This Reactome event shows RHIM-dependent interaction of RIPK1 and RIPK3.
",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q12933-1",
"Q9UNE7-1",
"Q14790-1",
"P98170-1",
"Q13546-1",
"O15294-1",
"Q13490-1",
"Q13489-1",
"Q9Y572-1"
],
"evidence": [
{
"id": "R-HSA-5213462",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5213462"
}
]
},
{
"id": "R-HSA-5689630",
"name": "BAP1 binds BAP1-interacting complex",
"equation": "",
"summary": "BRCA1-associated protein 1 (BAP1) is a ubiquitin COOH-terminal hydrolase that was initially identified as a protein that binds the RING finger domain of the breast and ovarian tumor suppressor BRCA1. BAP1 is a tumour suppressor that is believed to mediate its effects through chromatin modulation, transcriptional regulation, and possibly via the ubiquitin-proteasome system and the DNA damage response pathway (Murali et al. 2013).
The C-terminal coiled coil motif of BAP1 directly interacts with the zinc fingers of the transcription factor Yin Yang 1 (YY1) (Yu et al. 2010), part of a multiprotein complex containing numerous transcription factors and cofactors including the transcriptional regulator Host cell factor 1 (HCFC1), which binds the N-terminal portion of BAP1 (Misaghi et al. 2009, Machida et al. 2009). HCFC1 is a chromatin-associated protein initially identified as part of a multiprotein complex comprising the viral coactivator VP16 and the POU domain transcription factor POU2F1. During herpes simplex virus infection, this complex is recruited to the enhancer/promoter of the immediate-early gene to activate viral gene expression (Kristie et al. 2010).
The C-terminal extension of UCHL5 mediates association with Adrm1/Rpn13 of the proteasomal 19S regulatory subunit and with NFRKB of the INO80 chromatin remodeling complex. The extreme C-terminal segment of BAP1 is 38% identical to the C-terminus of UCHL5 (UCH37) and is necessary for binding to YY1 (Yu et al. 2010).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O15294-1",
"Q92560-1"
],
"evidence": [
{
"id": "R-HSA-5689630",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689630"
}
]
},
{
"id": "R-HSA-9687828",
"name": "O-GlcNAcylation of RIPK3 (TLR4 signaling)",
"equation": "",
"summary": "Receptor-interacting serine/threonine-protein kinase 3 (RIPK3) plays an integral role in mediating a pro-inflammatory form of cell death, termed necroptosis. RIPK3-dependent signaling is tightly regulated by post-translational modifications, including proteolysis, phosphorylation and ubiquitylation. O-linked \u03b2-N-acetylglucosamine (O-GlcNAc) transferase (OGT), a key enzyme for protein O-GlcNAcylation, was found to limit RIPK3 kinase-mediated inflammation and necroptosis in lipopolysaccharide (LPS)-stimulated mouse bone marrow-derived macrophages (BMM) and human monocyte-like THP-1 cells (Li X et al. 2019). Genetic deletion of Ogt in myeloid cells markedly exacerbated cytokine storm and host mortality in experimental sepsis in mice (Li X et al. 2019). Further, impaired O-GlcNAc signaling in patients with liver cirrhosis and in mice with ethanol-induced liver injury exhibited a significant increase in the level of phosphorylated mixed lineage kinase domain-like (MLKL) (Zhang B et al. 2019). OGT utilizes uridine diphosphate (UDP)-GlcNAc to catalyze O-linked attachment of a single GlcNAc to serine or threonine residues in target proteins. Co-immunoprecipitation assay showed that RIPK3 directly interacts with OGT in human embryonic kidney 293T (HEK293T) cells that were transfected with the tagged RIPK3 and OGT proteins (Li X et al. 2019; Zhang B et al. 2019). Further, both RIPK3 O-GlcNAcylation and the association between RIPK3 and OGT increased upon LPS stimulation in mouse BMM cells, despite attenuated total protein O-GlcNAcylation, which suggests that OGT actively and specifically promotes RIPK3 O-GlcNAcylation in response to LPS. In addition, upon LPS challenge, Ogt-deficient BMMs produced significantly higher amounts of inflammatory mediators. Similarly, OGT-deficient human THP-1 cells increased cytokine production in response to TLR2 (Pam3Cys), TLR4 (LPS) or TLR9 (CpG) agonists, suggesting that OGT negatively regulates cytokine production both in mouse and human cells (Li X et al. 2019). Thiamet-G (TMG), that increased intracellular O-GlcNAc levels, effectively shortened the half-life of RIPK3 in human non-small cell lung carcinoma cell line derived from the lymph node (H1299) as compared with the vehicle control suggesting that O-GlcNAcylation of RIPK3 decreases its protein stability (Zhang B et al. 2019). Truncations of human RIPK3 in conjunction with mass spectrometry and subsequent site-directed mutagenesis pinpointed the site of O-GlcNAcylation as residue T467 within the RIP homotypic interaction motif (RHIM) domain of RIPK3 (Li X et al. 2019). Examination of a RIPK3 T467A mutant, which is resistant to O-GlcNAc modification, confirmed that this modification repressed LPS-induced RIPK3-mediated phosphorylation events, cytokine production, and necroptotic cell death in THP-1 and RIPK3-expressing HEK293T cells (Li X et al. 2019). It should be noted that T467 on human RIPK3 is only partially conserved among mammalian species, suggesting a possibility that additional functional O-GlcNAcylation site(s) could exist in other species (Li X et al. 2019). Further, the O-GlcNAcylation of RIPK3 diminished RIPK1:RIPK3 and RIPK3:RIPK3 RHIM interactions and downstream RIPK3 kinase activation in RIPK3-expressing HEK293T cells. These findings are supported by structural modeling showing that O-GlcNAc modification lies in close proximity to the conserved RHIM VQVG motif and likely perturbs RHIM-mediated protein interaction through steric hinderance. Collectively these data show that OGT targets residue T467 of RIPK3 for O-GlcNAcylation to prevent RIPK3 activation in human cells. These findings demonstrate an immuno-metabolic crosstalk linking the hexosamine biosynthesis pathway (HBP)-associated O-GlcNAc signaling and innate immune cell activation (Li X et al. 2019; Zhang B et al. 2019).
",
"cellular_location": "cytosol",
"input_participant_list": [
"R-HSA-450328"
],
"output_participant_list": [
"R-ALL-110096",
"R-HSA-9687819"
],
"enzyme_list": [
"O15294-1",
"Q9Y572-1"
],
"evidence": [
{
"id": "R-HSA-9687828",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9687828"
}
]
},
{
"id": "R-HSA-9828175",
"name": "Formation of the NSL complex",
"equation": "",
"summary": "WDR5 is a subunit of an evolutionarily conserved lysine acetyltransferase Non-Specific-Lethal (NSL) complex together with the following proteins: KAT8 (also known as MOF) as the catalytic subunit, KANSL1-3 (also known as NSL1-3), MCRS1, HCFC1 (also known as Host cell factor 1 or HCF1), and one of the paralogous proteins: PHF20 or PHF20-like 1 (PHF20L1) (Smith et al, 2005; Cai et al, 2010; Van et al 2022). The NSL complex is responsible for the acetylation of lysine K5, K8, K12, and K16 of histone H4 (Smith et al, 2005; Cai et al, 2010; Zhao et al, 2013; Radzisheuskaya et al., 2021). The NSL complex binds to the promoters of house-keeping genes and regulates their expression (Radzisheuskaya et al., 2021), therefore in some contexts, it is essential for the viability and proliferation of human cells (Klein et al, 2016; Radzisheuskaya et al., 2021).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q9H7Z6-1",
"O15294-1"
],
"evidence": [
{
"id": "R-HSA-9828175",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9828175"
}
]
}
],
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