IndraLab

Statements


| 4 7

sparser
"Rather, the ApaG domain of FBXO3 is indispensable for FBXO3 interaction with USP4."

sparser
"FBXO3 can bind to and stabilize USP4, leading to Twist1 protein stabilization and increased breast cancer cell migration and tumor metastasis."

sparser
"This study reveals a non-canonical function of the E3 ubiquitin ligase FBXO3 in PI3K-induced breast cancer metastasis, showing that FBXO3 binds to and protects USP4 from aspartyl aminopeptidase (DNPEP)-mediated degradation, resulting in Twist1 protein stabilization and increased tumor metastasis."

reach
"FBXO3 can bind to and stabilize USP4, leading to Twist1 protein stabilization and increased breast cancer cell migration and tumor metastasis."

sparser
"FBXO3 binds to USP4 and disrupts the interaction between USP4 and DNPEP, leading to stabilization of USP4 and Twist1."

reach
"FBXO3 binds to USP4 and disrupts the interaction between USP4 and DNPEP, leading to stabilization of USP4 and Twist1."

sparser
"Indeed, the co-immunoprecipitation assays showed that wild-type FBXO3 or FBXO3 ΔF , but not FBXO3 ΔApaG , could form stable complexes with USP4 ( xref )."

reach
"Together, these results indicate that FBXO3 binds USP4 to interfere with the interaction between USP4 and DNPEP, leading to stabilization of the USP4 protein."

reach
"Rather, the ApaG domain of FBXO3 is indispensable for FBXO3 interaction with USP4."

sparser
"Together, these results indicate that FBXO3 binds USP4 to interfere with the interaction between USP4 and DNPEP, leading to stabilization of the USP4 protein."

sparser
"Mechanistically, we found that the ApaG domain of FBXO3 binds to USP4 to prevent USP4 interaction with DNPEP thereby leading to USP4 protein stabilization."