scholarly journals Cytoplasmic Polyadenylation Element-Binding Protein Regulates Neurotrophin-3-Dependent  -Catenin mRNA Translation in Developing Hippocampal Neurons

2009 ◽  
Vol 29 (43) ◽  
pp. 13630-13639 ◽  
Author(s):  
M. Kundel ◽  
K. J. Jones ◽  
C. Y. Shin ◽  
D. G. Wells
Keyword(s):  
Hippocampal Neurons ◽  
Binding Protein ◽  
Mrna Translation ◽  
Cytoplasmic Polyadenylation ◽  
Neurotrophin 3 ◽  
Element Binding Protein

Corrigendum to: Cytoplasmic polyadenylation element binding protein 2 (CPEB2) is required for tight-junction assembly for establishment of porcine trophectoderm epithelium

2019 ◽  
Vol 31 (3) ◽  
pp. 632
Author(s):  
Jeongwoo Kwon ◽  
Shuha Park ◽  
Min-Jung Seong ◽  
Inchul Choi ◽  
Nam-Hyung Kim
Keyword(s):  
Tight Junction ◽  
Mrna Stability ◽  
Rna Binding ◽  
Binding Protein ◽  
Mrna Translation ◽  
Coxsackie Virus ◽  
Cytoplasmic Polyadenylation ◽  
Apical Cell Membrane ◽  
Junction Protein ◽  
Element Binding Protein

Cytoplasmic polyadenylation element binding protein (CPEB) is an RNA-binding protein that promotes elongation of poly(A) tails and regulates mRNA translation. CPEB depletion in mammary epithelium is known to disrupt tight-junction (TJ) assembly via mislocalisation of tight junction protein 1 (TJP1), but the role of CPEB in the biological functions associated with TJs has not yet been studied. The objective of this study was to investigate the roles of CPEB2 during porcine parthenote development. CPEB2 was detected in both the nuclei and apical cytoplasm at the 4- and 8-cell stages and was localised to cell–cell contact after the initiation of the morula stage. Its depletion led to retarded blastocyst formation caused by impaired TJ assembly. Moreover, transcription of TJ-associated genes, including TJP1, Coxsackie virus and adenovirus receptor (CXADR) and occludin (OCLN), was not affected, but the corresponding proteins were not properly localised at the apical cell membrane in morulae, suggesting that CPEB2 confers mRNA stability or determines subcellular localisation for translation. Remarkably reduced relative levels of TJP1 transcripts bearing the 3′-untranslated region were noted, indicating that CPEB2 mediates TJP1 mRNA stability. In conclusion, our findings demonstrate that because of its regulation of TJP1, CPEB2 is required for TJ assembly during porcine blastocyst development.

Cytoplasmic polyadenylation element binding protein 2 (CPEB2) is required for tight-junction assembly for establishment of porcine trophectoderm epithelium

2019 ◽  
Vol 31 (2) ◽  
pp. 412 ◽  
Author(s):  
Jeongwoo Kwon ◽  
Shuha Park ◽  
Min-Jung Seong ◽  
Inchul Choi ◽  
Nam-Hyung Kim
Keyword(s):  
Tight Junction ◽  
Mrna Stability ◽  
Rna Binding ◽  
Binding Protein ◽  
Mrna Translation ◽  
Coxsackie Virus ◽  
Cytoplasmic Polyadenylation ◽  
Apical Cell Membrane ◽  
Junction Protein ◽  
Element Binding Protein

Cytoplasmic polyadenylation element binding protein (CPEB) is an RNA-binding protein that promotes elongation of poly(A) tails and regulates mRNA translation. CPEB depletion in mammary epithelium is known to disrupt tight-junction (TJ) assembly via mislocalisation of tight junction protein 1 (TJP1), but the role of CPEB in the biological functions associated with TJs has not yet been studied. The objective of this study was to investigate the roles of CPEB2 during porcine parthenote development. CPEB2 was detected in both the nuclei and apical cytoplasm at the 4- and 8-cell stages and was localised to cell–cell contact after the initiation of the morula stage. Its depletion led to retarded blastocyst formation caused by impaired TJ assembly. Moreover, transcription of TJ-associated genes, including TJP1, Coxsackie virus and adenovirus receptor (CXADR) and occludin (OCLN), was not affected, but the corresponding proteins were not properly localised at the apical cell membrane in morulae, suggesting that CPEB2 confers mRNA stability or determines subcellular localisation for translation. Remarkably reduced relative levels of TJP1 transcripts bearing the 3′-untranslated region were noted, indicating that CPEB2 mediates TJP1 mRNA stability. In conclusion, our findings demonstrate that because of its regulation of TJP1, CPEB2 is required for TJ assembly during porcine blastocyst development.

scholarly journals A continuous model of physiological prion aggregation suggests a role for Orb2 in gating long-term synaptic information

2018 ◽  
Vol 5 (12) ◽  
pp. 180336
Author(s):  
Michele Sanguanini ◽  
Antonino Cattaneo
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Mrna Translation ◽  
Continuous Model ◽  
Cellular Level ◽  
Long Term Memory ◽  
Cytoplasmic Polyadenylation ◽  
Differential Model

The regulation of mRNA translation at the level of the synapse is believed to be fundamental in memory and learning at the cellular level. The family of cytoplasmic polyadenylation element binding (CPEB) proteins emerged as an important RNA-binding protein family during development and in adult neurons. Drosophila Orb2 (homologue of mouse CPEB3 protein and of the neural isoform of Aplysia CPEB) has been found to be involved in the translation of plasticity-dependent mRNAs and has been associated with long-term memory. Orb2 protein presents two main isoforms, Orb2A and Orb2B, which form an activity-induced amyloid-like functional aggregate, thought to be the translation-inducing state of the RNA-binding protein. Here we present a first two-states continuous differential model for Orb2A–Orb2B aggregation. This model provides new working hypotheses for studying the role of prion-like CPEB proteins in long-term synaptic plasticity. Moreover, this model can be used as a first step to integrate translation- and protein aggregation-dependent phenomena in synaptic facilitation rules.

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