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USP4 deubiquitinates TGFBR1. 12 / 13
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"This phosphorylation promotes USP4 localization in membrane and cytoplasm, where USP4 deubiquitylates TbetaRI."

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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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"USP4 is regulated by AKT phosphorylation and directly deubiquitylates TGF-beta type I receptor [XREF_BIBR]."

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"After phosphorylation by AKT, USP4 associates with and deubiquitinates ALK5, leading to upregulation of TGFβ signal [84]."

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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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"USP4 can also deubiquitinate TGF-beta type I receptor (TbetaRI) and sustain its plasma membrane expression in a SMAD7 independent fashion, leading to hyperactivation of the TGF-beta pathway."

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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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"USP4 is regulated by AKT phosphorylation and directly deubiquitylates TGF-beta type I receptor."

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"USP4 is regulated by AKT phos phorylation and directly deubiquitylates TGF-beta type I receptor."

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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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"MicroRNA 27b (miR-27b) was identified as an inhibitor of ubiquitin-specific peptidase 4 (USP4), deubiquitylating TGF-beta receptor 1 (TbetaRI), downstream from CB2."