Ctenopharyngodon idella Tollip regulates MyD88-induced NF-κB activation
Developmental & Comparative Immunology, ISSN: 0145-305X, Vol: 123, Page: 104162
2021
- 8Citations
- 2Captures
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Metrics Details
- Citations8
- Citation Indexes8
- CrossRef3
- Captures2
- Readers2
Article Description
Toll-interacting protein (Tollip) and MyD88 are key components of the TLR/IL-1R signaling pathway in mammals. MyD88 is known as a universal adaptor protein involving in TLR/IL-1R-induced NF-κB activation. Tollip is a crucial negative regulator of TLR-mediated innate immune responses. Previous studies have demonstrated that teleost Tollip served as a negative regulator of MyD88-dependent TLR signaling pathway. However, the mechanism is still unclear. In particular, the effect of TBD, C2, and CUE domains of Tollip on MyD88-NF-κB signaling pathway remains to be elucidated. In this study, we found that the response of grass carp Tollip ( Ci Tollip) to LPS stimulation was faster and stronger than that of poly I:C treatment, and Ci Tollip diminished the expression of tnf-α induced by LPS. Further assays indicated that except for the truncated mutant of △CUE2 (1–173 aa), wild type Ci Tollip and other truncated mutants (△N-(52–276 aa), △C2-(173–276 aa) and △CUE1-(1–231 aa)) could associate with MyD88 and negatively regulate MyD88-induced NF-κB activation. It suggested that the C-terminal (173–276 aa), in particular the connection section between C2 and CUE domains (173–231 aa), played a pivotal role in suppressing MyD88-induced activation of NF-κB.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0145305X21001701; http://dx.doi.org/10.1016/j.dci.2021.104162; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85107533643&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/34090930; https://linkinghub.elsevier.com/retrieve/pii/S0145305X21001701; https://dx.doi.org/10.1016/j.dci.2021.104162
Elsevier BV
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