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Details on Person Necroptosis complements apoptosis as a host defense pathway ...
| Class:Id | Summation:9687462 |
|---|---|
| _displayName | Necroptosis complements apoptosis as a host defense pathway ... |
| _timestamp | 2020-07-17 23:03:04 |
| created | [InstanceEdit:9687477] Shamovsky, Veronica, 2020-05-09 |
| literatureReference | [LiteratureReference:9687450] Herpes simplex virus 1 ICP6 impedes TNF receptor 1-induced necrosome assembly during compartmentalization to detergent-resistant membrane vesicles [LiteratureReference:5364097] Identification of a novel homotypic interaction motif required for the phosphorylation of receptor-interacting protein (RIP) by RIP3 [LiteratureReference:9687472] Herpes Simplex Virus 1 (HSV-1) and HSV-2 Mediate Species-Specific Modulations of Programmed Necrosis through the Viral Ribonucleotide Reductase Large Subunit R1 [LiteratureReference:9687474] Herpes simplex virus suppresses necroptosis in human cells [LiteratureReference:9687481] Necroptosis: The Trojan horse in cell autonomous antiviral host defense [LiteratureReference:9687460] The ribonucleotide reductase R1 subunits of herpes simplex virus types 1 and 2 protect cells against TNFα- and FasL-induced apoptosis by interacting with caspase-8 |
| modified | [InstanceEdit:9696115] Shamovsky, Veronica, 2020-07-17 |
| text | Necroptosis complements apoptosis as a host defense pathway to stop virus infection. During infection in human cells, herpes simplex virus (HSV)-1 and HSV-2 modulate cell death pathways using the large subunit (R1) of viral ribonucleotide reductase (RIR1 or UL39) (Dufour F et al. 2011; Guo H et al. 2015; Yu X et al. 2016; Ali M et al.2019). The N-terminal region of RIR1 protein carrying the RIP homotypic interaction motif (RHIM)-like element is sufficient for RHIM-dependent interaction with receptor‐interacting protein kinase 1 (RIPK1) and receptor‐interacting protein kinase 3 (RIPK3) thus inhibiting the interaction between RIPK1 and RIPK3 (Guo H et al. 2015; Yu X et al. 2015). An intact RHIM is required for the interaction between RIPK1 and RIPK3 that occurs downstream of tumour necrosis factor receptor 1 (TNFR1) activation during the programmed cell death response known as necroptosis (Sun X et al. 2002). In addition, the large carboxyl-terminal region of HSV RIR1 protein mediates the binding to caspase 8 (CASP8) (Dufour F et al. 2011; Guo H et al. 2015). HSV RIR1 is thought to block necroptosis in infected human cells by interactions with RIPK1, RIPK3 and CASP8 (Guo H et al. 2015; Mocarski ES et al. 2015). |
| (summation) | [Reaction:9687465] HSV1 RIR1 binds RIPK1 [Homo sapiens] |
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