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

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.

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

Royal Society Open Science ◽

10.1098/rsos.180336 ◽

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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The 36-kilodalton embryonic-type cytoplasmic polyadenylation element-binding protein in Xenopus laevis is ElrA, a member of the ELAV family of RNA-binding proteins.

Molecular and Cellular Biology ◽

10.1128/mcb.17.11.6402 ◽

1997 ◽

Vol 17 (11) ◽

pp. 6402-6409 ◽

Cited By ~ 38

Author(s):

L Wu ◽

P J Good ◽

J D Richter

Keyword(s):

Xenopus Laevis ◽

Binding Proteins ◽

Rna Binding ◽

Rna Binding Proteins ◽

Binding Protein ◽

Dominant Negative ◽

Cytoplasmic Polyadenylation ◽

Element Binding Protein

The translational activation of several maternal mRNAs in Xenopus laevis is dependent on cytoplasmic poly(A) elongation. Messages harboring the UUUUUAU-type cytoplasmic polyadenylation element (CPE) in their 3' untranslated regions (UTRs) undergo polyadenylation and translation during oocyte maturation. This CPE is bound by the protein CPEB, which is essential for polyadenylation. mRNAs that have the poly(U)12-27 embryonic-type CPE (eCPE) in their 3' UTRs undergo polyadenylation and translation during the early cleavage and blastula stages. A 36-kDa eCPE-binding protein in oocytes and embryos has been identified by UV cross-linking. We now report that this 36-kDa protein is ElrA, a member of the ELAV family of RNA-binding proteins. The proteins are identical in size, antibody directed against ElrA immunoprecipitates the 36-kDa protein, and the two proteins have the same RNA binding specificity in vitro. C12 and activin receptor mRNAs, both of which contain eCPEs, are detected in immunoprecipitated ElrA-mRNP complexes from eggs and embryos. In addition, this in vivo interaction requires the eCPE. Although a number of experiments failed to define a role for ElrA in cytoplasmic polyadenylation, the expression of a dominant negative ElrA protein in embryos results in an exogastrulation phenotype. The possible functions of ElrA in gastrulation are discussed.

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

Journal of Neuroscience ◽

10.1523/jneurosci.2910-08.2009 ◽

2009 ◽

Vol 29 (43) ◽

pp. 13630-13639 ◽

Cited By ~ 31

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

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Functioning of the Drosophila orb gene in gurken mRNA localization and translation

Development ◽

10.1242/dev.128.16.3169 ◽

2001 ◽

Vol 128 (16) ◽

pp. 3169-3177 ◽

Cited By ~ 1

Author(s):

Jacqueline S. Chang ◽

Lihua Tan ◽

Melisande R. Wolf ◽

Paul Schedl

Keyword(s):

Signaling Pathway ◽

Rna Binding ◽

Binding Protein ◽

Growth Factor Receptor ◽

Follicle Cell ◽

Posterior Pole ◽

Rna Recognition Motif ◽

Cytoplasmic Polyadenylation ◽

Element Binding Protein ◽

Translational Regulators

The orb gene encodes an RNA recognition motif (RRM)-type RNA-binding protein that is a member of the cytoplasmic polyadenylation element binding protein (CPEB) family of translational regulators. Early in oogenesis, orb is required for the formation and initial differentiation of the egg chamber, while later in oogenesis it functions in the determination of the dorsoventral (DV) and anteroposterior axes of egg and embryo. In the studies reported here, we have examined the role of theorb gene in the gurken (grk)-Drosophila epidermal growth factor receptor (DER) signaling pathway. During the previtellogenic stages of oogenesis, the grk-DER signaling pathway defines the posterior pole of the oocyte by specifying posterior follicle cell identity. This is accomplished through the localized expression of Grk at the very posterior of the oocyte. Later in oogenesis, thegrk-DER pathway is used to establish the DV axis. Grk protein synthesized at the dorsal anterior corner of the oocyte signals dorsal fate to the overlying follicle cell epithelium. We show that orb functions in both the early and late grk-DER signaling pathways, and in each case is required for the localized expression of Grk protein. We have found thatorb is also required to promote the synthesis of a key component of the DV polarity pathway, K(10). Finally, we present evidence that Orb protein expression during the mid- to late stages of oogenesis is, in turn, negatively regulated by K(10).

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

10.1101/2020.05.16.100032 ◽

2020 ◽

Cited By ~ 1

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.

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Identification of RNA-binding proteins specific to Xenopus Eg maternal mRNAs: association with the portion of Eg2 mRNA that promotes deadenylation in embryos

Development ◽

10.1242/dev.116.4.1193 ◽

1992 ◽

Vol 116 (4) ◽

pp. 1193-1202

Author(s):

V. Legagneux ◽

P. Bouvet ◽

F. Omilli ◽

S. Chevalier ◽

H.B. Osborne

Keyword(s):

Untranslated Region ◽

Binding Proteins ◽

Rna Binding ◽

Rna Binding Proteins ◽

Binding Protein ◽

Untranslated Regions ◽

Cytoplasmic Polyadenylation ◽

Element Binding Protein ◽

Maternal Mrnas ◽

Post Transcriptional Regulation

Maternal Xenopus Eg mRNAs have been previously identified as transcripts that are specifically deadenylated after fertilization and degraded after the mid blastula transition. Destabilizing cis sequences were previously localised in the 3′ untranslated region of Eg2 mRNA. In order to characterize possible trans-acting factors which are involved in the post-transcriptional regulation of Eg mRNAs, gel-shift and u.v. cross-linking experiments were performed, which allowed the identification of a p53-p55 RNA-binding protein doublet specific for the 3′ untranslated regions of Eg mRNAs. These p53-p55 proteins do not bind to the 3′ untranslated regions of either ornithine decarboxylase or phosphatase 2Ac mRNAs, which remain polyadenylated in embryos. These novel RNA-binding proteins are distinct from the cytoplasmic polyadenylation element-binding protein that controls the polyadenylation of maternal mRNAs in maturing Xenopus oocytes, and from previously identified thermoresistant RNA-binding proteins present in oocyte mRNP storage particles. The p53-p55 bind a portion of the Eg2 mRNA 3′ untranslated region, distinct from the previously identified destabilizing region, that is able to confer the postfertilization deadenylation of CAT-coding chimeric mRNAs. This suggests that the p53-p55 RNA-binding proteins are good candidates for trans-acting factors involved in the deadenylation of Eg mRNAs in Xenopus embryos.

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