Reactome: A Curated Pathway Database
THIS SITE IS USED FOR CURATION AND TESTING
IT IS NOT STABLE, IS LINKED TO AN INCOMPLETE DATA SET, AND IS NOT MONITORED FOR PERFORMANCE. WE STRONGLY RECOMMEND THE USE OF OUR PUBLIC SITE

Query author contributions in Reactome

Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.

If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.

Name Email address

Details on Person Several studies showed that viral RNA binding to SARS-CoV-2 ...

Class:IdSummation:9756251
_displayNameSeveral studies showed that viral RNA binding to SARS-CoV-2 ...
_timestamp2022-02-18 04:40:26
created[InstanceEdit:9756233] Shamovsky, Veronica, 2021-10-12
literatureReference[LiteratureReference:9756239] The SARS-CoV-2 nucleocapsid phosphoprotein forms mutually exclusive condensates with RNA and the membrane-associated M protein
[LiteratureReference:9756244] The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA
[LiteratureReference:9755760] RNA-induced liquid phase separation of SARS-CoV-2 nucleocapsid protein facilitates NF-κB hyper-activation and inflammation
[LiteratureReference:9755753] Targeting liquid-liquid phase separation of SARS-CoV-2 nucleocapsid protein promotes innate antiviral immunity by elevating MAVS activity
modified[InstanceEdit:9756266] Shamovsky, Veronica, 2021-10-12
[InstanceEdit:9766212] Shamovsky, Veronica, 2022-02-18
textSeveral studies showed that viral RNA binding to SARS-CoV-2 nucleocapsid (N) protein induces liquid-liquid phase separation (LLPS) (Wu Y et al. 2021; Wang S et al. 2021; Cubuk J et al. 2021; Lu S et al. 2021). Viral N protein:RNA LLPS recruits TGF-beta-activated kinase 1 (TAK1) and IκB kinase (IKK) complexes and enhances their interaction which in turn promotes NF-kappaB activation and expression of pro-inflammatory cytokines (Wu Y et al. 2021). The C-terminal domain (CTD) of viral N is essential for LLPS (Wu Y et al. 2021; Wang S et al. 2021) and induction of NF-kappaB signaling in mammalian cells (Wu Y et al. 2021). Deletion of CTD abolished SARS-CoV-2 N LLPS and the recruitment of TAK1/IKK complexes. Co-immunoprecipitation analysis revealed that SARS-CoV-2 N protein interacted with the components of the TAK1 complex and the IKK complex, including TAK1, TAB1, TAB2, IKBKA (CHUK), IKBKB, and NEMO (IKBKG) upon co-expression in human embryonic kidney 293T (HEK293T) cells (Wu Y et al. 2021). Endogenous IKK and TAK1 immunoprecipitated together with N in human lung cancer Calu3 cells infected with SARS-CoV-2. Immunofluorescence analysis further revealed the enhanced co-localization between N protein and IKBKB after SARS-CoV-2 infection in human hepatoma Huh7 cells. These data sugget that SARS-CoV-2 N:RNA LLPS serves as a platform to enhance the interaction between TAK1 and IKK complexes promoting NF-kappaB-dependent inflammatory responses (Wu Y et al. 2021).

(summation)[Reaction:9755757] SARS-CoV-2 N binds TAK1 [Homo sapiens]
[Change default viewing format]
No pathways have been reviewed or authored by Several studies showed that viral RNA binding to SARS-CoV-2 ... (9756251)
Follow Reactome