IndraLab

Statements


5 | 9 5

reach
"We next examined whether USP18 interacted with TAK1."

reach
"USP18 binds and deubiquitinates TAK1 to attenuate hepatic steatosis and insulin resistance in non-alcoholic liver disease (37)."

sparser
"However, NEMO deficiency did not lead to loss of interaction between USP18 and TAK1 ( xref ), suggesting that USP18 targets TAK1 complex and IKK complex by distinct mechanisms."

sparser
"In terms of mechanism, we screened some targets of USP18 in mouse primary HSCs and found that USP18 could directly bind to TAK1."

sparser
"Moreover, USP18 also binds to and deubiquitinates TAK1, thereby promoting hepatic inflammatory responses ( xref – xref )."

reach
"Interestingly, in transfection experiments, Usp18 bound to and deubiquitinated Tak1, thereby reducing its kinase activity and the associated downstream signaling."

No evidence text available

reach
"Mechanistically, USP18 interacts with the TAK1-TAB1 complex and deubiquitinates TAK1, thereby restricting TCR-mediated NF-κB and NFAT activation, and subsequent expression of IL-2."

No evidence text available

No evidence text available

reach
"However, NEMO deficiency did not lead to loss of interaction between USP18 and TAK1 (XREF_FIG), suggesting that USP18 targets TAK1 complex and IKK complex by distinct mechanisms."

reach
"USP4 and USP18 bind with TAK1 and de-ubiquitinate TAK1 to inhibit its activation [10, 12]."

No evidence text available

reach
"Moreover, USP18 also binds to and deubiquitinates TAK1, thereby promoting hepatic inflammatory responses (90–92)."

sparser
"The mechanism is that USP18 interacted with transforming growth factor-β-activated kinase 1 (TAK1) and induced its deubiquitination, thereby inhibiting TAK1-p38/c-Jun N-terminal kinase 1/2 (JNK1/2) signaling, inhibiting cardiac fibrosis xref ."

No evidence text available

reach
"In terms of mechanism, we screened some targets of USP18 in mouse primary HSCs and found that USP18 could directly bind to TAK1."

reach
"The results indicated that USP18 interacted with TAK1, TAB1, and TAB2 without stimulation and PMA and ion stimulation reduced but did not totally abolish their association, whereas USP18 interacted with CARMA1 weakly in unstimulated cells and PMA and ion stimulation first enhanced their interaction and then resulted in their disassociation (XREF_FIG)."

sparser
"Although USP18 mutants can still bind to ubiquitinated TAK1, it fails to cleave the polyubiquitin chains, resulting in a stable USP18-ubiquitinated-TAK1 complex."