Research TopicsGenomes and Genes
| Cpeb3SummaryGene Symbol: Cpeb3 Description: cytoplasmic polyadenylation element binding protein 3 Alias: 4831444O18Rik, CPE-BP3, mKIAA0940, cytoplasmic polyadenylation element-binding protein 3, CPE-binding protein 3 Species: mouse Products: Cpeb3 Top Publications
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- Chao H, Tsai L, Lu Y, Lin P, Huang W, Chou H, et al. Deletion of CPEB3 enhances hippocampus-dependent memory via increasing expressions of PSD95 and NMDA receptors. J Neurosci. 2013;33:17008-22 pubmed publisher..To understand whether CPEB3 plays a part in learning and memory, we generated CPEB3 knock-out (KO) mice and found that the null mice exhibited ..
- Wang X, Cooper N. Characterization of the transcripts and protein isoforms for cytoplasmic polyadenylation element binding protein-3 (CPEB3) in the mouse retina. BMC Mol Biol. 2009;10:109 pubmed publisher..The purpose of the current study is to investigate the alternative splicing isoforms of a particular CPEB, CPEB3, based on current databases, and to characterize the expression of CPEB3 in the retina...
- Savtchouk I, Sun L, Bender C, Yang Q, Szabo G, Gasparini S, et al. Topological Regulation of Synaptic AMPA Receptor Expression by the RNA-Binding Protein CPEB3. Cell Rep. 2016;17:86-103 pubmed publisher..Graded dendritic depolarizations elevate CPEB3 protein at proximal dendrites, where we suggest that CPEB3 binds to GluA2 mRNA, suppressing GluA2 protein ..
- Fioriti L, Myers C, Huang Y, Li X, Stephan J, Trifilieff P, et al. The Persistence of Hippocampal-Based Memory Requires Protein Synthesis Mediated by the Prion-like Protein CPEB3. Neuron. 2015;86:1433-48 pubmed publisher..plasticity are mediated by the increase in level and in the aggregation of the prion-like translational regulator CPEB3 (cytoplasmic polyadenylation element-binding protein)...
- Chen Y, Bai G, Wu M, Chiao C, Huang Y. Loss of CPEB3 Upregulates MEGF10 to Impair Mosaic Development of ON Starburst Amacrine Cells. Front Mol Neurosci. 2016;9:105 pubmedb>Cytoplasmic polyadenylation element binding protein 3 (CPEB3) regulates target RNA translation in neurons. Here, we examined CPEB3 distribution and function in the mouse retina...
- Lai Y, Su C, Jiang S, Chang Y, Lai A, Huang Y. Deficiency of CPEB2-Confined Choline Acetyltransferase Expression in the Dorsal Motor Nucleus of Vagus Causes Hyperactivated Parasympathetic Signaling-Associated Bronchoconstriction. J Neurosci. 2016;36:12661-12676 pubmed..e., choline acetyltransferase). Consequently, increased parasympathetic signaling leads to hyperactivated bronchoconstriction and abnormal respiration in the KO neonates. ..
- Stephan J, Fioriti L, Lamba N, Colnaghi L, Karl K, Derkatch I, et al. The CPEB3 Protein Is a Functional Prion that Interacts with the Actin Cytoskeleton. Cell Rep. 2015;11:1772-85 pubmed publisherThe mouse cytoplasmic polyadenylation element-binding protein 3 (CPEB3) is a translational regulator implicated in long-term memory maintenance...
- Drisaldi B, Colnaghi L, Fioriti L, Rao N, Myers C, Snyder A, et al. SUMOylation Is an Inhibitory Constraint that Regulates the Prion-like Aggregation and Activity of CPEB3. Cell Rep. 2015;11:1694-702 pubmed publisher..The prion-like cytoplasmic polyadenylation element-binding protein 3 (CPEB3) regulates the translation of several mRNAs important for long-term synaptic plasticity in the hippocampus...
- Campbell Z, Menichelli E, Friend K, Wu J, Kimble J, Williamson J, et al. Identification of a conserved interface between PUF and CPEB proteins. J Biol Chem. 2012;287:18854-62 pubmed publisher..The equivalent loop in human PUM2 is required for binding to human CPEB3 in vitro, although the primary sequences of the human and C. elegans PUF proteins have diverged in that region...
- Chen P, Huang Y. CPEB2-eEF2 interaction impedes HIF-1? RNA translation. EMBO J. 2012;31:959-71 pubmed publisher..This study delineates the molecular mechanism of CPEB2-repressed translation and presents a unique model for controlling transcript-selective translation at elongation. ..
- White R, Boydston L, Brookshier T, McNulty S, Nsumu N, Brewer B, et al. Iron metabolism mutant hbd mice have a deletion in Sec15l1, which has homology to a yeast gene for vesicle docking. Genomics. 2005;86:668-73 pubmed..The hbd mice have an exon deletion in Sec15l1, which is the first known mutation of a SEC gene homologue in mammals. ..