A Structural View of Negative Regulation of the Toll-like Receptor-Mediated Inflammatory Pathway.
İstanbul, Turkey. In Biophys J, Oct 2015
Structural data suggest that 1) Toll/IL-1R (TIR) domain-containing regulators (BCAP, SIGIRR, and ST2) interfere with TIR domain signalosome formation; 2) major deubiquitinases such as A20, CYLD, and DUBA prevent association of TRAF6 and TRAF3 with their partners, in addition to removing K63-linked ubiquitin chains that serve as a docking platform for downstream effectors; 3) alternative downstream pathways of TLRs also restrict signaling by competing to bind common partners through shared binding sites.
DUBA-UBR5 axis: other than transactivation.
Boston, United States. In Cell Res, Mar 2015
A recent publication by Rutz et al. in Nature describes a novel deubiquitylating enzyme DUBA as a negative regulator for IL-17 by regulating stability of RORγt, the master transcription factor that induces Th17 cells.
Pattern-recognition receptor signaling regulator mRNA expression in humans and mice, and in transient inflammation or progressive fibrosis.
München, Germany. In Int J Mol Sci, 2012
We therefore determined the mRNA expression levels of A20, CYLD, DUBA, ST2, CD180, SIGIRR, TANK, SOCS1, SOCS3, SHIP, IRAK-M, DOK1, DOK2, SHP1, SHP2, TOLLIP, IRF4, SIKE, NLRX1, ERBIN, CENTB1, and Clec4a2 in human and mouse solid organs.
Phosphorylation meets proteolysis.
Basel, Switzerland. In Structure, 2012
Huang and colleagues and Velázquez-Delgado and Hardy (this issue of Structure) describe how phosphorylation activates the protease activity of the deubiquitinating enzyme DUBA and how it inhibits caspase-6, respectively.