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WW domain containing E3 ubiquitin protein ligase 1

WWP1, WW domain-containing protein, AIP5
WW domain-containing proteins are found in all eukaryotes and play an important role in the regulation of a wide variety of cellular functions such as protein degradation, transcription, and RNA splicing. This gene encodes a protein which contains 4 tandem WW domains and a HECT (homologous to the E6-associated protein carboxyl terminus) domain. The encoded protein belongs to a family of NEDD4-like proteins, which are E3 ubiquitin-ligase molecules and regulate key trafficking decisions, including targeting of proteins to proteosomes or lysosomes. Alternative splicing of this gene generates at least 6 transcript variants; however, the full length nature of these transcripts has not been defined. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, CAN, Nedd4, V1a, Itch
Papers on WWP1
Overexpression of WWP1 promotes tumorigenesis and predicts unfavorable prognosis in patients with hepatocellular carcinoma.
Xia et al., Guangzhou, China. In Oncotarget, Jan 2016
WW domain-containing E3 ubiquitin protein ligase 1 (WWP1) has been speculated to play important roles in the development of several kinds of cancers.
Integrated analysis of gene expression and genomic aberration data in osteosarcoma (OS).
Wang et al., Chongqing, China. In Cancer Gene Ther, Nov 2015
Comparing genomic aberrations and DGEs, we found 41 SNP-associated DEGs and 124 CNV-associated DEGs, in which 7 DGEs were associated with both SNPs and CNVs, including WWP1, EXT1, LDHB, C8orf59, PLEKHA5, CCT3 and VWF.
Cardiomyocyte-specific overexpression of the ubiquitin ligase Wwp1 contributes to reduction in Connexin 43 and arrhythmogenesis.
Matesic et al., Columbia, United States. In J Mol Cell Cardiol, Nov 2015
We hypothesized that Wwp1, an ubiquitin ligase whose expression in known to increase in aging-related pathologies, may regulate Cx43 in vivo by targeting it for ubiquitylation and degradation and yield tissue-specific Cx43 loss of function phenotypes.
Ataxin-3 like (ATXN3L), a member of the Josephin family of deubiquitinating enzymes, promotes breast cancer proliferation by deubiquitinating Krüppel-like factor 5 (KLF5).
Chen et al., Kunming, China. In Oncotarget, Sep 2015
KLF5 protein degradation is increased by several E3 ubiquitin ligases, including WWP1 and SCFFbw7, through the ubiquitin-proteasome pathway.
Characterization of WWP1 protein expression in skeletal muscle of muscular dystrophy chickens.
Takeda et al., Kodaira, Japan. In J Biochem, Sep 2015
UNASSIGNED: A missense mutation in the gene encoding WWP1 was identified as the most promising candidate responsible for chicken muscular dystrophy (MD) by genetic linkage analysis.
Functional Characterization of a WWP1/Tiul1 Tumor-derived Mutant Reveals a Paradigm of Its Constitutive Activation in Human Cancer.
Prunier et al., Paris, France. In J Biol Chem, Sep 2015
In this study, we sought to investigate potential mechanisms that govern WWP1/Tiul1 (WWP1) ubiquitin ligase activity, focusing on its ability to trigger degradation of TGFβ type I receptor (TβRI) in conjunction with Smad7.
Expression and purification of human WWP2 HECT domain in Escherichia coli.
Jia et al., Beijing, China. In Protein Expr Purif, Jun 2015
WWP2 (WW domain-containing protein 2) is an E3 ubiquitin ligase belonging to the NEDD4-like protein family involved in various cell regulations, such as carcinogenesis, transcription control and cellular transport.
Genome-wide analysis of the WW domain-containing protein genes in silkworm and their expansion in eukaryotes.
Lu et al., Chongqing, China. In Mol Genet Genomics, Jun 2015
WW domains are protein modules that mediate protein-protein interactions through recognition of proline-rich peptide motifs and phosphorylated serine/threonine-proline sites.
Knockdown of WWP1 inhibits growth and invasion, but induces apoptosis of osteosarcoma cells.
Huang et al., Shanghai, China. In Int J Clin Exp Pathol, 2014
Recent studies have shown that WW domain containing E3 ubiquitin protein ligase 1 (WWP1) is frequently amplified in various cancers.
Suppressor of Deltex mediates Pez degradation and modulates Drosophila midgut homeostasis.
Zhang et al., Shanghai, China. In Nat Commun, 2014
Moreover, PTPN14, a Pez mammalian homolog, is degraded by overexpressed Su(dx) or Su(dx) homologue WWP1 in mammalian cells.
MiR-21 suppresses endothelial progenitor cell proliferation by activating the TGFβ signaling pathway via downregulation of WWP1.
He et al., Shanghai, China. In Int J Clin Exp Pathol, 2014
Next, we used a luciferase reporter assay to demonstrate that miR-21 downregulates the expression of WW domain-containing protein 1 (WWP1), a negative regulator of TGFβ signaling, by directly targeting the 3'-UTR of WWP1.
WWP1: a versatile ubiquitin E3 ligase in signaling and diseases.
Chen et al., Kunming, China. In Cell Mol Life Sci, 2012
WWP1 may function as the E3 ligase for several PY motif-containing proteins, such as Smad2, KLF5, p63, ErbB4/HER4, RUNX2, JunB, RNF11, SPG20, and Gag, as well as several non-PY motif containing proteins, such as TbetaR1, Smad4, KLF2, and EPS15. Review.
The ubiquitin E3 ligase WWP1 decreases CXCL12-mediated MDA231 breast cancer cell migration and bone metastasis.
Xing et al., Rochester, United States. In Bone, 2012
WWP1 negatively regulates cell migration to CXCL12 by limiting CXCR4 degradation to promote breast cancer metastasis to bone.
TAZ antagonizes the WWP1-mediated KLF5 degradation and promotes breast cell proliferation and tumorigenesis.
Chen et al., Kunming, China. In Carcinogenesis, 2012
TAZ promotes breast cell growth partially through protecting KLF5 from WWP1-mediated degradation and enhancing KLF5's activities.
Tumor necrosis factor inhibits mesenchymal stem cell differentiation into osteoblasts via the ubiquitin E3 ligase Wwp1.
Xing et al., Rochester, United States. In Stem Cells, 2011
Wwp1 promotes ubiquitination and degradation of JunB, an AP-1 transcription factor that positively regulates osteoblast differentiation.
Exclusion of WWP1 mutations in a cohort of dystroglycanopathy patients.
Muntoni et al., London, United Kingdom. In Muscle Nerve, 2011
WWP1 mutations are not a common cause of human dystroglycanopathy.
The Nedd4-like family of E3 ubiquitin ligases and cancer.
Matesic et al., Albany, United States. In Cancer Metastasis Rev, 2007
The assertion that Nedd4-like E3s play a role in cancer is supported by the overexpression of Smurf2 in esophageal squamous cell carcinoma, WWP1 in prostate and breast cancer, Nedd4 in prostate and bladder cancer, and Smurf1 in pancreatic cancer.
Control of postnatal bone mass by the zinc finger adapter protein Schnurri-3.
Wein et al., Boston, United States. In Ann N Y Acad Sci, 2007
The molecular mechanism was revealed to be the recruitment of WWP1, a Nedd4 family E3 ubiquitin ligase, by Shn3 to the major transcriptional regulator of the osteoblast, Runx2.
Regulation of adult bone mass by the zinc finger adapter protein Schnurri-3.
Glimcher et al., Boston, United States. In Science, 2006
Shn3 was found to control protein levels of Runx2, the principal transcriptional regulator of osteoblast differentiation, by promoting its degradation through recruitment of the E3 ubiquitin ligase WWP1 to Runx2.
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