Cytoplasmic Polyadenylation Element Binding Protein 3 Proteins (CPEB3)

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

1. Overexpression of miR (show MLXIP Proteins)-452-3p promoted cell proliferation and mobility and suppressed apoptosis. MiR (show MLXIP Proteins)-452-3p enhanced EGFR (show EGFR Proteins) and phosphorylated AKT (pAKT (show AKT1 Proteins)) expression but inhibited p21 (show CDKN1A Proteins) expression level. MiR (show MLXIP Proteins)-452-3p promoted hepatocellular carcinoma (HCC (show FAM126A Proteins))cell proliferation and mobility by directly targeting the CPEB3/EGFR (show EGFR Proteins) 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 (show MLXIP Proteins)-26a and miR (show MLXIP Proteins)-29a was significantly down regulated in leukoplakia and cancer tissues but up regulated in lichen planus tissues. Expression of target genes such as, ADAMTS7 (show ADAMTS7 Proteins), ATP1B1 (show ATP1B1 Proteins), COL4A2 (show COL4a2 Proteins), CPEB3, CDK6 (show CDK6 Proteins), DNMT3a (show DNMT3A Proteins) 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 (show EGFR Proteins)) is involved in the microRNA miR (show MLXIP Proteins)-107 pathogenesis of hepatocellular carcinoma (HCC (show FAM126A Proteins)) 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 (show CAPN2 Proteins) accounts for the activity-related translation of CPEB3-targeted RNAs

7. Together, these results indicate that Tob (show TDO2 Proteins) mediates the recruitment of Caf1 (show CHAF1B Proteins) 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 (show GRIA3 Proteins) receptor expression by the RNA-binding protein CPEB3 has been demonstrated.

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

3. CPEB3 is SUMOylated in hippocampal neurons. CPEB3 regulates SUMO-2 (show SUMO2 Proteins) translation.

4. CPEB3 interacts with the actin cytoskeleton in yeast and at mouse synapses. CPEB3 is a functional prion (show PRNP Proteins) with a tripartite prion (show PRNP Proteins) 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 (show DLG4 Proteins), NMDA receptors and GluA1 (show GRIA1 Proteins).

7. cleavage of CPEB3 by NMDA-activated calpain 2 (show CAPN2 Proteins) 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 (show STAT5B Proteins)-dependent EGFR (show EGFR Proteins) 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.