ASB17 Facilitates the Burst of LPS-Induced Inflammation Through Maintaining TRAF6 Stability.
Front Cell Infect Microbiol
; 12: 759077, 2022.
Article
de En
| MEDLINE
| ID: mdl-35174103
ABSTRACT
ASB17, a member of the ankyrin repeat and SOCS box-containing protein (ASB) family, has been supposed to act as an E3 ubiquitin ligase. Actually, little is known about its biological function. In this study, we found that ASB17 knocking-out impaired the expression of the pro-inflammatory cytokines CCL2 and IL-6 in bone marrow-derived dendritic cells (BMDCs) stimulated by lipopolysaccharide (LPS), indicating an inflammation-promoting role of this gene. We reveal that ASB17 promotes LPS-induced nuclear factor kappa B (NF-κB) signal activation through interacting with TNF receptor-associated factor 6 (TRAF6) which is a crucial adaptor protein downstream of toll-like receptors (TLR). ASB17 via its aa177-250 segment interacts with the Zn finger domain of TRAF6. The interaction of ASB17 stabilizes TRAF6 protein through inhibiting K48-linked TRAF6 polyubiquitination. Therefore, we suggest that ASB17 facilitates LPS-induced NF-κB activation by maintaining TRAF6 protein stability. The inflammation enhancer role of ASB17 is recognized here, which provides new understanding of the activation process of inflammation and immune response.
Mots clés
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Lipopolysaccharides
/
Protéines et peptides de signalisation intracellulaire
/
Facteur-6 associé aux récepteurs de TNF
Limites:
Animals
/
Humans
Langue:
En
Journal:
Front Cell Infect Microbiol
Année:
2022
Type de document:
Article
Pays d'affiliation:
Chine