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Human SMURF1 Protein expressed in Wheat germ - ABIN1320726
Wang, Zhang, Weng, Qiao, Ma, Xiao, Yu, Pan, Sun et al.: Impaired phosphorylation and ubiquitination by p70 S6 kinase (p70S6K) and Smad ubiquitination regulatory factor 1 (Smurf1) promote tribbles homolog 2 (TRIB2) stability and carcinogenic property in ... in The Journal of biological chemistry 2013
that Smurf1 promotes Lhx9 ubiquitylation and is involved in testosterone production in Leydig cells directly
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.
Reciprocal regulation between betaTrCP and Smurf1 has been found to inhibit proliferative capacity of liver cancer cells.
Nedd8 binding to Smurf plays important roles in the regulation of cell migration and the BMP and TGFbeta signaling pathways.
Expression of Smurf1 was increased with WHO grade and was consistent with poor prognosis of gliomas.
Smurf1 interacts with and targets Securin, an inhibitor of sister-chromatid separation, for poly-ubiquitination and proteasomal degradation.
Smurf1 overexpression decreases USP25 protein turnover, and the E3 ligase enzymatic activity of Smurf1 is required for USP25 degradation.
SMURF1 can be potentially used as a clinical biomarker and target for novel treatment of human GC.
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.
High smurf1 expression is associated with neoplasms.
activation of AMPK upregulated Smad6 and Smurf1 and thereby enhanced their interactions, resulting in its proteosome-dependent degradation of ALK2.
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.
SMURF1 is increased in patients with pulmonary arterial hypertension
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)
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.
results reveal the regulatory circuit between RUNX2 and SMURF1 controls RUNX2 expression and regulates odntoblastic differentiation in hDPSCs.
EGF/Smurf1 inhibits Wnt/beta-catenin-induced osteogenic differentiation and that Smurf1 downregulates Wnt/b-catenin signaling by enhancing proteasomal degradation of beta-catenin.
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.
SND1 promoted expression of the E3 ubiquitin ligase Smurf1, leading to RhoA ubiquitination and degradation.
NF-kappaB bind to the -411 to -420 region of the SMURF1 promoter and plays an essential role in the expression of SMURF1.
Smurf1 is a new positive regulator for macrophage proliferation and apoptosis, but a negative regulator for macrophage migration.
Inhibition of osteoblastic Smurf1 promotes bone formation in mouse models of distinctive age-related osteoporosis
Smurf1 expression in osteoblast differentiation is regulated by CRTC2.
Six2 mediates the protective effects of GDNF on damaged DA neurons by regulating Smurf1 expression.
TGF-beta inhibited osteoblastic differentiation by inducing the MAPK-ERK pathway which upregulated the expression of ubiquitin ligase SMURF1 and resulted in reduced presence of osteogenic proteins.
demonstration that Smurf1 acts as a brake for integrin activation by controlling Kindlin-2 protein levels, a new mechanism that permits precise modulation of integrin-mediated cellular functions
miR-140-5p and SMURF1 are key regulators of disease pathology in pulmonary arterial hypertension
Smurf1 is required for selective autophagy of Mycobacterium tuberculosis and host defense against tuberculosis infection.
Smurf1 regulates glucose metabolism and inhibits osteoblast differentiation. Smurf1 function requires the presence of serine 148 (S148) in Smurf1.
Smurf1 mediates NGF signaling and ubiquitinates RhoA in growth cones, regulating the need for local translation and degradation.
Smurf-mediated endocytosis of Patched1 is required in sonic hedgehog signal reception
Inhibition of rhBMP-2-induced ALP activity by intracellular delivery of SMURF1 in murine calvarial preosteoblast cells.
Smurf1-mediated Lys29-linked nonproteolytic polyubiquitination of axin1 negatively regulates Wnt/beta-catenin signaling.
These results suggest that the JNK/AP-1 and ERK/Runx2 signaling pathways mediate TNF-alpha-dependent Smurf1 transcription.
Smurf1 is a negative feedback regulator for IFN-gamma signaling by targeting STAT1 for ubiquitination and proteasomal degradation.
studies uncover a cell-cycle-independent function of Cdh1, establishing Cdh1 as an upstream component that governs Smurf1 activity
ER stress induces Smurf1 degradation and WFS1 up-regulation
Smurf1 negatively regulates mesenchymal stem cell proliferation and differentiation by controlling JunB turnover through an ubiquitin-proteasome pathway.
Data demonstrate that Smurf1 and Smurf2 have overlapping and distinct functionalities during early frog embryogenesis; collectively, they regulate ectodermal and mesodermal induction and patterning to ensure normal development of Xenopus embryos.
In Xenopus embryos, the BMP pathway is a major physiological target of Smurf1. We propose that in normal development Smurf1 cooperates with secreted BMP antagonists to limit BMP signaling in dorsal ectoderm.
This gene encodes a ubiquitin ligase that is specific for receptor-regulated SMAD proteins in the bone morphogenetic protein (BMP) pathway. This protein plays a key roll in the regulation of cell motility, cell signalling, and cell polarity. Alternative splicing results in multiple transcript variants encoding different isoforms.
Smad ubiquitination regulatory factor 1
, E3 ubiquitin-protein ligase SMURF1
, SMAD specific E3 ubiquitin protein ligase 1
, e3 ubiquitin-protein ligase SMURF1-like
, E3 ubiquitin ligase SMURF1
, SMAD-specific E3 ubiquitin-protein ligase 1
, Smad-specific E3 ubiquitin ligase 1
, SMAD ubiquitination regulatory factor 1