Control of mRNA stability contributes to low levels of nuclear poly(A) binding protein 1 (PABPN1) in skeletal muscle

Skeletal Muscle

Volumn 3, Issue 1, 2013, Pages

  Apponi, Luciano H ^a   Corbett, Anita H ^a   Pavlath, Grace K ^a  

^a EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Muscular dystrophy; OPMD; PABPN1; Polyalanine expansion; Skeletal muscle

Indexed keywords

MUS;

EID: 84884770981     PISSN: None     EISSN: 20445040     Source Type: Journal    
DOI: 10.1186/2044-5040-3-23     Document Type: Article

References (43)

1. Keene JD. RNA regulons: coordination of post-transcriptional events. Nat Rev Genet 2007, 8:533-543. 10.1038/nrg2111, 17572691.
2. Kuhn U, Wahle E. Structure and function of poly(A) binding proteins. Biochim Biophys Acta 2004, 1678:67-84. 10.1016/j.bbaexp.2004.03.008, 15157733.
3. Kerwitz Y, Kuhn U, Lilie H, Knoth A, Scheuermann T, Friedrich H, Schwarz E, Wahle E. Stimulation of poly(A) polymerase through a direct interaction with the nuclear poly(A) binding protein allosterically regulated by RNA. EMBO J 2003, 22:3705-3714. 10.1093/emboj/cdg347, 165617, 12853485.
4. Kuhn U, Gundel M, Knoth A, Kerwitz Y, Rudel S, Wahle E. Poly(A) tail length is controlled by the nuclear poly(A)-binding protein regulating the interaction between poly(A) polymerase and the cleavage and polyadenylation specificity factor. J Biol Chem 2009, 284:22803-22814. 10.1074/jbc.M109.018226, 2755688, 19509282.
5. Jenal M, Elkon R, Loayza-Puch F, van Haaften G, Kühn U, Menzies FM, Oude Vrielink JA, Bos AJ, Drost J, Rooijers K, Rubinsztein DC, Agami R. The poly(A)-binding protein nuclear 1 suppresses alternative cleavage and polyadenylation sites. Cell 2012, 149:538-553. 10.1016/j.cell.2012.03.022, 22502866.
6. Lutz CS, Moreira A. Alternative mRNA polyadenylation in eukaryotes: an effective regulator of gene expression. Wiley Interdiscip Rev RNA 2011, 2:22-31.
7. Beaulieu YB, Kleinman CL, Landry-Voyer AM, Majewski J, Bachand F. Polyadenylation-dependent control of long noncoding RNA expression by the poly(A)-binding protein nuclear 1. PLoS Genet 2012, 8:e1003078. 10.1371/journal.pgen.1003078, 3499365, 23166521.
8. Brais B, Bouchard JP, Xie YG, Rochefort DL, Chrétien N, Tomé FM, Lafrenière RG, Rommens JM, Uyama E, Nohira O, Blumen S, Korczyn AD, Heutink P, Mathieu J, Duranceau A, Codère F, Fardeau M, Rouleau GA. Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy. Nat Genet 1998, 18:164-167. 10.1038/ng0298-164, 9462747.
9. Victor M, Hayes R, Adams RD. Oculopharyngeal muscular dystrophy. A familial disease of late life characterized by dysphagia and progressive ptosis of the evelids. N Engl J Med 1962, 267:1267-1272. 10.1056/NEJM196212202672501, 13997067.
10. Ruegg S, Lehky Hagen M, Hohl U, Kappos L, Fuhr P, Plasilov M, Muller H, Heinimann K. Oculopharyngeal muscular dystrophy - an under-diagnosed disorder?. Swiss Med Wkly 2005, 135:574-586.
11. Van Der Sluijs BM, Hoefsloot LH, Padberg GW, Van Der Maarel SM, Van Engelen BG. Oculopharyngeal muscular dystrophy with limb girdle weakness as major complaint. J Neurol 2003, 250:1307-1312. 10.1007/s00415-003-0201-6, 14648146.
12. Abu-Baker A, Rouleau GA. Oculopharyngeal muscular dystrophy: recent advances in the understanding of the molecular pathogenic mechanisms and treatment strategies. Biochim Biophys Acta 2007, 1772:173-185. 10.1016/j.bbadis.2006.10.003, 17110089.
13. Tome FM, Fardeau M. Nuclear inclusions in oculopharyngeal dystrophy. Acta Neuropathol 1980, 49:85-87. 10.1007/BF00692226, 6243839.
14. Tome FM, Chateau D, Helbling-Leclerc A, Fardeau M. Morphological changes in muscle fibers in oculopharyngeal muscular dystrophy. Neuromuscul Disord 1997, 7(Suppl 1):S63-S69.
15. Banerjee A, Apponi LH, Pavlath GK, Corbett AH. PABPN1: Molecular function and muscle disease. FEBS J 2013, 280:4230-4250. 10.1111/febs.12294, 23601051.
16. Apponi LH, Leung SW, Williams KR, Valentini SR, Corbett AH, Pavlath GK. Loss of nuclear poly(A)-binding protein 1 causes defects in myogenesis and mRNA biogenesis. Hum Mol Genet 2010, 19:1058-1065. 10.1093/hmg/ddp569, 2830829, 20035013.
17. O'Connor RS, Mills ST, Jones KA, Ho SN, Pavlath GK. A combinatorial role for NFAT5 in both myoblast migration and differentiation during skeletal muscle myogenesis. J Cell Sci 2007, 120:149-159.
18. Bondesen BA, Mills ST, Kegley KM, Pavlath GK. The COX-2 pathway is essential during early stages of skeletal muscle regeneration. Am J Physiol Cell Physiol 2004, 287:C475-C483. 10.1152/ajpcell.00088.2004, 15084473.
19. Ausubel FM, Brent R, Kingston ER, Moore DD, Seidman JG, Smith JA, Struhl K. Current Protocols in Molecular Biology 2001, New York, NY: John Wiley and Sons.
20. Workman JL, Kingston RE. Alteration of nucleosome structure as a mechanism of transcriptional regulation. Ann Rev Biochem 1998, 67:545-579. 10.1146/annurev.biochem.67.1.545, 9759497.
21. Csermely P, Schnaider T, Soti C, Prohaszka Z, Nardai G. The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol Ther 1998, 79:129-168. 10.1016/S0163-7258(98)00013-8, 9749880.
22. Nemeth A, Krause S, Blank D, Jenny A, Jeno P, Lustig A, Wahle E. Isolation of genomic and cDNA clones encoding bovine poly(A) binding protein II. Nucleic Acids Res 1995, 23:4034-4041. 10.1093/nar/23.20.4034, 307339, 7479061.
23. Lee YJ, Lee J, Yang IC, Hahn Y, Lee Y, Chung JH. Genomic structure and expression of murine poly(A) binding protein II gene. Biochim Biophys Acta 1998, 1395:40-46. 10.1016/S0167-4781(97)00147-4, 9434149.
24. Lai RY, Ljubicic V, D'Souza D, Hood DA. Effect of chronic contractile activity on mRNA stability in skeletal muscle. Am J Physiol Cell Physiol 2010, 299:C155-C163. 10.1152/ajpcell.00523.2009, 2904257, 20375275.
25. Zhang L, Lee JE, Wilusz J, Wilusz CJ. The RNA-binding protein CUGBP1 regulates stability of tumor necrosis factor mRNA in muscle cells: implications for myotonic dystrophy. J Biol Chem 2008, 283:22457-22463. 10.1074/jbc.M802803200, 2504872, 18559347.
26. Lee JE, Lee JY, Wilusz J, Tian B, Wilusz CJ. Systematic analysis of cis-elements in unstable mRNAs demonstrates that CUGBP1 is a key regulator of mRNA decay in muscle cells. PloS One 2010, 5:e11201. 10.1371/journal.pone.0011201, 2888570, 20574513.
27. Thorrez L, Van Deun K, Tranchevent LC, Van Lommel L, Engelen K, Marchal K, Moreau Y, Van Mechelen I, Schuit F. Using ribosomal protein genes as reference: a tale of caution. PloS One 2008, 3:e1854. 10.1371/journal.pone.0001854, 2267211, 18365009.
28. Hsiao LL, Dangond F, Yoshida T, Hong R, Jensen RV, Misra J, Dillon W, Lee KF, Clark KE, Haverty P, Weng Z, Mutter GL, Frosch MP, MacDonald ME, Milford EL, Crum CP, Bueno R, Pratt RE, Mahadevappa M, Warrington JA, Stephanopoulos G, Stephanopoulos G, Gullans SR. A compendium of gene expression in normal human tissues. Physiol Genomics 2001, 7:97-104.
29. Welle S, Bhatt K, Thornton CA. Inventory of high-abundance mRNAs in skeletal muscle of normal men. Genome Res 1999, 9:506-513. 310786, 10330131.
30. Ramskold D, Wang ET, Burge CB, Sandberg R. An abundance of ubiquitously expressed genes revealed by tissue transcriptome sequence data. PLoS Comp Biol 2009, 5:e1000598.
31. Schwanhausser B, Busse D, Li N, Dittmar G, Schuchhardt J, Wolf J, Chen W, Selbach M. Global quantification of mammalian gene expression control. Nature 2011, 473:337-342. 10.1038/nature10098, 21593866.
32. Gingerich TJ, Feige JJ, LaMarre J. AU-rich elements and the control of gene expression through regulated mRNA stability. Anim Health Res Rev 2004, 5:49-63. 10.1079/AHR200460, 15460540.
33. Wilusz CJ, Wilusz J. Bringing the role of mRNA decay in the control of gene expression into focus. Trends Genet 2004, 20:491-497. 10.1016/j.tig.2004.07.011, 15363903.
34. Garneau NL, Wilusz J, Wilusz CJ. The highways and byways of mRNA decay. Nat Rev Mol Cell Biol 2007, 8:113-126. 10.1038/nrm2104, 17245413.
35. Barreau C, Paillard L, Osborne HB. AU-rich elements and associated factors: are there unifying principles?. Nucleic Acids Res 2005, 33:7138-7150. 10.1093/nar/gki1012, 1325018, 16391004.
36. Zoghbi HY, Orr HT. Polyglutamine diseases: protein cleavage and aggregation. Curr Opin Neurobiol 1999, 9:566-570. 10.1016/S0959-4388(99)00013-6, 10508741.
37. Nasrallah IM, Minarcik JC, Golden JA. A polyalanine tract expansion in Arx forms intranuclear inclusions and results in increased cell death. J Cell Biol 2004, 167:411-416. 10.1083/jcb.200408091, 2172475, 15533998.
38. Caburet S, Demarez A, Moumne L, Fellous M, De Baere E, Veitia RA. A recurrent polyalanine expansion in the transcription factor FOXL2 induces extensive nuclear and cytoplasmic protein aggregation. J Med Genet 2004, 41:932-936. 10.1136/jmg.2004.024356, 1735658, 15591279.
39. Winter R, Liebold J, Schwarz E. The unresolved puzzle why alanine extensions cause disease. Biol Chem 2013, 394:951-963.
40. Berciano MT, Villagra NT, Ojeda JL, Navascues J, Gomes A, Lafarga M, Carmo-Fonseca M. Oculopharyngeal muscular dystrophy-like nuclear inclusions are present in normal magnocellular neurosecretory neurons of the hypothalamus. Hum Mol Genet 2004, 13:829-838. 10.1093/hmg/ddh101, 14976164.
41. Anvar SY, Raz Y, Verway N, van der Sluijs B, Venema A, Goeman JJ, Vissing J, van der Maarel SM, t Hoen PA, van Engelen BG, Raz V. A decline in PABPN1 induces progressive muscle weakness in oculopharyngeal muscle dystrophy and in muscle aging. Aging 2013, 5:412-426.
42. Davies JE, Sarkar S, Rubinsztein DC. Wild-type PABPN1 is anti-apoptotic and reduces toxicity of the oculopharyngeal muscular dystrophy mutation. Hum Mol Genet 2008, 17:1097-1108. 10.1093/hmg/ddm382, 18178579.