IndraLab

Statements


USP15 binds TRIM25 and E6. 5 / 5
| 5

sparser
"Furthermore, HPV E6 protein forms a ternary complex with USP15 and TRIM25, resulting in the inhibition of immune surveillance and antiviral responses, thereby exhibiting a direct involvement in immune system regulation [ xref ]."

sparser
"As TRIM25 protein stability is regulated by the balance between degradative K48-linked ubiquitination and USP15-mediated deubiquitination, the authors performed coimmunoprecipitation experiments in HEK 293T and cervical-carcinoma-derived C33a cells ectopically expressing FLAG-tagged E6 of HPV16, showing that E6 binds exogenous TRIM25 and USP15, giving rise to a ternary E6-TRIM25-USP15 complex."

sparser
"In the RLR-mediated signaling pathway, E6 forms a three-molecule complex with TRIM25 and USP15, which triggers the K48-linked ubiquitination and proteasomal degradation of TRIM25, attenuates the TRIM25-mediated K63-linked ubiquitination of RIG-I."

sparser
"Interestingly, it has been shown that HPV16 E6, but not E7, forms a complex with TRIM25 and its regulator ubiquitin carboxyl-terminal hydrolase 15 (USP15), inducing TRIM25 degradation [ xref ]."

sparser
"HPV E6 binds to both TRIM25 and USP15 when ectopically expressed or in natively HPV-infected cells."