Cytoplasmic Polyadenylation Element Binding Protein 3 Proteins (CPEB3)

Human Cytoplasmic Polyadenylation Element Binding Protein 3 (CPEB3) interaction partners

1. Overexpression of miR-452-3p promoted cell proliferation and mobility and suppressed apoptosis. MiR-452-3p enhanced EGFR and phosphorylated AKT (pAKT) expression but inhibited p21 expression level. MiR-452-3p promoted hepatocellular carcinoma (HCC)cell proliferation and mobility by directly targeting the CPEB3/EGFR axis

2. Data show that the expression of cytoplasmic polyadenylation element binding protein 3 (CPEB3) positively correlated with tumor progression and malignancy but negatively correlated with protein phosphorylation in the alternatively spliced region.

3. Expression of miR-26a and miR-29a was significantly down regulated in leukoplakia and cancer tissues but up regulated in lichen planus tissues. Expression of target genes such as, ADAMTS7, ATP1B1, COL4A2, CPEB3, CDK6, DNMT3a and PI3KR1 was significantly down regulated in at least two of three disease types with respect to normal tissues.

4. Data show that EGF receptor (EGFR) is involved in the microRNA miR-107 pathogenesis of hepatocellular carcinoma (HCC) through cytoplasmic polyadenylation element binding protein 3 (CPEB3).

5. Data suggest that the RNA recognition motif (RRM) domain of CPEB3 (as a soluble peptide fragment) exhibits protein conformation distinct from those of the canonical RRM domain.

6. cleavage of CPEB3 by NMDA-activated calpain 2 accounts for the activity-related translation of CPEB3-targeted RNAs

7. Together, these results indicate that Tob mediates the recruitment of Caf1 to the target of CPEB3 and elicits deadenylation and decay of the mRNA.

8. Secondary structure determination and native gel analyses reveal that the cleaved population of the CPEB3 ribozyme has a single, secondary structure that closely resembles the HDV ribozyme

9. isolation of a ribozyme conserved mammalian sequence that resides in an intron of the CPEB3 gene

Mouse (Murine) Cytoplasmic Polyadenylation Element Binding Protein 3 (CPEB3) interaction partners

1. Topological regulation of synaptic AMPA receptor expression by the RNA-binding protein CPEB3 has been demonstrated.

2. CPEB3-regulated translation of TRPV1 RNA may play a role in fine-tuning thermal sensitivity of nociceptors.

3. CPEB3 is SUMOylated in hippocampal neurons. CPEB3 regulates SUMO-2 translation.

4. CPEB3 interacts with the actin cytoskeleton in yeast and at mouse synapses. CPEB3 is a functional prion with a tripartite prion domain architecture.

5. The main finding of our study is that CPEB3-mediated protein synthesis is required for long-term hippocampal-based memory storage.

6. Cpeb3 null mice exhibited enhanced short-term fear memory and translationally elevated PSD95, NMDA receptors and GluA1.

7. cleavage of CPEB3 by NMDA-activated calpain 2 accounts for the activity-related translation of CPEB3-targeted RNAs

8. These results suggest a model whereby Neuralized1-dependent ubiquitination facilitates hippocampal plasticity and hippocampal-dependent memory storage by modulating the activity of CPEB3 and CPEB3-dependent protein synthesis and synapse formation.

9. CPEB3 has a novel function in the nucleus as to suppress Stat5b-dependent EGFR gene transcription

10. show that CPEB3 expression is increased in a time-dependent manner during the course of postnatal development, and CPEB3 is localized mostly in the inner retina, including retinal ganglion cells.

11. CPEB3 is expressed in the principal cell layers of the hippocampus

12. CPEB3 is a sequence-specific translational regulatory protein.