IndraLab

Statements

TRAF6 binds USP20. 9 / 9
4 | 5
sparser
"The serine/threonine kinase IRAK1 is a key mediator of TRAF6 activation downstream of TLR4 and the IL-1R. Therefore, IRAK1 could not only promote TRAF6 activation but also prevent TRAF6 inactivation (deubiquitination)—if, indeed, IRAK1 phosphorylates USP20 on Ser334 (and thereby reduces the association of USP20 with TRAF6)."
37311534
biogrid
No evidence text available
26839314
sparser
"Thus, it seems that preventing USP20 phosphorylation on Ser334 augments the association of USP20 with its intracellular substrate TRAF6, even though it has no effect on the association of USP20 with the idealized substrate Ub-VME ( xref , A and B )."
37311534
sparser
"Thus, IRAK1 not only transduces IL-1R signaling ( xref ) but also prevents its termination: phosphorylation of USP20 on Ser334 reduces USP20’s binding to TRAF6 and thereby diminishes (a) USP20-mediated deubiquitination/deactivation of TRAF6 and (b) consequent attenuation of downstream NFκB activation."
37311534
sparser
"Our findings reveal novel mechanisms regulating IL-1β-induced proinflammatory signaling: by phosphorylating USP20 Ser334, IRAK1 diminishes the association of USP20 with TRAF6 and thus augments NFκB activation, SMC inflammation, and neointimal hyperplasia."
37311534
biogrid
No evidence text available
26839314
biogrid
No evidence text available
21525354
sparser
"Together, these results suggest that IRAK1 inhibits USP20-mediated deubiquitination of TRAF6 by phosphorylating USP20 on Ser334 and reducing USP20:TRAF6 association."
37311534
biogrid
No evidence text available
21525354