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

Parp2  -  poly (ADP-ribose) polymerase family, member 2

Mus musculus

 
 
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 Parp2

 

High impact information on Parp2

  • Poly-(ADP-ribose) polymerase-2 (PARP-2) belongs to a large family of enzymes that synthesize and transfer ADP-ribose polymers to acceptor proteins, modifying their functional properties [5].
  • In addition, DP thymocytes from Parp-2(-/-) have a reduced expression of T-cell receptor (TCR)alpha and a skewed repertoire of TCRalpha toward the 5' Jalpha segments [5].
  • Here we show that inactivation of mouse Parp-2, but not Parp-1, produced a two-fold reduction in CD4(+)CD8(+) double-positive (DP) thymocytes associated with decreased DP cell survival [5].
  • Functional interaction between PARP-1 and PARP-2 in chromosome stability and embryonic development in mouse [6].
  • The DNA damage-dependent poly(ADP-ribose) polymerases, PARP-1 and PARP-2, homo- and heterodimerize and are both involved in the base excision repair (BER) pathway [6].
 

Biological context of Parp2

  • As indicated by site-directed mutagenesis, PARP-2 cleavage occurs preferentially at the LQMD sequence mapped between the DNA binding and the catalytic domains of the protein [1].
  • The generation by homologous recombination of deficient mouse models have confirmed the caretaker function of PARP-1 and PARP-2 in mammalian cells under genotoxic stress [7].
  • This review summarizes our present knowledge on their physiological role in the cellular response to DNA damage and on the genetic interactions between PARP-1, PARP-2, Atm that play an essential role during early embryogenesis [7].
  • Together, these results support the notion that PARP-1 and PARP-2 possess both overlapping and non-redundant functions in the maintenance of genomic stability [6].
  • Reporter gene constructs showed that the 113-base pair intergenic region was indeed sufficient for the expression of both genes and revealed the importance of both the TATA and the DSE/Oct-1 expression control elements for the PARP-2 gene transcription [8].
 

Anatomical context of Parp2

  • Finally, we show that murine fibroblasts deficient in PARP-1 or PARP-2 are not affected in the transcription of ribosomal RNAs [9].
  • Moreover, Parp-2(-/-) spermatids are severely compromised in differentiation and exhibit a marked delay in nuclear elongation [10].
  • Altogether, our findings indicate that, in addition to its well known role in DNA repair, Parp-2 exerts essential functions during meiosis I and haploid gamete differentiation [10].
  • Although Parp-2(-/-) spermatocytes exhibit normal telomere dynamics and normal chromosome synapsis, they display defective meiotic sex chromosome inactivation associated with derailed regulation of histone acetylation and methylation and up-regulated X- and Y-linked gene expression [10].
  • Endogenous PARP-2 was coimmunoprecipitated from transformed mouse lung epithelial cell (MLE15) extracts with TTF-1 and was identified by mass spectrometry [11].
 

Other interactions of Parp2

  • Here we show that PARP-1 and PARP-2 subnuclear distributions partially overlap, with both proteins accumulating within the nucleolus independently of each other [9].
  • We have identified a nuclear localization signal and a nucleolar localization signal within the N-terminal domain of PARP-2 [9].
  • Interestingly, the PARP-2 gene lies head to head with the gene encoding the mouse RNase P RNA subunit [8].
 

Analytical, diagnostic and therapeutic context of Parp2

  • After CA/CPR, PARP-2 deletion significantly increased neuronal cell loss in the hippocampal CA1 field (65%+/-36% ischemic neurons) when compared with WT mice (31%+/-33%), with no effect in either striatum or cortex [2].

References

  1. Active caspase-8 translocates into the nucleus of apoptotic cells to inactivate poly(ADP-ribose) polymerase-2. Benchoua, A., Couriaud, C., Guégan, C., Tartier, L., Couvert, P., Friocourt, G., Chelly, J., Ménissier-de Murcia, J., Onténiente, B. J. Biol. Chem. (2002) [Pubmed]
  2. Differential effect of PARP-2 deletion on brain injury after focal and global cerebral ischemia. Kofler, J., Otsuka, T., Zhang, Z., Noppens, R., Grafe, M.R., Koh, D.W., Dawson, V.L., de Murcia, J.M., Hurn, P.D., Traystman, R.J. J. Cereb. Blood Flow Metab. (2006) [Pubmed]
  3. Antisense oligonucleotides to poly(ADP-ribose) polymerase-2 ameliorate colitis in interleukin-10-deficient mice. Popoff, I., Jijon, H., Monia, B., Tavernini, M., Ma, M., McKay, R., Madsen, K. J. Pharmacol. Exp. Ther. (2002) [Pubmed]
  4. Inhibition of poly(ADP-ribose) polymerase attenuates the severity of acute pancreatitis and associated lung injury. Mota, R.A., Sánchez-Bueno, F., Saenz, L., Hernández-Espinosa, D., Jimeno, J., Tornel, P.L., Martínez-Torrano, A., Ramírez, P., Parrilla, P., Yélamos, J. Lab. Invest. (2005) [Pubmed]
  5. PARP-2 deficiency affects the survival of CD4(+)CD8(+) double-positive thymocytes. Yélamos, J., Monreal, Y., Saenz, L., Aguado, E., Schreiber, V., Mota, R., Fuente, T., Minguela, A., Parrilla, P., de Murcia, G., Almarza, E., Aparicio, P., Ménissier-de Murcia, J. EMBO J. (2006) [Pubmed]
  6. Functional interaction between PARP-1 and PARP-2 in chromosome stability and embryonic development in mouse. Ménissier de Murcia, J., Ricoul, M., Tartier, L., Niedergang, C., Huber, A., Dantzer, F., Schreiber, V., Amé, J.C., Dierich, A., LeMeur, M., Sabatier, L., Chambon, P., de Murcia, G. EMBO J. (2003) [Pubmed]
  7. PARP-1, PARP-2 and ATM in the DNA damage response: functional synergy in mouse development. Huber, A., Bai, P., de Murcia, J.M., de Murcia, G. DNA Repair (Amst.) (2004) [Pubmed]
  8. A bidirectional promoter connects the poly(ADP-ribose) polymerase 2 (PARP-2) gene to the gene for RNase P RNA. structure and expression of the mouse PARP-2 gene. Ame, J.C., Schreiber, V., Fraulob, V., Dolle, P., de Murcia, G., Niedergang, C.P. J. Biol. Chem. (2001) [Pubmed]
  9. PARP-1 and PARP-2 interact with nucleophosmin/B23 and accumulate in transcriptionally active nucleoli. Meder, V.S., Boeglin, M., de Murcia, G., Schreiber, V. J. Cell. Sci. (2005) [Pubmed]
  10. Poly(ADP-ribose) polymerase-2 contributes to the fidelity of male meiosis I and spermiogenesis. Dantzer, F., Mark, M., Quenet, D., Scherthan, H., Huber, A., Liebe, B., Monaco, L., Chicheportiche, A., Sassone-Corsi, P., de Murcia, G., M??nissier-de Murcia, J. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  11. PARP-2 interacts with TTF-1 and regulates expression of surfactant protein-B. Maeda, Y., Hunter, T.C., Loudy, D.E., Davé, V., Schreiber, V., Whitsett, J.A. J. Biol. Chem. (2006) [Pubmed]
 
WikiGenes - Universities