IndraLab

Statements

AKT binds USP4. 7 / 7
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"Conceivably, AKT directly interacts with USP4 for its phosphorylation and translocates nuclear USP4 to the membrane and thus maintains TbetaRI stability and possibly modulates TGF-beta induced EMT and MMT."
25885904
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"Interestingly, it was also found that Akt directly associates and phosphorylates USP4, and then induces the translocation of USP4 from the nucleus to the cytoplasm and plasmalemma for maintaining TbetaRI stability [XREF_BIBR]."
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"Interestingly, AKT directly interacts and phosphorylates USP4, which then translocates from the nucleus to the plasma membrane where it stabilizes TGFbeta receptor I through direct interaction [XREF_BIBR]."
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"They further showed that USP4 could interact with Akt at endogenous level, and phosphorylate USP4 in vitro and in vivo."
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"They further showed that USP4 could interact with Akt at endogenous level, and phosphorylate USP4 in vitro and in vivo."
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"As mentioned above, USP4 binds to and deubiquitinates the TGF-beta type I receptor and associates with AKT, leading to enhanced TGF-beta signalling and AKT induced breast cancer cell migration (Zhang [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Conceivably, AKT directly interacts with USP4 for its phosphorylation and translocates nuclear USP4 to the membrane and thus maintains TβRI stability and possibly modulates TGF-β induced EMT/MMT."
25885904