IndraLab

Statements


7 | 4 3

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sparser
"Researchers found that OTUB1 directly binds to TRAF6 and removes K63-linked polyubiquitination modifications on TRAF6 through its deubiquitinating enzyme activity, an effect that inhibits TRAF6-mediated ubiquitination and activation of ASK1, which in turn down-regulates the expression of lipid metabolism-related genes (CD36, Fabp1, Scd1, PPARG and PPARα) and collagen-related genes (Col1a1, Col3a1, and α-SMA), which ultimately attenuated NASH ( xref )."

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reach
"OTUB1 and OTUB2 interact with and deubiquitinate TRAF3 and TRAF6, which are required for virus triggered IRF3 and NF-kappaB activation [XREF_BIBR]."

reach
"Coimmunoprecipitation analyses indicate that OTUB1 and OTUB2 associate with TRAF3 and TRAF6, negatively regulating antiviral responses by deubiquitinating their respective K63 linked polyubiquitin chains."

reach
"Coimmunoprecipitations indicated OTUB1 and -2 interacted with TRAF3 and TRAF6, two E3 ubiquitin ligases required for virus triggered IRF3 and NF-kappaB activation, respectively."

reach
"In contrast, we did not detect any interactions between OTUB1 and IRAK1, Pellino, or TRAF6 (Supplementary Fig. 3a)."

sparser
"OTUB1 directly binds to TRAF6, suppresses its K63-linked ubiquitination, and inhibits the activation of ASK1 and the JNK/p38 pathway under MASH conditions ( xref )."

sparser
"A20 was shown to directly interact with TRAF6 [48] and the OTU domain is involved in removing K63-linked polyubiquitin chains from TRAF6 [49] ."