scholarly journals The low complexity motif of cytoplasmic polyadenylation element binding protein 3 (CPEB3) is critical for the trafficking of its targets in neurons

2020 ◽  
Author(s):  
Lenzie Ford ◽  
Arun Asok ◽  
Arielle D. Tripp ◽  
Cameron Parro ◽  
Michelle Fitzpatrick ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Low Complexity ◽  
Long Term Memory ◽  
Cytoplasmic Polyadenylation ◽  
Term Memory ◽  
Local Protein Synthesis ◽  
Element Binding Protein ◽  
Local Protein

SummaryBiomolecular condensates, membraneless organelles found throughout the cell, play critical roles in many aspects of cellular function. Ribonucleoprotein granules (RNPs), a type of biomolecular condensate found in neurons that are necessary for local protein synthesis and are involved in long-term potentiation (LTP). Several RNA-binding proteins present in RNPs are necessary for the synaptic plasticity involved in LTP and long-term memory. Most of these proteins possess low complexity motifs, allowing for increased promiscuity. We explore the role the low complexity motif plays for RNA binding protein cytoplasmic polyadenylation element binding protein 3 (CPEB3), a protein necessary for long-term memory persistence. We found that RNA binding and SUMOylation are necessary for CPEB3 localization to the P body, thereby having functional implications on translation. Here, we investigate the role of the low complexity motif of CPEB3 and find that it is necessary for P body localization and downstream targeting for local protein synthesis.

Hippocampal long term memory: Effect of the cholinergic system on local protein synthesis

2013 ◽  
Vol 106 ◽  
pp. 246-257 ◽  
Author(s):  
Daniele Lana ◽  
Francesca Cerbai ◽  
Jacopo Di Russo ◽  
Francesca Boscaro ◽  
Ambra Giannetti ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Memory Effect ◽  
Cholinergic System ◽  
Long Term Memory ◽  
Term Memory ◽  
Local Protein Synthesis ◽  
Local Protein

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.

Deficient long-term memory in mice with a targeted mutation of the cAMP-responsive element-binding protein

Cell ◽  
1994 ◽  
Vol 79 (1) ◽  
pp. 59-68 ◽  
Author(s):  
Roussoudan Bourtchuladze ◽  
Bruno Frenguelli ◽  
Julie Blendy ◽  
Diana Cioffi ◽  
Gunther Schutz ◽  
...  
Keyword(s):  
Binding Protein ◽  
Long Term Memory ◽  
Term Memory ◽  
Targeted Mutation ◽  
Element Binding Protein ◽  
Responsive Element ◽  
Camp Responsive Element Binding

scholarly journals Long-Term Memory Is Facilitated by cAMP Response Element-Binding Protein Overexpression in the Amygdala

2001 ◽  
Vol 21 (7) ◽  
pp. 2404-2412 ◽  
Author(s):  
Sheena A. Josselyn ◽  
Chanjun Shi ◽  
William A. Carlezon ◽  
Rachael L. Neve ◽  
Eric J. Nestler ◽  
...  
Keyword(s):  
Binding Protein ◽  
Camp Response Element Binding ◽  
Long Term Memory ◽  
Protein Overexpression ◽  
Camp Response Element ◽  
Response Element ◽  
Term Memory ◽  
Element Binding Protein

scholarly journals The CPEB3 ribozyme modulates hippocampal-dependent memory

2021 ◽  
Author(s):  
Claire C. Chen ◽  
Joseph Han ◽  
Carlene A. Chinn ◽  
Xiang Li ◽  
Mehran Nikan ◽  
...  
Keyword(s):  
Cortical Neurons ◽  
Antisense Oligonucleotide ◽  
Long Term Memory ◽  
Cytoplasmic Polyadenylation ◽  
Term Memory ◽  
Mrna Maturation ◽  
Element Binding Protein ◽  
Cultured Cortical Neurons ◽  
Underlying Mechanisms

AbstractA self-cleaving ribozyme mapping to an intron of the cytoplasmic polyadenylation element binding protein 3 (CPEB3) gene has been suggested to play a role in human episodic memory, but the underlying mechanisms mediating this effect are not known. The ribozymes maps to the second intron of the CPEB3 gene and its self-scission half-life matches the time it takes an RNA polymerase to reach the immediate downstream exon, suggesting that the ribozyme-dependent intron cleavage is tuned to co-transcriptional splicing of the CPEB3 mRNA. Here we report that the murine ribozyme modulates its own host mRNA maturation in both cultured cortical neurons and the hippocampus. Inhibition of the ribozyme using an antisense oligonucleotide leads to increased CPEB3 protein expression, which enhances polyadenylation and translation of localized plasticity-related target mRNAs, and subsequently strengthens hippocampal-dependent long-term memory. These findings reveal a previously unknown role for self-cleaving ribozyme activity in regulating experience-induced co-transcriptional and local translational processes required for learning and memory.

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