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Results revealed that SMURF1 was upregulated in ovarian cancer (OC) cell lines of greater aggression than less aggressive cells. SMURF1 induced OC cell migration and invasion via activation of the Ras homolog family member A/Rhoassociated protein kinase signaling pathway. Higher levels of SMURF1 expression were associated with shorter overall survival in patients with OC.
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Reciprocal regulation between betaTrCP and Smurf1 has been found to inhibit proliferative capacity of liver cancer cells.
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Nedd8 binding to Smurf plays important roles in the regulation of cell migration and the BMP and TGFbeta signaling pathways.
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Expression of Smurf1 was increased with WHO grade and was consistent with poor prognosis of gliomas.
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Smurf1 interacts with and targets Securin, an inhibitor of sister-chromatid separation, for poly-ubiquitination and proteasomal degradation.
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Smurf1 overexpression decreases USP25 protein turnover, and the E3 ligase enzymatic activity of Smurf1 is required for USP25 degradation.
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SMURF1 can be potentially used as a clinical biomarker and target for novel treatment of human GC.
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Uev1A appears to be involved in the BMP signaling pathway in which it collaborates with a ubiquitin E3 ligase Smurf1 to promote Smad1 degradation in a Ubc13-independent manner.
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High smurf1 expression is associated with neoplasms.
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activation of AMPK upregulated Smad6 and Smurf1 and thereby enhanced their interactions, resulting in its proteosome-dependent degradation of ALK2.
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we propose that the PKA-Smurf1-PIPKIgamma pathway has an important role in pulmonary tumorigenesis and imposes substantial clinical impact on development of novel diagnostic markers and therapeutic targets for lung cancer treatment.
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SMURF1 is increased in patients with pulmonary arterial hypertension
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Data suggest that SMURF1 is required for S phase progression; SMURF1 promotes ubiquitination-dependent degradation of WEE1; these functions of SMURF1 appear to be linked and may be important in cell proliferation and tumorigenesis. (SMURF1 = SMAD specific E3 ubiquitin protein ligase 1; WEE1 = wee 1 homolog [S pombe] protein)
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Taken together, our study for the first time clarified that the E3 ligase Smurf1 regulates USP5 protein stability and USP5-mediated TNF-alpha production through the ubiquitin proteasome pathway.
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results reveal the regulatory circuit between RUNX2 and SMURF1 controls RUNX2 expression and regulates odntoblastic differentiation in hDPSCs.
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EGF/Smurf1 inhibits Wnt/beta-catenin-induced osteogenic differentiation and that Smurf1 downregulates Wnt/b-catenin signaling by enhancing proteasomal degradation of beta-catenin.
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a model that CD166 regulates MCAM through a signaling flow from activation of PI3K/AKT and c-Raf/MEK/ERK signaling to the inhibition of potential MCAM ubiquitin E3 ligases, betaTrCP and Smurf1.
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SND1 promoted expression of the E3 ubiquitin ligase Smurf1, leading to RhoA ubiquitination and degradation.
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NF-kappaB bind to the -411 to -420 region of the SMURF1 promoter and plays an essential role in the expression of SMURF1.
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Smurf1 determines cell apoptosis rates downstream of DNA damage-induced ATR/Chk1 signalling by promoting degradation of RhoB.