GarD-ing the pathogen-containing vacuole from destruction

Gilliland, Haleigh N.; Olive, Andrew J.

doi:10.1016/j.chom.2022.11.007

Cited by 1 publication

(2 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Therefore, the host was able to recognize the ubiquitin-labeled PVs and to initiate the host immune defense against Toxoplasma gondii infection ( Hernandez et al., 2022 ) ( Figure 2B ). RNF213 mediates IFN-γ–dependent M1- and K63-linked ubiquitination of the Toxoplasma PVs to control pathogen replication, which is likely a shared pattern of pathogenesis between distinct intracellular pathogens ( Gilliland and Olive, 2022 ). However, it is unclear whether RNF213 catalyzes M1- or K63-ubiquitin chain directly in vivo .…”

Section: Anti-parasitic Role Of Rnf213mentioning

confidence: 99%

“…In Chlamydia trachomatis infection, important clues have successfully identified GarD as the first example of pathogen evasion within this previously unknown IFN-γ–dependent cell-autonomous immune pathway ( Gilliland and Olive, 2022 ). In the absence of GarD, RNF213 could decorate inclusion bodies by linear ubiquitin.…”

Section: Conclusion and Future Prospectsmentioning

confidence: 99%

See 1 more Smart Citation

The emerging role of E3 ubiquitin ligase RNF213 as an antimicrobial host determinant

Zhang,

Yuan,

Jiang

et al. 2023

Front. Cell. Infect. Microbiol.

View full text Add to dashboard Cite

Ring finger protein 213 (RNF213) is a large E3 ubiquitin ligase with a molecular weight of 591 kDa that is associated with moyamoya disease, a rare cerebrovascular disease. It is located in the cytosol and perinuclear space. Missense mutations in this gene have been found to be more prevalent in patients with moyamoya disease compared with that in healthy individuals. Understanding the molecular function of RNF213 could provide insights into moyamoya disease. RNF213 contains a C3HC4-type RING finger domain with an E3 ubiquitin ligase domain and six AAA+ adenosine triphosphatase (ATPase) domains. It is the only known protein with both AAA+ ATPase and ubiquitin ligase activities. Recent studies have highlighted the role of RNF213 in fighting against microbial infections, including viruses, parasites, bacteria, and chlamydiae. This review aims to summarize the recent research progress on the mechanisms of RNF213 in pathogenic infections, which will aid researchers in understanding the antimicrobial role of RNF213.

show abstract

Section: Anti-parasitic Role Of Rnf213mentioning

confidence: 99%

Section: Conclusion and Future Prospectsmentioning

confidence: 99%