IndraLab

Statements


AKT phosphorylates USP4. 7 / 7
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rlimsp
"AKT phosphorylates USP4, leading to USP4 relocalization to the membrane, reinforcing the pro-tumorigenic functions of TGFβ [77]."

rlimsp
"Interestingly, USP4 was found also to associate with AKT and to be phosphorylated by AKT on it conserved Ser445 motif. This phosphorylation promotes USP4 localization in membrane and cytoplasm, where USP4 deubiquitylates TβRI."

rlimsp
"Furthermore, the cell type or context-dependent selectivity of one of these DUBs over the others (e.g. the AKT phosphorylation site in USP4 is not conserved in USP11 or USP15) is a possibility and needs to be investigated further."

rlimsp
"The AKT-mediated phosphorylation of USP4 also affects its stability and DUB activity."

rlimsp
"Interestingly, AKT directly interacts and phosphorylates USP4, which then translocates from the nucleus to the plasma membrane where it stabilizes TGFβ receptor I through direct interaction [22]."

rlimsp
"Furthermore, the phosphorylation of USP4 by Akt was also required for it to associate with other DUBs to deubiquitylate the TGF-β receptors."

rlimsp
"These results indicate that Akt phosphorylates USP4 and regulates it subcellular localization by promoting USP4 to the membrane and cytoplasm."