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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

CUGBP, Elav-like family member 2

CUGBP2, ETR-3, NAPOR, BRUNOL3
Members of the CELF/BRUNOL protein family contain two N-terminal RNA recognition motif (RRM) domains, one C-terminal RRM domain, and a divergent segment of 160-230 aa between the second and third RRM domains. Members of this protein family regulate pre-mRNA alternative splicing and may also be involved in mRNA editing, and translation. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CUGBP1, CAN, EXP, ACID, cyclooxygenase
Papers on CUGBP2
Upregulation of cugbp2 increases response of pancreatic cancer cells to chemotherapy.
New
Dambrauskas et al., Kaunas, Lithuania. In Langenbecks Arch Surg, Jan 2016
PURPOSE: Altered expression and/or function of ribosomal RNA (rRNA)-binding proteins CUGBP2/CELF2 might influence post-transcriptional regulation of the HO-1- and COX-2-mediated cytoprotective pathways and represents an important therapeutic target.
Microarray analysis of neonatal rat anteroventral periventricular transcriptomes identifies the proapoptotic Cugbp2 gene as sex-specific and regulated by estradiol.
New
Petersen et al., Amherst Center, United States. In Neuroscience, Oct 2015
Of targets that changed similarly in males and E2-treated females, the gene encoding CUG triplet repeat, RNA-binding protein 2 (Cugbp2), a proapoptotic protein, showed the highest fold-changes.
Downregulation of miR-95-3p inhibits proliferation, and invasion promoting apoptosis of glioma cells by targeting CELF2.
New
Yang et al., Shijiazhuang, China. In Int J Oncol, Sep 2015
We searched on-line tool Targetscan and selected CELF (CUGBP- and ETR-3-like family 2) as a putative target.
Purification and partial characterization of a ribosome-inactivating protein from the latex of Euphorbia trigona Miller with cytotoxic activity toward human cancer cell lines.
New
Castañón et al., Vitoria-Gasteiz, Spain. In Phytomedicine, Aug 2015
RESULTS: Three isolectins, ETR1, ETR2 and ETR3, were purified by anion exchange chromatography.
Identification of differentially expressed genes and small molecule drugs for the treatment of tendinopathy using microarray analysis.
New
Lou et al., Shanghai, China. In Mol Med Report, Apr 2015
The most significant microRNA, miR‑499, was screened and was found to regulate specific genes, including CUGBP2 and MYB.
Genetic association of CUGBP2 and DNMBP with Alzheimer' s disease in the Chinese Han population.
Wu et al., Hangzhou, China. In Curr Alzheimer Res, 2014
OBJECTIVE: Recently, candidate genetic studies revealed the single nucleotide polymorphisms (SNPs) of CUGBP2 (rs2242451) and DNMBP (rs11190305 and rs3740058) associated with Alzheimer's disease (AD).
How slow RNA polymerase II elongation favors alternative exon skipping.
Kornblihtt et al., Buenos Aires, Argentina. In Mol Cell, 2014
Using CFTR alternative exon 9 (E9) as a model, we show here that slowing down elongation can also cause exon skipping by promoting the recruitment of the negative factor ETR-3 onto the UG-repeat at E9 3' splice site, which displaces the constitutive splicing factor U2AF65 from the overlapping polypyrimidine tract.
Role of microRNA-95 in the anticancer activity of Brucein D in hepatocellular carcinoma.
Chen et al., Hong Kong, Hong Kong. In Eur J Pharmacol, 2014
We further identified CUG triplet repeat RNA-binding protein 2 (CUGBP2) as the downstream target of miR-95.
Evaluating the effects of CELF1 deficiency in a mouse model of RNA toxicity.
Mahadevan et al., Charlottesville, United States. In Hum Mol Genet, 2014
The toxic RNA transcripts produced from the mutant allele alter the function of RNA-binding proteins leading to the functional depletion of muscleblind-like (MBNL) proteins and an increase in steady state levels of CUG-BP1 (CUGBP-ETR-3 like factor 1, CELF1).
Purification, crystallization and preliminary crystallographic studies of C-terminal RNA recognition motif (RRM-3) of human ELAV-type RNA-binding protein 3 (ETR-3).
Bhavesh et al., New Delhi, India. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2013
Human embryonically lethal abnormal vision (ELAV)-type RNA-binding protein 3 (ETR-3) has been implicated in many aspects of RNA-processing events including alternative splicing, stability, editing and translation.
Alternative splicing of the neurofibromatosis type I pre-mRNA.
Review
Lou et al., Cleveland, United States. In Biosci Rep, 2012
Exon 23a inclusion is tightly regulated by at least three different families of RNA-binding proteins: CELF {CUG-BP (cytosine-uridine-guanine-binding protein) and ETR-3 [ELAV (embryonic lethal abnormal vision)-type RNA-binding protein]-like factor}, Hu and TIA-1 (T-cell intracellular antigen 1)/TIAR (T-cell intracellular antigen 1-related protein).
Mis-splicing of Tau exon 10 in myotonic dystrophy type 1 is reproduced by overexpression of CELF2 but not by MBNL1 silencing.
GeneRIF
Sergeant et al., Lille, France. In Biochim Biophys Acta, 2011
results indicate the occurrence of a mis-splicing event in myotonic dystrophy type 1 that is induced neither by a loss of muscleblind-like 1 (MBNL1) function nor by a gain of CUGBP1
Signal- and development-dependent alternative splicing of LEF1 in T cells is controlled by CELF2.
GeneRIF
Lynch et al., Philadelphia, United States. In Mol Cell Biol, 2011
Alternative splicing of LEF1 exon 6 is regulated during pre-TCR signaling in thymic development and in response to activation of the JSL1 T-cell line and this is driven by the activity of CELF2.
Genome-wide association of familial late-onset Alzheimer's disease replicates BIN1 and CLU and nominates CUGBP2 in interaction with APOE.
GeneRIF
NIA-LOAD/NCRAD Family Study Group et al., Seattle, United States. In Plos Genet, 2011
There was evidence of association for recently-reported late-onset Alzheimer's disease risk loci, including BIN1 and CLU and CUGBP2 with APOE.
The role of CELF proteins in neurological disorders.
Review
Spickett et al., London, United Kingdom. In Rna Biol, 2010
CELF (CUG-BP and ETR-3-like factors) proteins are structurally related RNA-binding proteins involved in various aspects of RNA processing including splicing and mRNA stability.
Growth factor regulation of prostaglandin-endoperoxide synthase 2 (Ptgs2) expression in colonic mesenchymal stem cells.
GeneRIF
Stappenbeck et al., Saint Louis, United States. In J Biol Chem, 2010
Colonic MSCs expressed high Ptgs2 levels as a consequence of mRNA stabilization downstream of Fgf9. This stabilization was mediated partially through a mechanism involving endogenous CUG-binding protein 2.
The CUGBP2 splicing factor regulates an ensemble of branchpoints from perimeter binding sites with implications for autoregulation.
GeneRIF
Grabowski et al., Pittsburgh, United States. In Plos Genet, 2009
CUGBP2 interacts with functionally significant RNA motifs surrounding the branch sites upstream of exon 6 of the CUGBP2 transcript itself.
Mammalian CELF/Bruno-like RNA-binding proteins: molecular characteristics and biological functions.
Review
Osborne et al., Rennes, France. In Biochimie, 2006
The founder members of the family are the CUG-BP1 (CELF1) and ETR-3 (CELF2) proteins.
The Muscleblind family of proteins: an emerging class of regulators of developmentally programmed alternative splicing.
Review
Artero et al., Valencia, Spain. In Differentiation, 2006
Human Muscleblind homologs MBNL1, MBNL2 and MBNL3 promote inclusion or exclusion of specific exons on different pre-mRNAs by antagonizing the activity of CUG-BP and ETR-3-like factors (CELF proteins) bound to distinct intronic sites.
Molecular biology of the small intestine.
Review
Anant et al., New Delhi, India. In Curr Opin Gastroenterol, 2006
Manipulation of CUGBP2 expression may modulate the response of normal intestine to radiation therapy.
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