Welander distal myopathy is caused by a mutation in the RNA-binding protein TIA1

Annals of Neurology

Volumn 73, Issue 4, 2013, Pages 500-509

  Hackman, Peter ^a   Sarparanta, Jaakko ^a   Lehtinen, Sara ^a   Vihola, Anna ^a   Evilä, Anni ^a   Jonson, Per Harald ^a   Luque, Helena ^a   Kere, Juha ^a,b   Screen, Mark ^a   Chinnery, Patrick F ^c   Åhlberg, Gabrielle ^d   Edström, Lars ^d   Udd, Bjarne ^a,e,f  

^a UNIVERSITY OF HELSINKI   (Finland)

^b KAROLINSKA INSTITUTE   (Sweden)

^c NEWCASTLE UNIVERSITY   (United Kingdom)

^d KAROLINSKA UNIVERSITY HOSPITAL   (Sweden)

^e VAASA CENTRAL HOSPITAL   (Finland)

^f TAMPERE UNIVERSITY HOSPITAL   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; RNA BINDING PROTEIN; RNA BINDING PROTEIN TIA1; UNCLASSIFIED DRUG;

ARTICLE; AUTOSOMAL DOMINANT DISORDER; CELL CULTURE; CELL GRANULE; CELL STRESS; CONTENT ANALYSIS; CONTROLLED STUDY; CYTOLOGY; DISTAL MYOPATHY; FLUORESCENCE RECOVERY AFTER PHOTOBLEACHING; GENE MUTATION; GENE SEQUENCE; GENE TARGETING; GENETIC LINKAGE; GENETIC TRANSCRIPTION; GENOME; HAPLOTYPE; HELA CELL; HIGH THROUGHPUT SEQUENCING; HUMAN; HUMAN CELL; HUMAN TISSUE; IMMUNOFLUORESCENCE MICROSCOPY; MAJOR CLINICAL STUDY; MICROSATELLITE MARKER; MUSCLE BIOPSY; MUTANT; MYOBLAST; PATHOPHYSIOLOGY; PRIORITY JOURNAL; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; RNA ISOLATION; RNA SPLICING; SANGER SEQUENCING; SINGLE NUCLEOTIDE POLYMORPHISM; WELANDER DISTAL MYOPATHY; WESTERN BLOTTING;

CELLS, CULTURED; DISTAL MYOPATHIES; FEMALE; FLUORESCENCE RECOVERY AFTER PHOTOBLEACHING; GENETIC LINKAGE; GENETIC PREDISPOSITION TO DISEASE; GENOTYPE; GREEN FLUORESCENT PROTEINS; HELA CELLS; HUMANS; MALE; MICROSATELLITE REPEATS; MUSCLE, SKELETAL; MUTATION; PHOTOBLEACHING; POLY(A)-BINDING PROTEINS; POLYMORPHISM, SINGLE NUCLEOTIDE; PROTEINS; UBIQUITIN;

EID: 84878423714     PISSN: 03645134     EISSN: 15318249     Source Type: Journal    
DOI: 10.1002/ana.23831     Document Type: Article

References (45)

1. Welander L,. Myopathia distalis tarda hereditaria; 249 examined cases in 72 pedigrees. Acta Med Scand Suppl 1951; 265: 1-124.
2. von Tell D, Somer H, Udd B, et al. Welander distal myopathy outside the swedish population: phenotype and genotype. Neuromuscul Disord 2002; 12: 544-547.
3. Åhlberg G, Borg K, Edström L, Anvret M,. Welander hereditary distal myopathy, a molecular genetic comparison to hereditary myopathies with inclusion bodies. Neuromuscul Disord 1998; 8: 111-114.
4. Borg K, Åhlberg G, Anvret M, Edström L,. Welander distal myopathy-an overview. Neuromuscul Disord 1998; 8: 115-118.
5. Edström L,. Histochemical and histopathological changes in skeletal muscle in late-onset hereditary distal myopathy (Welander). J Neurol Sci 1975; 26: 147-157.
6. Borg K, Åhlberg G, Borg J, Edström L,. Welander's distal myopathy: clinical, neurophysiological and muscle biopsy observations in young and middle aged adults with early symptoms. J Neurol Neurosurg Psychiatry 1991; 54: 494-498.
7. Åhlberg G, von Tell D, Borg K, et al. Genetic linkage of Welander distal myopathy to chromosome 2p13. Ann Neurol 1999; 46: 399-404.
8. von Tell D, Bruder CE, Anderson LV, et al. Refined mapping of the Welander distal myopathy region on chromosome 2p13 positions the new candidate region telomeric of the DYSF locus. Neurogenetics 2003; 4: 173-177.
9. Kedersha NL, Gupta M, Li W, et al. RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules. J Cell Biol 1999; 147: 1431-1442.
10. Del Gatto-Konczak F, Bourgeois CF, Le Guiner C, et al. The RNA-binding protein TIA-1 is a novel mammalian splicing regulator acting through intron sequences adjacent to a 5′ splice site. Mol Cell Biol 2000; 20: 6287-6299.
11. Förch P, Puig O, Kedersha N, et al. The apoptosis-promoting factor TIA-1 is a regulator of alternative pre-mRNA splicing. Mol Cell 2000; 6: 1089-1098.
12. Piecyk M, Wax S, Beck AR, et al. TIA-1 is a translational silencer that selectively regulates the expression of TNF-alpha. EMBO J 2000; 19: 4154-4163.
13. Aznarez I, Barash Y, Shai O, et al. A systematic analysis of intronic sequences downstream of 5′ splice sites reveals a widespread role for U-rich motifs and TIA1/TIAL1 proteins in alternative splicing regulation. Genome Res 2008; 18: 1247-1258.
14. Damgaard CK, Lykke-Andersen J,. Translational coregulation of 5′TOP mRNAs by TIA-1 and TIAR. Genes Dev 2011; 25: 2057-2068.
15. Kedersha N, Cho MR, Li W, et al. Dynamic shuttling of TIA-1 accompanies the recruitment of mRNA to mammalian stress granules. J Cell Biol 2000; 151: 1257-1268.
16. Gilks N, Kedersha N, Ayodele M, et al. Stress granule assembly is mediated by prion-like aggregation of TIA-1. Mol Biol Cell 2004; 15: 5383-5398.
17. Anderson P, Nagler-Anderson C, O'Brien C, et al. A monoclonal antibody reactive with a 15-kDa cytoplasmic granule-associated protein defines a subpopulation of CD8+ T lymphocytes. J Immunol 1990; 144: 574-582.
18. Medley QG, Kedersha N, O'Brien S, et al. Characterization of GMP-17, a granule membrane protein that moves to the plasma membrane of natural killer cells following target cell recognition. Proc Natl Acad Sci U S A 1996; 93: 685-689.
19. Izquierdo JM, Valcárcel J,. Two isoforms of the T-cell intracellular antigen 1 (TIA-1) splicing factor display distinct splicing regulation activities: control of TIA-1 isoform ratio by TIA-1-related protein. J Biol Chem 2007; 282: 19410-19417.
20. Kang PB, Kho AT, Sanoudou D, et al. Variations in gene expression among different types of human skeletal muscle. Muscle Nerve 2005; 32: 483-491.
21. Kawakami A, Tian Q, Streuli M, et al. Intron-exon organization and chromosomal localization of the human TIA-1 gene. J Immunol 1994; 152: 4937-4945.
22. Beck AR, Medley QG, O'Brien S, et al. Structure, tissue distribution and genomic organization of the murine RRM-type RNA binding proteins TIA-1 and TIAR. Nucleic Acids Res 1996; 24: 3829-3835.
23. Li W, Li Y, Kedersha N, et al. Cell proteins TIA-1 and TIAR interact with the 3′ stem-loop of the West Nile virus complementary minus-strand RNA and facilitate virus replication. J Virol 2002; 76: 11989-12000.
24. Lõpez-Urrutia E, Valdés J, Bonilla-Moreno R, et al. A few nucleotide polymorphisms are sufficient to recruit nuclear factors differentially to the intron 1 of HPV-16 intratypic variants. Virus Res 2012; 166: 43-53.
25. Suzuki E, Tsutsumi A, Sugihara M, et al. Expression of TNF-alpha, tristetraprolin, T-cell intracellular antigen-1 and hu antigen R genes in synovium of patients with rheumatoid arthritis. Int J Mol Med 2006; 18: 273-278.
26. Vanderweyde T, Yu H, Varnum M, et al. Contrasting pathology of the stress granule proteins TIA-1 and G3BP in tauopathies. J Neurosci 2012; 32: 8270-8283.
27. White JP, Lloyd RE,. Poliovirus unlinks TIA1 aggregation and mRNA stress granule formation. J Virol 2011; 85: 12442-12454.
28. Tiainen M, Ylikorkala A, Mäkelä TP,. Growth suppression by Lkb1 is mediated by a G(1) cell cycle arrest. Proc Natl Acad Sci U S A 1999; 96: 9248-9251.
29. Schneider CA, Rasband WS, Eliceiri KW,. NIH image to ImageJ: 25 years of image analysis. Nat Methods 2012; 9: 671-675.
30. Zuccato E, Buratti E, Stuani C, et al. An intronic polypyrimidine-rich element downstream of the donor site modulates cystic fibrosis transmembrane conductance regulator exon 9 alternative splicing. J Biol Chem 2004; 279: 16980-16988.
31. Liu-Yesucevitz L, Bilgutay A, Zhang YJ, et al. Tar DNA binding protein-43 (TDP-43) associates with stress granules: analysis of cultured cells and pathological brain tissue. PLoS One 2010; 5: e13250.
32. Anderson P, Kedersha N,. Stress granules: the tao of RNA triage. Trends Biochem Sci 2008; 33: 141-150.
33. Förch P, Puig O, Martínez C, et al. The splicing regulator TIA-1 interacts with U1-C to promote U1 snRNP recruitment to 5′ splice sites. EMBO J 2002; 21: 6882-6892.
34. Izquierdo JM, Majõs N, Bonnal S, et al. Regulation of fas alternative splicing by antagonistic effects of TIA-1 and PTB on exon definition. Mol Cell 2005; 19: 475-484.
35. Le Guiner C, Lejeune F, Galiana D, et al. TIA-1 and TIAR activate splicing of alternative exons with weak 5′ splice sites followed by a U-rich stretch on their own pre-mRNAs. J Biol Chem 2001; 276: 40638-40646.
36. Sarparanta J, Jonson PH, Golzio C, et al. Mutations affecting the cytoplasmic functions of the co-chaperone DNAJB6 cause limb-girdle muscular dystrophy. Nat Genet 2012; 44: 450-455, S1-S2.
37. Harms MB, Sommerville RB, Allred P, et al. Exome sequencing reveals DNAJB6 mutations in dominantly-inherited myopathy. Ann Neurol 2012; 71: 407-416.
38. Castle JC, Zhang C, Shah JK, et al. Expression of 24,426 human alternative splicing events and predicted cis regulation in 48 tissues and cell lines. Nat Genet 2008; 40: 1416-1425.
39. Lee JE, Cooper TA,. Pathogenic mechanisms of myotonic dystrophy. Biochem Soc Trans 2009; 37 (pt 6): 1281-1286.
40. Johnson BS, Snead D, Lee JJ, et al. TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity. J Biol Chem 2009; 284: 20329-20339.
41. Sun Z, Diaz Z, Fang X, et al. Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS. PLoS Biol 2011; 9: e1000614.
42. Bonne G, Di Barletta MR, Varnous S, et al. Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy. Nat Genet 1999; 21: 285-288.
43. Bitoun M, Maugenre S, Jeannet PY, et al. Mutations in dynamin 2 cause dominant centronuclear myopathy. Nat Genet 2005; 37: 1207-1209.
44. Sreedharan J, Blair IP, Tripathi VB, et al. TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 2008; 319: 1668-1672.
45. Hofmann S, Cherkasova V, Bankhead P, et al. Translation suppression promotes stress granule formation and cell survival in response to cold shock. Mol Biol Cell 2012; 23: 3786-3800.