Abstract:
:Interleukin (IL)-37 diminishes a variety of inflammatory responses through ligation to its receptor IL-1R8/Sigirr. Sigirr is a Toll like receptor/IL-1R family member. We have shown that Sigirr is not stable in response to IL-37 treatment. IL-37-induced Sigirr degradation is mediated by the ubiquitin-proteasome system, and the process is reversed by a deubiquitinase, USP13. However, the molecular mechanisms by which USP13 regulates Sigirr stability have not been revealed. In this study, we investigate the roles of glycogen synthesis kinase 3β (GSK3β) in Sigirr phosphorylation and stability. IL-37 stimulation induced Sigirr phosphorylation and degradation, as well as activation of GSK3β. Inhibition of GSK3β attenuated IL-37-induced Sigirr phosphorylation, while exogenous expressed GSK3β promoted Sigirr phosphorylation at threonine (T)372 residue. Sigirr association with GSK3β was detected. Amino acid residues 51-101 in GSK3β were identified as the Sigirr binding domain. These data indicate that GSK3β mediates IL-37-induced threonine phosphorylation of Sigirr. Further, we investigated the role of GSK3β-mediated phosphorylation of Sigirr in Sigirr degradation. Inhibition of GSK3β attenuated IL-37-induced Sigirr degradation, while T372 mutant of Sigirr was resistant to IL-37-mediated degradation. Furthermore, inhibition of Sigirr phosphorylation prevented Sigirr internalization and association with USP13, suggesting GSK3β promotes Sigirr degradation through disrupting Sigirr association with USP13.
journal_name
J Cell Physioljournal_title
Journal of cellular physiologyauthors
Li L,Wei J,Suber TL,Ye Q,Miao J,Li S,Taleb SJ,Tran KC,Tamaskar AS,Zhao J,Zhao Ydoi
10.1002/jcp.30253subject
Has Abstractpub_date
2021-01-05 00:00:00eissn
0021-9541issn
1097-4652pub_type
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