protein
| binds RIPK1 through its unique C-terminal segment to inhibit RIP- and TNF receptor-1-mediated NF-kappaB activation |
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ZBP1 recruits RIPK1 and RIPK3 through RIP homotypic interaction motifs to activate NF-kappaB |
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BIRC2, BIRC3 are direct E3 ubiquitin ligases for all four RIP proteins and that BIRC2 is capable of conjugating the RIPs with diverse types of ubiquitin chains, including linear chains |
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PGAM5 is a kinase substrate of RIPK1/RIPK3 |
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necroptosis depends on the kinases RIPK1 and RIPK3, which interact through their RHIM domains to form the necrosome |
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CASP8 control of death receptor and TLR necrotic death signaling depends on basal catalytic activity that suppresses the RIPK3 kinase pathway |
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pseudokinase MLKL functions as a substrate of RIPK3 to mediate downstream signaling |
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MLKL is a key RIPK3 downstream component of tumour necrosis factor (TNF)-induced necroptosis |
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RIPK1 blocks early postnatal lethality mediated by CASP8 and RIPK3 |
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XIAP controls RIPK3-dependent cell death and IL1B secretion in response to TNF, which might contribute to hyperinflammation in patients with XLP2 |
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RIPK1 intrinsically suppresses spontaneous RIPK3 activation in the cytosol by controlling RIPK3 oligomerization |
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RIPK1 regulates hematopoiesis and prevents inflammation by suppressing RIPK3 activation |
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RIPK3 is an unexpected positive regulator of CASP8 activity that promotes IL1B maturation in bone marrow-derived dendritic cells (BMDCs) |
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HSP90AA1 and CDC37 cochaperone complex-mediated protein folding is thus an important part of the RIPK3 activation process during necroptosis. |
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PGAM5 is a mitochondrial phosphatase that has been reported to function downstream of RIPK3 to promote necroptosis and IL1B secretion |
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RHIM motif of RIPK1 is critical for preventing ZBP1/RIPK3/MLKL-dependent necroptosis during development |
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RIPK3 interacts with MAVS to regulate type I IFN-mediated immunity to Influenza A virus infection |
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unexpected roles for RIPK1 and RIPK3 kinases in the production of IFNB1 during the host inflammatory responses to bacterial infection, suggesting that the axis in which these kinases operate may represent a target for bacterial virulence factors |
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USP22 controls necroptosis by regulating RIPK3 ubiquitination |