IndraLab

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USP15 deubiquitinates TGFBR. 8 / 8
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"USP15 binds to the SMAD7–SMAD E3 ligase complex and deubiquitinates and stabilizes the type I TGF-β receptor (TGFβR-I), leading to an enhanced TGF-β signal."

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"USP15 in this trimeric complex deubiquitinates and stabilizes type 1 TGF-beta receptor, upregulating the TGF-beta signaling and providing a critically pathogenic factor for glioblastoma."

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"For example, they are involved in the TGF-beta signaling pathway; USP15 deubiquitinates and stabilizes TGF-beta receptor I or receptor activated SMADs, while USP4 regulates the signaling pathway of TGF-beta receptor I and is associated with a poor prognosis in breast cancer."

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"USP15 binds to the SMAD7-SMAD specific E3 ubiquitin protein ligase 2 (SMURF2) complex and deubiquitinates and stabilizes type I TGF-beta receptor (TbetaR-I), leading to an enhanced TGF-beta signal."

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"USP15 can deubiquitinate type I TGF-β receptor (TβR-I) and enhance TGF-β activity; and over-expression of USP15 is closely related to TGF-β activation as well as a poor prognosis for glioblastoma patients."

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"USP15 binds to the SMURF2 complex and prevents ubiquitination of the TGF-β receptor resulting in elevated TGF-β signaling."

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"We hypothesized that USP15 deubiquitinated TGF-β receptor I to enhances TGF-β/Smad signaling, which in turn up-regulated USP15, leading to enhancement of the proliferation, migration, invasion, and collagen deposition of hypertrophic scar–derived fibroblasts in vitro."

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"It has been known that the TGF-β receptors can be deubiquitinated and stabilized by USP4, USP15 and USP11 [[18], [19], [20]]."