scholarly journals Antiproliferative protein Tob directly regulates c-myc proto-oncogene expression through cytoplasmic polyadenylation element-binding protein CPEB

Oncogene ◽  
2012 ◽  
Vol 33 (1) ◽  
pp. 55-64 ◽  
Author(s):  
K Ogami ◽  
N Hosoda ◽  
Y Funakoshi ◽  
S Hoshino
Keyword(s):  
Binding Protein ◽  
Cytoplasmic Polyadenylation ◽  
Oncogene Expression ◽  
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.

Identification and characterization of the gene encoding human cytoplasmic polyadenylation element binding protein

Gene ◽  
2001 ◽  
Vol 263 (1-2) ◽  
pp. 113-120 ◽  
Author(s):  
Joseph F Welk ◽  
Amanda Charlesworth ◽  
Gary D Smith ◽  
Angus M MacNicol
Keyword(s):  
Binding Protein ◽  
Gene Encoding ◽  
Cytoplasmic Polyadenylation ◽  
Element Binding Protein ◽  
Identification And Characterization

scholarly journals Cytoplasmic polyadenylation element binding protein is a conserved target of tumor suppressor HRPT2/CDC73

2010 ◽  
Vol 17 (10) ◽  
pp. 1551-1565 ◽  
Author(s):  
J-H Zhang ◽  
L M Panicker ◽  
E M Seigneur ◽  
L Lin ◽  
C D House ◽  
...  
Keyword(s):  
Tumor Suppressor ◽  
Binding Protein ◽  
Cytoplasmic Polyadenylation ◽  
Element Binding Protein

scholarly journals 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.

1997 ◽  
Vol 17 (11) ◽  
pp. 6402-6409 ◽  
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.

Sign in / Sign up

Export Citation Format

Share Document