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USP15 activates TGFB. 23 / 25
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"Besides ALK3 , USP15 also interacts with and deubiquitinates monoubiquitinated R-SMADs , causing enhanced TGF-beta and BMP responses in both mammalian cells and Xenopus embryos ."
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"These observations shed light on the function and mechanisms of USP15 mediated modulation of the TGF-beta signalling pathway during wound healing, thus providing a novel potential target for the treatment of refractory wounds."
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"Taken together, USP15 can enhance TGFbeta signaling by opposing both TGFbeta receptor polyubiquitination and R-SMAD monoubiquitination, which may contribute to tumor progression."
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"38, 39, 40, 41 For example, USP15 upregulates the TGF-beta pathway to promote cell proliferation in glioblastoma pathogenesis."
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"Although the mechanisms by which USP15 acts on TGFbeta and BMP signalling proposed in this study differ from those described above, the fundamental observations that USP15 enhances both TGFbeta and BMP signalling are consistent with studies described above XREF_BIBR."
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"By enhancing TGF-β signaling, USP15 promotes oncogenesis (27)."
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"In this study USP15 was found to potentiate both the TGF-beta pathway and the related BMP pathway by targeting mono-ubiquitinated R-SMADs for deubiquitination."
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"Our results indicated that USP15 stimulated TGF-beta and SMAD2 signaling and the cartilage phenotype."
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"It has been shown that knockdown of USP15 in immortalized HaCaT keratinocytes can impair TGF-beta and Smad-dependent growth arrest."
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"USP15 was reported to enhance TGFbeta signalling by binding to the SMAD7 and SMURF2 complex and deubiquitylating ALK5 in the process XREF_BIBR (XREF_FIG A)."
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"USP15 Enhances TGF-beta Signaling by Deubiquitinating the Type I TGFbeta Receptor ALK5 The TGF-beta signaling pathway is involved in diverse cellular processes in both the developing embryo and the adult organism ; these processes include cell growth and differentiation , immune response , apoptosis , cellular homeostasis , wound healing , and many other functions ."
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"USP15 is known to promote stabilization of the TGF-beta receptor and its downstream signal transducers, known as receptor activated SMADS (R-SMADS), thus empowering the TGF-beta signaling [XREF_BIBR, XREF_BIBR]."
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"USP15 stabilizes the TGF-beta receptor as well as its downstream signal transducers , the R-SMADs , and enhances TGF-beta activity ."
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"In addition, USP15 also promotes TGF-beta and BMP signaling by opposing monoubiquitylation of R-SMADs, thereby allowing activated R-SMAD-SMAD4 complexes to recognize target promoters [XREF_BIBR]."
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"By enhancing TGF-b signaling, USP15 promotes oncogenesis (27) ."
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"The DUBs USP4, USP11, USP15, and UCH37 have previously been demonstrated to modulate TGF-beta pathway activity by directly deubiquitinating the TbetaRI, resulting in increased TbetaRI stability (XREF_FIG) XREF_BIBR XREF_BIBR XREF_BIBR XREF_BIBR."
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"In this respect it is important to note that while functional linkage of USP4 to the TGF-beta and SMAD pathway was shown by employing a breast cancer model, USP15 can enhance the tumorigenic effect of TGF-beta in glioblastoma."
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"USP15 can deubiquitinate type I TGF-beta receptor ( TbetaR-I ) and enhance TGF-beta activity ; and over-expression of USP15 is closely related to TGF-beta activation as well as a poor prognosis for glioblastoma patients ."
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"Conversely, the deubiquitylating enzyme USP15 reverses this modification and restores responsiveness to TGF-beta."
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"Both USP15 and USP4 stimulate TGF-beta signaling by deubiquitylating and stabilizing two key signaling molecules in this pathway, TGF-beta receptor I (TbetaRI) and R-SMADs, suggesting that these two closely related DUBs act in concert to modulate central signaling processes that are involved in oncogenesis and innate immunity."
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"Moreover, Eichhorn et al. (2012) found that inhibition of USP15 decreased TGF-beta type I receptor and -phosphorylated Smad2 concentrations in these cells, thus corroborating the notion that USP15 sta[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"USP15 directly interacts with SMAD7 and other SMAD family members to deubiquitinate and stabilize type 1 TGF-beta receptors , promoting TGF-beta signaling ( 40 , 41 ) ."
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"In immortalized HaCaT keratinocytes , USP15 knockdown impairs TGF-beta / SMAD-dependent growth arrest but is required for TGF-beta-induced cell motility in metastatic MDA-MB-231 breast cancer cells [ 48 ] ."
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