XCFX mice appear to be normal and fertile. Intestinal epithelial cell (IEC)s of XCFY mice die by necroptosis that subsequently induces massive apoptosis of IECs. Deletion of Ripk3 or Mlkl that are essential for necroptosis rescues embryonic lethality of XCFY mice by preventing both apoptosis and necroptosis of IECs. Surprisingly, deletion of RORγt+ ILC3s or Il22 rescues embryonic lethality of CFLARs Tg mice by preventing apoptosis, but not necroptosis of IECs. Thus, necroptosis of IECs triggered by cFLIPs activates RORγt+ ILC3s, resulting in induction of lethal ileitis in preterm mice.

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Quantitative analysis of phosphoproteome in necroptosis reveals a role of TRIM28 phosphorylation in promoting necroptosis-induced cytokine production

Project description:Necroptosis is a form of regulated necrotic cell death which promotes inflammation. In cells undergoing necroptosis, the activated RIPK1 kinase mediates the formation of RIPK1/RIPK3/MLKL complex to promote MLKL oligomerization and execution of necroptosis. RIPK1 kinase activity also promotes cell-autonomous activation of proinflammatory cytokine production in necroptosis. However, the signaling pathways downstream of RIPK1 kinase in necroptosis and how RIPK1 kinase activation controls inflammatory response induced by necroptosis are still largely unknown. Here we quantitatively measured the temporal dynamics of over 7000 confident phosphosites during necroptosis using mass spectrometry. Our study defined a RIPK1-dependent phosphorylation pattern in late necroptosis that is associated with a proinflammatory component marked by p-S473 TRIM28. We show that the activation of p38 MAPK mediated by oligomerized MLKL promotes the phosphorylation of S473 TRIM28, which in turn mediates inflammation during late necroptosis. Taken together, our study illustrates a mechanism by which p38 MAPK may be activated by oligomerized MLKL to promote inflammation in necroptosis.

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Quantitative proteomics characterization of proteins modified by very long chain fatty acids (VLCFAs) under necroptosis

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