IndraLab

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USP4 binds TGFBR1. 8 / 13
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"Likewise USP4 as a deubiquitylating enzyme also interacts with TbetaRI at the plasma membrane and reverses its ubiquitination and thus regulates the TbetaRI levels [XREF_BIBR]."
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"USP4 directly interacts with and deubiquitinates TGF-beta type I receptor (TbetaRI), regulating TGF-beta signaling by controlling TbetaRI levels at the plasma membrane."
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"Co-immunoprecipitation assay showed that exogenous USP4 and TGFR-1 directly bound to each other ( xref )."
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"Deubiquitinating TbetaRI and stimulation of TGF-beta signaling pathway also associate USP4 with liver fibrosis and cirrhosis where it facilitates activation of hepatic stellate cell and EMT in hepatocytes."
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"Mechanistically, we revealed that USP4 interacted directly with and deubiquitinated TGF-beta receptor type I (TGFR-1) to activate the TGF-beta signaling pathway, and subsequently induced the Epithelial-Mesenchymal Transition (EMT) in HCC cells."
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"Taken together, our results elucidate that USP4 is highly expressed in HCC and promotes the tumor invasion and metastasis, the underlying mechanism is that USP4 directly interacts with and deubiquitinates TGFR-1 to increase TGF-beta signaling Induced EMT."
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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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"For instance, USP4 directly interacts with and deubiquitinates TGF-beta type I receptor (TbetaRI), thereby determining the levels of TGF-beta signaling."
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