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Gene Review

PABPN1  -  poly(A) binding protein, nuclear 1

Homo sapiens

Synonyms: Nuclear poly(A)-binding protein 1, OPMD, PAB2, PABII, PABP-2, ...
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Disease relevance of PABPN1


High impact information on PABPN1


Chemical compound and disease context of PABPN1


Biological context of PABPN1

  • Here, we show that PABPC1, like the major nuclear poly(A) binding protein PABPN1, associates with nuclear pre-mRNAs that are polyadenylated and intron containing [11].
  • A concomitant reduction of cell death in drug-treated mutant PABPN1 expressing cells was also observed [12].
  • This was achieved by inactivating the mutant PABPN1 nuclear localization signal and by generating full-length mutant PABPN1 fused to a strong nuclear export sequence [13].
  • This indicated larger genetic heterogeneity and showed that unequal crossing-over and not replication slippage must be the underlying mechanism of elongation.We performed sequencing of the PABPN1 gene in 30 German OPDM index patients to determine the exact genotype [14].
  • PABP2 binds to the growing poly(A) tail, stimulating its extension during the polyadenylation process, and limits the length of the newly synthesized poly(A) tail [15].

Anatomical context of PABPN1


Associations of PABPN1 with chemical compounds


Physical interactions of PABPN1


Regulatory relationships of PABPN1

  • The reporter assays showed that PABP2 co-operated with SKIP to synergistically activate E-box-mediated transcription through MYOD: Moreover, both PABP2 and SKIP were directly associated with MyoD to form a single complex [15].
  • In vitro the NS1A protein inhibits the ability of PABII to stimulate the processive synthesis of long poly(A) tails catalyzed by poly(A) polymerase (PAP) [18].

Other interactions of PABPN1

  • The disorder is caused by trinucleotide (GCG) expansions in the N-terminal part of the poly(A)-binding protein 1 (PABPN1) that result in the extension of a 10-alanine segment by up to seven more alanines [19].
  • PABPN1 is involved in the synthesis of poly (A) tails, increasing the processivity of poly (A) polymerase and contributing to defining the length of a newly synthesized poly (A) tail [20].
  • Intriguingly, among FRG1P-associated proteins are SMN and PABPN1, both being involved in neuromuscular disorders, possibly through RNA biogenesis-related processes [21].

Analytical, diagnostic and therapeutic context of PABPN1


  1. Ectopic expression of a polyalanine expansion mutant of poly(A)-binding protein N1 in muscle cells in culture inhibits myogenesis. Wang, Q., Bag, J. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  2. A Drosophila model of oculopharyngeal muscular dystrophy reveals intrinsic toxicity of PABPN1. Chartier, A., Benoit, B., Simonelig, M. EMBO J. (2006) [Pubmed]
  3. Transgenic expression of an expanded (GCG)13 repeat PABPN1 leads to weakness and coordination defects in mice. Dion, P., Shanmugam, V., Gaspar, C., Messaed, C., Meijer, I., Toulouse, A., Laganiere, J., Roussel, J., Rochefort, D., Laganiere, S., Allen, C., Karpati, G., Bouchard, J.P., Brais, B., Rouleau, G.A. Neurobiol. Dis. (2005) [Pubmed]
  4. Oculopharyngeal muscular dystrophy with PABPN1 mutation in a Chinese Malaysian woman. Goh, K.J., Wong, K.T., Nishino, I., Minami, N., Nonaka, I. Neuromuscul. Disord. (2005) [Pubmed]
  5. Involvement of the ubiquitin-proteasome pathway and molecular chaperones in oculopharyngeal muscular dystrophy. Abu-Baker, A., Messaed, C., Laganiere, J., Gaspar, C., Brais, B., Rouleau, G.A. Hum. Mol. Genet. (2003) [Pubmed]
  6. Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy. Brais, B., Bouchard, J.P., Xie, Y.G., Rochefort, D.L., Chrétien, N., Tomé, F.M., Lafrenière, R.G., Rommens, J.M., Uyama, E., Nohira, O., Blumen, S., Korczyn, A.D., Heutink, P., Mathieu, J., Duranceau, A., Codère, F., Fardeau, M., Rouleau, G.A., Korcyn, A.D. Nat. Genet. (1998) [Pubmed]
  7. Nonsense-mediated mRNA decay: splicing, translation and mRNP dynamics. Maquat, L.E. Nat. Rev. Mol. Cell Biol. (2004) [Pubmed]
  8. The other trinucleotide repeat: polyalanine expansion disorders. Albrecht, A., Mundlos, S. Curr. Opin. Genet. Dev. (2005) [Pubmed]
  9. Trehalose reduces aggregate formation and delays pathology in a transgenic mouse model of oculopharyngeal muscular dystrophy. Davies, J.E., Sarkar, S., Rubinsztein, D.C. Hum. Mol. Genet. (2006) [Pubmed]
  10. Nuclear inclusions in oculopharyngeal muscular dystrophy consist of poly(A) binding protein 2 aggregates which sequester poly(A) RNA. Calado, A., Tomé, F.M., Brais, B., Rouleau, G.A., Kühn, U., Wahle, E., Carmo-Fonseca, M. Hum. Mol. Genet. (2000) [Pubmed]
  11. Evidence that poly(A) binding protein C1 binds nuclear pre-mRNA poly(A) tails. Hosoda, N., Lejeune, F., Maquat, L.E. Mol. Cell. Biol. (2006) [Pubmed]
  12. Induction of HSP70 expression and recruitment of HSC70 and HSP70 in the nucleus reduce aggregation of a polyalanine expansion mutant of PABPN1 in HeLa cells. Wang, Q., Mosser, D.D., Bag, J. Hum. Mol. Genet. (2005) [Pubmed]
  13. Cytoplasmic targeting of mutant poly(A)-binding protein nuclear 1 suppresses protein aggregation and toxicity in oculopharyngeal muscular dystrophy. Abu-Baker, A., Laganiere, S., Fan, X., Laganiere, J., Brais, B., Rouleau, G.A. Traffic (2005) [Pubmed]
  14. Genetic heterogeneity in 30 German patients with oculopharyngeal muscular dystrophy. Müller, T., Deschauer, M., Kolbe-Fehr, F., Zierz, S. J. Neurol. (2006) [Pubmed]
  15. The product of an oculopharyngeal muscular dystrophy gene, poly(A)-binding protein 2, interacts with SKIP and stimulates muscle-specific gene expression. Kim, Y.J., Noguchi, S., Hayashi, Y.K., Tsukahara, T., Shimizu, T., Arahata, K. Hum. Mol. Genet. (2001) [Pubmed]
  16. Prevention of oculopharyngeal muscular dystrophy-associated aggregation of nuclear polyA-binding protein with a single-domain intracellular antibody. Verheesen, P., de Kluijver, A., van Koningsbruggen, S., de Brij, M., de Haard, H.J., van Ommen, G.J., van der Maarel, S.M., Verrips, C.T. Hum. Mol. Genet. (2006) [Pubmed]
  17. Nuclear poly(A)-binding protein PABPN1 is associated with RNA polymerase II during transcription and accompanies the released transcript to the nuclear pore. Bear, D.G., Fomproix, N., Soop, T., Björkroth, B., Masich, S., Daneholt, B. Exp. Cell Res. (2003) [Pubmed]
  18. Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3'-end processing machinery. Chen, Z., Li, Y., Krug, R.M. EMBO J. (1999) [Pubmed]
  19. Effect of oculopharyngeal muscular dystrophy-associated extension of seven alanines on the fibrillation properties of the N-terminal domain of PABPN1. Lodderstedt, G., Hess, S., Hause, G., Scheuermann, T., Scheibel, T., Schwarz, E. FEBS J. (2007) [Pubmed]
  20. Structure and function of poly(A) binding proteins. Kühn, U., Wahle, E. Biochim. Biophys. Acta (2004) [Pubmed]
  21. FRG1P-mediated aggregation of proteins involved in pre-mRNA processing. van Koningsbruggen, S., Straasheijm, K.R., Sterrenburg, E., de Graaf, N., Dauwerse, H.G., Frants, R.R., van der Maarel, S.M. Chromosoma (2007) [Pubmed]
  22. A de novo PABPN1 germline mutation in a patient with oculopharyngeal muscular dystrophy. Gürtler, N., Plasilova, M., Podvinec, M., Boesch, N., Müller, H., Heinimann, K. Laryngoscope (2006) [Pubmed]
  23. Oculopharyngeal muscular dystrophy: a point mutation which mimics the effect of the PABPN1 gene triplet repeat expansion mutation. Robinson, D.O., Wills, A.J., Hammans, S.R., Read, S.P., Sillibourne, J. J. Med. Genet. (2006) [Pubmed]
  24. Animal model of oculopharyngeal muscular dystrophy. Uyama, E., Hino, H., Araki, K., Takeya, M., Uchino, M., Yamamura, K. Acta myologica : myopathies and cardiomyopathies : official journal of the Mediterranean Society of Myology / edited by the Gaetano Conte Academy for the study of striated muscle diseases. (2005) [Pubmed]
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