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SMAD specific E3 ubiquitin protein ligase 1

Smurf1, E3 ubiquitin ligase Smurf1
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.[provided by RefSeq, Dec 2010] (from NCBI)
Top mentioned proteins: Ubiquitin, V1a, Smad1, RhoA, TGF-beta
Papers on Smurf1
Melatonin, bone regulation and the ubiquitin-proteasome connection: A review.
Reiter et al., Winnipeg, Canada. In Life Sci, Jan 2016
The ubiquitin ligases that are reported to be of major significance in regulating these pathways are the ubiquitin SCF(B-TrCP) ligase (which regulates activation of NF-κB via degradation of IkBα in osteoclasts, and regulates bone transcription factors via degradation of β-catenin), the Keap-Cul3-Rbx1 ligase (which regulates degradation of IkB kinase, Nrf2, and the antiapoptotic factor Bcl-2), and Smurf1.
Aberrant TGFβ Signalling Contributes to Altered Trophoblast Differentiation in Preeclampsia.
Caniggia et al., Toronto, Canada. In Endocrinology, Jan 2016
Additionally, we found that the TGFβ SMAD-independent signalling via PARD6/SMURF1 was activated around 10-12 weeks of gestation in cytotrophoblast and extravillous trophoblast (EVT) cells comprising the anchoring column.
IKKβ acts as a tumor suppressor in cancer-associated fibroblasts during intestinal tumorigenesis.
Greten et al., Frankfurt am Main, Germany. In J Exp Med, Jan 2016
In Ikkβ-deficient fibroblasts, transcription of negative regulators of TGFβ signaling, including Smad7 and Smurf1, is impaired, causing up-regulation of a TGFβ gene signature and elevated hepatocyte growth factor (HGF) secretion.
Genomic profiling of invasive melanoma cell lines by array comparative genomic hybridization.
Balázs et al., Debrecen, Hungary. In Melanoma Res, Jan 2016
Invasive primary cell lines showed high frequencies of CNAs, including the loss of 7q and gain of 12q chromosomal regions targeting PTPN12, ADAM22, FZD1, TFPI2, GNG11, COL1A2, SMURF1, VGF, RELN and GLIPR1 genes.
Pilot study of DNA methylation in the pathogenesis of chronic rhinosinusitis with nasal polyps.
Wang et al., In Rhinology, Dec 2015
The four top genes that changed, COL18A1, EP300, GNAS and SMURF1, were selected for further study.
E3 ubiquitin ligases as molecular targets in human oral cancers.
Kitagawa et al., Hamamatsu, Japan. In Curr Cancer Drug Targets, Dec 2015
Moreover, the HECT-type E3 ligase WWP family and Smurf1 are also involved in the development and growth of human oral cancers.
[Regulation of Smad ubiquitination regulatory factor 1 expression by NF-κB].
Chen et al., Shenyang, China. In Zhonghua Yi Xue Yi Chuan Xue Za Zhi, Aug 2015
OBJECTIVE: To identify a nuclear factor κB (NF-κB) responsive element within the Smad ubiquitination regulatory factor 1 (SMURF1) gene promoter, and to demonstrate its role in the regulation of SMURF1 expression.
A Smurf1 tale: function and regulation of an ubiquitin ligase in multiple cellular networks.
Zhang et al., Beijing, China. In Cell Mol Life Sci, 2013
Since being discovered and intensively studied for over a decade, Smad ubiquitylation regulatory factor-1 (Smurf1) has been linked with several important biological pathways, including the bone morphogenetic protein pathway, the non-canonical Wnt pathway, and the mitogen-activated protein kinase pathway.
Smurf E3 ubiquitin ligases at the cross roads of oncogenesis and tumor suppression.
Pillai et al., Thiruvananthapuram, India. In Biochim Biophys Acta, 2013
Smad ubiquitin regulatory factors (Smurfs) belong to the HECT- family of E3 ubiquitin ligases and comprise mainly of two members, Smurf1 and Smurf2.
Pharmaceutical perspectives of HECT-type ubiquitin ligase Smurf1.
Zhang et al., Beijing, China. In Curr Pharm Des, 2012
Smad ubiquitylation regulatory factor-1 (Smurf1) is a HECT-type ubiquitin ligase.
The E3 ligase Cdh1-anaphase promoting complex operates upstream of the E3 ligase Smurf1 in the control of axon growth.
Stegmüller et al., Göttingen, Germany. In Development, 2012
A Cdh1-APC/Smurf1/RhoA pathway that mediates axonal growth suppression in the developing mammalian brain.
Smurf1 protein negatively regulates interferon-γ signaling through promoting STAT1 protein ubiquitination and degradation.
Gao et al., Jinan, China. In J Biol Chem, 2012
Smurf1 is a negative feedback regulator for IFN-gamma signaling by targeting STAT1 for ubiquitination and proteasomal degradation.
Cdh1 regulates osteoblast function through an APC/C-independent modulation of Smurf1.
Wei et al., Boston, United States. In Mol Cell, 2012
studies uncover a cell-cycle-independent function of Cdh1, establishing Cdh1 as an upstream component that governs Smurf1 activity
Image-based genome-wide siRNA screen identifies selective autophagy factors.
Levine et al., Dallas, United States. In Nature, 2012
Murine embryonic fibroblasts lacking one of these gene products, the C2-domain containing protein, SMURF1, are deficient in the autophagosomal targeting of Sindbis and herpes simplex viruses and in the clearance of damaged mitochondria.
MiR-17 modulates osteogenic differentiation through a coherent feed-forward loop in mesenchymal stem cells isolated from periodontal ligaments of patients with periodontitis.
Jin et al., Xi'an, China. In Stem Cells, 2011
Inflammatory cytokines led to direct activation of Smurf1 and downregulation of miR-17, thereby increasing degradation of Smurf1-mediated osteoblast-specific factors.
SMURF1 amplification promotes invasiveness in pancreatic cancer.
Pollack et al., Stanford, United States. In Plos One, 2010
SMURF1 is an amplified oncogene driving multiple tumorigenic phenotypes in pancreatic cancer
Smurf1 zaps the talin head.
Critchley, In Nat Cell Biol, 2009
New results show that the talin head liberated from talin by calpain II cleavage has a key role in these events, and that its levels are tightly regulated by Smurf1-mediated ubiquitylation counteracted by Cdk5-mediated phosphorylation.
Talin phosphorylation by Cdk5 regulates Smurf1-mediated talin head ubiquitylation and cell migration.
Ginsberg et al., Chapel Hill, United States. In Nat Cell Biol, 2009
Here we show that talin head binds Smurf1, an E3 ubiquitin ligase involved in cell polarity and migration, more tightly than full-length talin does and that this interaction leads to talin head ubiquitylation and degradation.
Regulation of planar cell polarity by Smurf ubiquitin ligases.
Wrana et al., Toronto, Canada. In Cell, 2009
Mice mutant for Smurf1 and Smurf2 display planar cell polarity defects in the cochlea and convergence and extension movements defects that include a failure to close the neural tube.
Targeting WW domains linker of HECT-type ubiquitin ligase Smurf1 for activation by CKIP-1.
He et al., Beijing, China. In Nat Cell Biol, 2008
the WW domains linker is important in complex assembly and in regulating activity of HECT-type E3s and CKIP-1 functions as the first auxiliary factor to enhance the activation of Smurf1.
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