gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 02 Oct 2014.

CUGBP, Elav-like family member 1

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. This gene may play a role in myotonic dystrophy type 1 (DM1) via interactions with the dystrophia myotonica-protein kinase (DMPK) gene. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008] (from NCBI)
Sponsored links
Top mentioned proteins: DM2, EXP, CUGBP2, 4E-BP1, V1a
Papers on CUGBP1
Evaluating the effects of CELF1 deficiency in a mouse model of RNA toxicity.
Mahadevan et al., Charlottesville, United States. In Hum Mol Genet, Feb 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).
A defective Krab-domain zinc-finger transcription factor contributes to altered myogenesis in myotonic dystrophy type 1.
Martinat et al., France. In Hum Mol Genet, Jan 2014
In this paper, we show that this defect in expression, which derives from a loss of RNA stability, is controlled by the RNA-binding protein, CUGBP1, and is associated with impaired myogenesis-a functional defect reminiscent of that observed in DM1.
Suppression of CUGBP1 inhibits growth of hepatocellular carcinoma cells.
Qin et al., In Clin Invest Med, Dec 2013
PURPOSE: The multifunctional RNA-binding protein, CUGBP1, regulates splicing, stability and translation of mRNAs.
Exercise training increases the expression and nuclear localization of mRNA destabilizing proteins in skeletal muscle.
Holloway et al., Guelph, Canada. In Am J Physiol Regul Integr Comp Physiol, Nov 2013
Therefore, in the current study we have examined whether exercise promotes mRNA accumulation through the induction of proteins affiliated with mRNA stabilization (human antigen R, HuR) or conversely by decreasing the expression of mRNA destabilizing proteins [AU-rich binding factor (AUF1) and CUG binding protein (CUG-BP1)].
Molecular mechanisms of muscle atrophy in myotonic dystrophies.
Timchenko, Houston, United States. In Int J Biochem Cell Biol, Oct 2013
These expansions cause DM pathologies through accumulation of mutant RNAs that alter RNA metabolism in patients' tissues by targeting RNA-binding proteins such as CUG-binding protein 1 (CUGBP1) and Muscle blind-like protein 1 (MBNL1).
Dysfunction of protein homeostasis in myotonic dystrophies.
Timchenko et al., Milano, Italy. In Histol Histopathol, Sep 2013
The pathogenic role of CUG and CCUG repeats in the mis-regulation of alternative splicing, mediated by RNA-binding proteins CUGBP1 and MBNL1, has been discussed in a number of excellent reviews.
Overexpression of CUGBP1 in skeletal muscle from adult classic myotonic dystrophy type 1 but not from myotonic dystrophy type 2.
Meola et al., Milano, Italy. In Plos One, 2012
The common key feature of DM pathogenesis is nuclear accumulation of mutant RNA which causes aberrant alternative splicing of specific pre-mRNAs by altering the functions of two RNA binding proteins, MBNL1 and CUGBP1.
Celf1 regulation of dmrt2a is required for somite symmetry and left-right patterning during zebrafish development.
Bessho et al., Nara, Japan. In Development, 2012
Celf1-dependent fine-tuning of dmrt2a expression is essential for generating bilateral symmetry of somites and left-right asymmetric patterning during zebrafish development.
Myotonic dystrophy: is a narrow focus obscuring the rest of the field?
Mahadevan, Charlottesville, United States. In Curr Opin Neurol, 2012
The role of other RNA-binding proteins beyond MBNL1 and CUGBP1, such as Staufen 1 and DDX5, are being identified and studied with respect to their role in myotonic dystrophy.
The role of CUGBP1 in age-dependent changes of liver functions.
Timchenko et al., Houston, United States. In Ageing Res Rev, 2012
This review is focused on the role of a conserved, multi-functional RNA-binding protein, CUGBP1, in the development of aging phenotype in the liver.
The RNA-binding protein CUG-BP1 increases survivin expression in oesophageal cancer cells through enhanced mRNA stability.
Battafarano et al., Baltimore, United States. In Biochem J, 2012
CUG-BP1 is overexpressed in oesophageal cancer cell lines and human oesophageal cancer specimens. CUG-BP1 associates with the 3'-untranslated region of survivin mRNA.
Regulation of CUG-binding protein 1 (CUGBP1) binding to target transcripts upon T cell activation.
Bohjanen et al., Minneapolis, United States. In J Biol Chem, 2012
CUGBP1 binding to certain GRE-containing target transcripts decreased following T cell activation through activation-dependent phosphorylation of CUGBP1.
miR-503 represses CUG-binding protein 1 translation by recruiting CUGBP1 mRNA to processing bodies.
Wang et al., Baltimore, United States. In Mol Biol Cell, 2012
These findings identify miR-503 as both a novel regulator of CUGBP1 expression and a modulator of intestinal epithelial homoeostasis
The importance of CELF control: molecular and biological roles of the CUG-BP, Elav-like family of RNA-binding proteins.
Ladd et al., Cleveland, United States. In Wiley Interdiscip Rev Rna, 2012
The CUG-BP, Elav-like family (CELF) of RNA-binding proteins regulate several steps of RNA processing in the nucleus and cytoplasm, including pre-mRNA alternative splicing, C to U RNA editing, deadenylation, mRNA decay, and translation.
RNA-binding proteins and gene regulation in myogenesis.
Pavlath et al., Atlanta, United States. In Trends Pharmacol Sci, 2011
The focus of this review is to highlight the roles of the best-characterized RNA-binding proteins in muscle, including HuR, KSRP, CUGBP1, PABPN1, Lin-28 and TTP.
Regulation of cyclin-dependent kinase 4 translation through CUG-binding protein 1 and microRNA-222 by polyamines.
Wang et al., Baltimore, United States. In Mol Biol Cell, 2011
polyamine-regulated CUG-binding protein 1 and miR-222 modulate cyclin-dependent kinase 4 (CDK4) translation at least in part by altering the recruitment of CDK4 mRNA to processing bodies
Expression of 24,426 human alternative splicing events and predicted cis regulation in 48 tissues and cell lines.
Johnson et al., Seattle, United States. In Nat Genet, 2008
An unbiased, systematic screen of 21,760 4-mer to 7-mer words for cis-regulatory motifs identified 143 RNA 'words' enriched near regulated cassette exons, including six clusters of motifs represented by UCUCU, UGCAUG, UGCU, UGUGU, UUUU and AGGG, which map to trans-acting regulators PTB, Fox, Muscleblind, CELF/CUG-BP, TIA-1 and hnRNP F/H, respectively.
Reversible model of RNA toxicity and cardiac conduction defects in myotonic dystrophy.
Phillips et al., Charlottesville, United States. In Nat Genet, 2006
However, we observed increased levels of CUG-binding protein (CUG-BP1) in skeletal muscle, as seen in individuals with DM1.
Aberrant regulation of insulin receptor alternative splicing is associated with insulin resistance in myotonic dystrophy.
Cooper et al., Houston, United States. In Nat Genet, 2001
Steady-state levels of CUG-BP, a regulator of pre-mRNA splicing proposed to mediate some aspects of DM1 pathogenesis, are increased in DM1 skeletal muscle; overexpression of CUG-BP in normal cells induces a switch to IR-A.
Disruption of splicing regulated by a CUG-binding protein in myotonic dystrophy.
Cooper et al., Houston, United States. In Science, 1998
Data presented here indicate that the conserved heterogeneous nuclear ribonucleoprotein, CUG-binding protein (CUG-BP), may mediate the trans-dominant effect of the RNA.
share on facebooktweetadd +1mail to friends