IndraLab

Statements

USP4 is dephosphorylated. 2 / 2
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"Dephosphorylation of USP4 can cause its nuclear accumulation which enhances its interaction with squamous cell carcinoma antigen recognized by T cells 3 (SART3) and regulate spliceosome dynamics through deubiquitinating precursor RNA processing 3 [ xref ]."
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"For instance, dephosphorylated USP4 accumulates in the nucleus, whereas the AKT-mediated phosphorylated form of USP4 (at residue Ser445) was primarily localized in the cytoplasm and cell membrane."
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