IndraLab

Statements


USP4 is phosphorylated on S445. 5 / 8
| 5 3

sparser
"AKT-mediated phosphorylation of USP4 at the Ser 445 residue is essential to form a complex with other protein partners such as USP15 or TβRI [ 54 ]."

sparser
"Results have shown that AKT-mediated phosphorylation of USP4 at the Ser445 residue is essential for it to form a complex with itself or with other protein partners, such as USP15 or TβRI ( xref )."

sparser
"To examine whether the phosphorylation of USP4 at Ser445 affects the interaction between USP4 and Rheb, we generated a USP4 dephospho-mimetic mutant (USP4-S445A) and a phospho-mimetic mutant (USP4-S445D)."

sparser
"The study that identified USP4 as a DUB for ALK5 also demonstrated that phosphorylation of USP4 on S445 triggers homomeric and heteromeric complex formation with USP11, USP15 and USP19, suggesting that these DUBs could act as a complex xref ."

sparser
"Taken together, these findings indicate that EGF regulates Rheb deubiquitination by inducing USP4 phosphorylation at S445."