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AKT activates USP4. 6 / 6
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"Based on this study, it would be interesting to investigate whether USP4 function, which is also modulated by AKT as described above, is also affected in CYLD knockout mice XREF_BIBR."
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"According to a previous study by Iyengar [XREF_BIBR], Akt promotes USP4 to enter the cell membrane and cytoplasm to phosphorylate USP4 and regulate its subcellular localization, and Akt phosphorylation of USP4 occurs by combining with other de-ubiquitinating enzymes (DUBs) to de-ubiquitinate the TGF-beta receptor [XREF_BIBR]."
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"A recent study has demonstrated that AKT mediates the nuclear-to-cytoplasmic transport of USP4, leading USP4 to interact with and deubiquitinate TGF-β type I receptor (TβRI), which indicates USP4 as a[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Here, Akt phospho-activated the deubiquitylating enzyme USP4, resulting in reduced ubiquitylation-mediated degradation of TβR-I and thus enhanced Smad signaling ( Zhang et al., 2012 )."
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"These results suggest that the USP4 effect on myogenesis is possibly mediated by AKT and p38 signalings.We found that USP4 performs a function in myogenesis, but not as a deubiquitinase."
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"This study suggests that Akt activation in breast cancer cells induces USP4 to relocate and stabilize TbetaRI in the plasma membrane, and thereby enforces TGF-beta-induced pro tumorigenic responses."
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