IndraLab

Statements

USP15 binds CARD9. 11 / 11
1 | 1 9
sparser
"More broadly, compounds that modulate the strength of CARD9-USP15 interactions may also represent an avenue for the specific regulation of this signaling pathway in fungal infections and inflammatory or autoimmune syndromes."
33093067
sparser
"Here, we identify the deubiquitinase USP15 as a novel regulator of CARD9, demonstrating that USP15 constitutively associates with CARD9 and removes TRIM62-deposited ubiquitin marks."
33093067
reach
"In this study, we identify the deubiquitinase USP15 as a novel regulator of CARD9, demonstrating that USP15 constitutively associates with CARD9 and removes TRIM62 deposited ubiquitin marks."
33093067
sparser
"This result supports that CARD9 interacts with USP15 and suggests that the N-terminus of CARD9 harbors the USP15 interaction domain."
33093067
biogrid
No evidence text available
25416956
sparser
"To validate the interaction between USP15 and CARD9, we overexpressed Flag-StrepII-tagged full length CARD9 as well as N-terminal and C-terminal fragments together with USP15 in HEK293T cells ( xref )."
33093067
sparser
"We next tested whether USP15 binds to CARD9 endogenously in primary murine BMDCs."
33093067
sparser
"We immunoprecipitated endogenous USP15 with endogenous CARD9, demonstrating that the USP15-CARD9 interaction occurs under physiological conditions."
33093067
sparser
"The negative regulation demonstrated in this study mediated by the USP15-CARD9 association could occur at multiple levels – deactivation of CARD9 after ubiquitination and modulation of CARD9-mediated signaling intensity, duration, or both – with the dynamic balance between TRIM62 and USP15 enzymatic activities likely critical in controlling the overall output of this pathway."
33093067
sparser
"Importantly, we observed that USP15 binds to CARD9 in BMDCs in the absence of stimulation and that this interaction is largely unaffected by Dectin-1 ligand binding, indicating that USP15 constitutively interacts with CARD9 and may act to prevent aberrant CARD9 signaling at steady state."
33093067
sparser
"In this study, we identify the deubiquitinase USP15 as a novel regulator of CARD9, demonstrating that USP15 constitutively associates with CARD9 and removes TRIM62-deposited ubiquitin marks."
33093067