Abstract:
:As a canonical adaptor for the Toll-like receptor (TLR) family, myeloid differentiation primary response protein 88 (MyD88) has crucial roles in host defense against infection by microbial pathogens, and its dysregulation might induce autoimmune diseases. Here, we demonstrate that the chicken Cullin 3-based ubiquitin ligase adaptor Speckle-type BTB-POZ protein (chSPOP) recognizes the intermediate domain of chicken MyD88 (chMyD88) and degrades it through the proteasome pathway. Knockdown or genetic ablation of chSPOP leads to aberrant elevation of chMyD88 protein. Through this interaction, chSPOP negatively regulates NF-κB pathway activity and thus the production of IL-1β upon LPS challenge in chicken macrophages. Furthermore, Spop-deficient mice are more susceptible to infection with Salmonella typhimurium. Collectively, these findings demonstrate MyD88 as a bona fide substrate of SPOP and uncover a mechanism by which SPOP regulates MyD88 abundance and disease susceptibility.
journal_name
PLoS Pathogjournal_title
PLoS pathogensauthors
Li Q,Wang F,Wang Q,Zhang N,Zheng J,Zheng M,Liu R,Cui H,Wen J,Zhao Gdoi
10.1371/journal.ppat.1008188subject
Has Abstractpub_date
2020-05-04 00:00:00pages
e1008188issue
5eissn
1553-7366issn
1553-7374pii
PPATHOGENS-D-19-01994journal_volume
16pub_type
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