The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

CELF2  -  CUGBP, Elav-like family member 2

Homo sapiens

Synonyms: BRUNOL3, Bruno-like protein 3, CELF-2, CUG triplet repeat RNA-binding protein 2, CUG-BP-and ETR-3-like factor 2, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of CUGBP2

 

High impact information on CUGBP2

 

Biological context of CUGBP2

 

Anatomical context of CUGBP2

  • In the mouse large intestine, the editing was 48% and had a 2.7-fold relatively greater CUGBP2 level [11].
  • In the human intestinal cell line Caco-2, the increase of apoB mRNA editing from approximately 1.7% to approximately 23% was associated with 6- and 3.2-fold increases of apobec-1 and CUGBP2, respectively [11].
  • Short interfering RNA-mediated gene-specific knockdown of CUGBP2, GRY-RBP, and hnRNP-C1 resulted in increased editing in Caco-2 cells, consistent with their known inhibitory function [11].
  • Furthermore, FLAG-tagged HuR and myc-tagged CUGBP2 colocalize in the nucleus of HCT-116 cells [7].
  • Expression and mutation analysis of BRUNOL3, a candidate gene for heart and thymus developmental defects associated with partial monosomy 10p [2].
 

Associations of CUGBP2 with chemical compounds

  • These effects were reversed by NS398, a COX-2-specific inhibitor, suggesting that lipopolysaccharide-mediated inhibition of CUGBP2 is a PG-dependent mechanism [12].
  • Dynamic antagonism between RNA-binding protein CUGBP2 and cyclooxygenase-2-mediated prostaglandin E2 in radiation damage [12].
  • CUGBP2 binds apoB RNA, specifically an AU-rich sequence located immediately upstream of the edited cytidine [8].
  • Five ethylene receptor genes, OS-ERS1, OS-ERS2, OS-ETR2, OS-ETR3, and OS-ETR4 were isolated and characterized from rice [13].
  • The compound also effectively inhibited the biological and biochemical responses caused by another axonopathy inducer, colchicine, including tyrosine phosphorylation of Pyk2, formation of an 85-kDa poly(ADP-ribose)polymerase (PARP) fragment and apoptosis-associated induction of the NAPOR gene as well as neuronal cell death [14].
 

Other interactions of CUGBP2

  • Genomic organization and isoform-specific tissue expression of human NAPOR (CUGBP2) as a candidate gene for familial arrhythmogenic right ventricular dysplasia [4].
  • We identified a 20-residue region of CELF4 required for repression or activation, in contrast to ETR-3, for which the required residues are more disperse [15].
  • We created minigenes for two of these genes, the CFTR and MTMR1 genes, and confirmed that ETR-3 regulates their splicing patterns [10].
  • By using cellular models with a control- or DM1-like splicing pattern of Tau transcripts, we demonstrate that ETR-3 promotes selectively the exclusion of Tau exon 2 [3].
  • The founder members of the family are the CUG-BP1 (CELF1) and ETR-3 (CELF2) proteins [16].
 

Analytical, diagnostic and therapeutic context of CUGBP2

References

  1. CUGBP2 plays a critical role in apoptosis of breast cancer cells in response to genotoxic injury. Mukhopadhyay, D., Jung, J., Murmu, N., Houchen, C.W., Dieckgraefe, B.K., Anant, S. Ann. N. Y. Acad. Sci. (2003) [Pubmed]
  2. Expression and mutation analysis of BRUNOL3, a candidate gene for heart and thymus developmental defects associated with partial monosomy 10p. Lichtner, P., Attié-Bitach, T., Schuffenhauer, S., Henwood, J., Bouvagnet, P., Scambler, P.J., Meitinger, T., Vekemans, M. J. Mol. Med. (2002) [Pubmed]
  3. ETR-3 represses Tau exons 2/3 inclusion, a splicing event abnormally enhanced in myotonic dystrophy type I. Leroy, O., Dhaenens, C.M., Schraen-Maschke, S., Belarbi, K., Delacourte, A., Andreadis, A., Sablonnière, B., Buée, L., Sergeant, N., Caillet-Boudin, M.L. J. Neurosci. Res. (2006) [Pubmed]
  4. Genomic organization and isoform-specific tissue expression of human NAPOR (CUGBP2) as a candidate gene for familial arrhythmogenic right ventricular dysplasia. Li, D., Bachinski, L.L., Roberts, R. Genomics (2001) [Pubmed]
  5. Coupled mRNA stabilization and translational silencing of cyclooxygenase-2 by a novel RNA binding protein, CUGBP2. Mukhopadhyay, D., Houchen, C.W., Kennedy, S., Dieckgraefe, B.K., Anant, S. Mol. Cell (2003) [Pubmed]
  6. Dynamic antagonism between ETR-3 and PTB regulates cell type-specific alternative splicing. Charlet-B, N., Logan, P., Singh, G., Cooper, T.A. Mol. Cell (2002) [Pubmed]
  7. Functional Antagonism Between RNA Binding Proteins HuR and CUGBP2 Determines the Fate of COX-2 mRNA Translation. Sureban, S.M., Murmu, N., Rodriguez, P., May, R., Maheshwari, R., Dieckgraefe, B.K., Houchen, C.W., Anant, S. Gastroenterology (2007) [Pubmed]
  8. Novel role for RNA-binding protein CUGBP2 in mammalian RNA editing. CUGBP2 modulates C to U editing of apolipoprotein B mRNA by interacting with apobec-1 and ACF, the apobec-1 complementation factor. Anant, S., Henderson, J.O., Mukhopadhyay, D., Navaratnam, N., Kennedy, S., Min, J., Davidson, N.O. J. Biol. Chem. (2001) [Pubmed]
  9. A web-accessible complete transcriptome of normal human and DMD muscle. Bakay, M., Zhao, P., Chen, J., Hoffman, E.P. Neuromuscul. Disord. (2002) [Pubmed]
  10. Identification of putative new splicing targets for ETR-3 using sequences identified by systematic evolution of ligands by exponential enrichment. Faustino, N.A., Cooper, T.A. Mol. Cell. Biol. (2005) [Pubmed]
  11. ApoB mRNA editing is mediated by a coordinated modulation of multiple apoB mRNA editing enzyme components. Chen, Z., Eggerman, T.L., Patterson, A.P. Am. J. Physiol. Gastrointest. Liver Physiol. (2007) [Pubmed]
  12. Dynamic antagonism between RNA-binding protein CUGBP2 and cyclooxygenase-2-mediated prostaglandin E2 in radiation damage. Murmu, N., Jung, J., Mukhopadhyay, D., Houchen, C.W., Riehl, T.E., Stenson, W.F., Morrison, A.R., Arumugam, T., Dieckgraefe, B.K., Anant, S. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  13. Differential expression of three genes encoding an ethylene receptor in rice during development, and in response to indole-3-acetic acid and silver ions. Yau, C.P., Wang, L., Yu, M., Zee, S.Y., Yip, W.K. J. Exp. Bot. (2004) [Pubmed]
  14. Discovery of a novel compound: insight into mechanisms for acrylamide-induced axonopathy and colchicine-induced apoptotic neuronal cell death. Nakagawa-Yagi, Y., Choi, D.K., Ogane, N., Shimada, S., Seya, M., Momoi, T., Ito, T., Sakaki, Y. Brain Res. (2001) [Pubmed]
  15. Identification of CELF splicing activation and repression domains in vivo. Han, J., Cooper, T.A. Nucleic Acids Res. (2005) [Pubmed]
  16. Mammalian CELF/Bruno-like RNA-binding proteins: molecular characteristics and biological functions. Barreau, C., Paillard, L., Méreau, A., Osborne, H.B. Biochimie (2006) [Pubmed]
  17. Expression profiling in spinal muscular atrophy reveals an RNA binding protein deficit. Anderson, K.N., Baban, D., Oliver, P.L., Potter, A., Davies, K.E. Neuromuscul. Disord. (2004) [Pubmed]
 
WikiGenes - Universities