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Human CPEB1 Protein expressed in Wheat germ - ABIN1350186
Kochanek, Wells: CPEB1 regulates the expression of MTDH/AEG-1 and glioblastoma cell migration. in Molecular cancer research : MCR 2013
c-mos mRNA localizes with Zorba around the animal pole in the zebrafish oocyte suggesting that the animal cortex is the central core of oocyte maturation in zebrafish.
These findings indicated that the overexpression of miR4543p inhibited cell proliferation, migration and invasion by downregulating CPEB1.
Upon binding to p27(Kip1) 3'UTR, CPEB1 promotes elongation of poly-A tail and the subsequent translation of p27(Kip1) mRNA. This leads to higher levels of p27(Kip1) in the cell, in turn significantly inhibiting cell proliferation, and confers to CPEB1 a potential value as a tumor suppressor in Glioblastoma.
CPEB1 regulation of MMP9 mRNA expression mediates metastasis of breast cancer cells
The host RNA-binding protein CPEB1 was highly induced after cytomegalovirus infection and ectopic expression of CPEB1 in non-infected cells recapitulated infection-related post-transcriptional changes. CPEB1 was also required for poly(A)-tail lengthening of viral RNAs important for productive infection.
Expression levels of CPEB4 and CPEB1 genes are correlated with overall survival in patients with glioma.
WEE1 is regulated at the translational level by CPEB1 and miR-15b in a coordinated and cell-cycle-dependent manner.
This mechanical catalysis makes possible a positive feedback loop that would help localize the formation of CPEB fibers to active synapse areas and mark those synapses for forming a long-term memory after the prion form is established. The functional role of the CPEB helical oligomers in this mechanism carries with it implications for targeting such species in neurodegenerative diseases.
Structural Analysis of the Pin1-CPEB1 interaction and its potential role in CPEB1 degradation has been described.
Identify a mechanism of VEGF overexpression in liver and mesentery that promotes pathologic, but not physiologic, angiogenesis, via sequential and nonredundant functions of CPEB1 and CPEB4.
CPEB1, 2, and 4, are essential to successful mitotic cell division.
Results suggest that CPEB1-mediated translational control is essential for the differentiation of GSCs.
CPEB accelerates deadenylation and decay of the c-myc mRNA by recruiting the Tob-Caf1 complex.
Downregulation of CPEB1 induces senescence of glioma cells in a p53-dependent manner.
FMRP and CPEB1, an activator of translation, are present in neuronal dendrites, are predicted to bind many of the same mRNAs and may mediate a translational homeostasis that, when imbalanced, results in fragile X syndrome.
The structural similarity to other ZZ domains suggests that the CPEB1-ZZ domain recruits sumoylated proteins during assembly of the ribonucleoprotein complex prior to mRNA export from the nucleus.
results reveal a novel function of CPEB1 in mediating alternative 3'-UTR processing, which is coordinated with regulation of mRNA translation, through its dual nuclear and cytoplasmic functions
poly(A) polymerase Gld2, deadenylase PARN, and translation inhibitory factor neuroguidin (Ngd) are components of a dendritic CPEB-associated polyadenylation apparatus
The first evidence of CPEB1 involvement in GC is presented, along with the molecular mechanism underlying the regulation of its expression and its potential role in invasion and angiogenesis.
CPEB-mediated zonal occludens-1 mRNA localization is essential for tight-junction assembly and mammary epithelial cell polarity
depleted of CPEB demonstrated that this protein directly regulates the translation of PTEN and Stat3 mRNAs. Our results show that CPEB regulated translation is a key process involved in insulin signaling
CPEB1 level was increased in the basolateral amygdala (BLA) of model mice injected with Complete Freund's Adjuvant. CPEB1 knockdown in the BLA can relieve anxiety-like behaviors but not pain-like behaviors by heightening inhibitory transmission and restoring the excitatory/inhibitory balance in model mice.
DAZL and CPEB1 regulate mRNA translation during oocyte maturation.
cytoplasmic-element-binding control of transforming growth factor beta-activated kinase 1 mRNA translation mediates the inflammatory immune response
Myoepithelial cells prevent EMT by influencing the polarity and proliferation of luminal epithelial cells in a mechanism that requires translational silencing of myoepithelial Twist1 by CPEB1.
Fmr1(-/y); Cpeb1(-/-) double-knockout mice displayed amelioration of biochemical, morphological, electrophysiological and behavioral phenotypes associated with fragile X syndrome.
when the Cpeb1 knockout mice were fed a high-fat diet, their livers became insulin-resistant.Our results show that Cpeb1 regulated translation is a key process involved in insulin signaling
CPEB deficiency not only increases IL-6 production but also renders the cell incapable of a senescence-promoting response.
Data suggest that KHDC1B, via its interaction with mCEPB1, may regulate translation of mRNA targets required for oocyte maturation.
CPEB undergoes Thr 171 phosphorylation at E16.5, but dephosphorylation at the E18.5, when most oocytes are entering diplotene
Data suggest that CPEB-1 contributes in the translational control of mRNAs that is critical only for some selected forms of long-term potentiation and long-term depression.
These results demonstrate that CPEB phosphorylation and translation are regulated by CaMKII activity and provide a possible mechanism for how dendritic protein synthesis in the hippocampus may be stimulated during synaptic plasticity
CPEB binds the small intracellular domain (ICD) of APLP1.
a new eukaryotic initiation factor 4E (eIF4E) binding protein, Neuroguidin (Ngd), and its interaction with CPEB is described.
CPEB knockout mouse is sterile but overtly normal, but embryo fibroblasts derived from this mouse (MEF) do not enter senescence in culture as do wild-type MEFs, but instead are immortal.
CPEB controls the expression of Gdf9 mRNA, which in turn is necessary for oocyte-follicle development.
CPEB-1 control of c-Jun mRNA translation regulates GH gene expression and resulting downstream signaling events (e.g., synaptic plasticity) in the mouse hippocampus.
CPEB, localized in oocyte cytoplasm, was hyperphosphorylated during prophase/metaphase-I transition.
Aurora kinase A is unlikely to be involved in CPEB1 activating phosphorylation and cyclin B1 mRNA polyadenylation during meiotic maturation of porcine oocytes.
results suggest the involvement of mammalian CPEB1 in Cyclin B syntheses and meiotic resumption in mammalian oocytes
This gene encodes a member of the cytoplasmic polyadenylation element (CPE) binding protein family. This highly conserved protein binds to a specific RNA sequence called the CPE found in the 3' UTR of some mRNAs. Similar proteins in Xenopus and mouse function to induce cytoplasmic polyadenylation of dormant mRNAs with short polyA tails, resulting in their translation. Members of this protein family regulate translation of cyclin B1 during embryonic cell divisions. Multiple transcript variants encoding different isoforms have been found for this gene.
cytoplasmic polyadenylation element binding protein 1
, CPE-binding protein 1
, cytoplasmic polyadenylation element-binding protein 1
, cytoplasmic polyadenylation element-binding protein 1-like
, Orb/CPEB-related RNA-binding protein
, protein Zorba
, zebrafish orb-type a
, CPEB-related RNA binding protein