Implications of the prion-related Q/N domains in TDP-43 and FUS

References

• Charcot JM, Joffroy A. Deux cas d'atrophie musculaire progressive avec les lesions de la substance grise et faiscaux anterolateraux de la moelle epiniere. Archives de Physiologic Normale et Pathologique 1869; 2:354 - 367
   Google Scholar
• Gowers WR. A manual of diseases of the nervous system 1886; London Churchill
   Google Scholar
• Ravits J, Laurie P, Fan Y, Moore DH. Implications of ALS focality: rostral-caudal distribution of lower motor neuron loss postmortem. Neurology 2007; 68:1576 - 1582
   PubMed Web of Science ®Google Scholar
• Ravits JM, La Spada AR. ALS motor phenotype heterogeneity, focality and spread: deconstructing motor neuron degeneration. Neurology 2009; 73:805 - 811
   PubMed Web of Science ®Google Scholar
• Neumann M, Sampathu DM, Kwong LK, Truax AC, Micsenyi MC, Chou TT, et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 2006; 314:130 - 133
   PubMed Web of Science ®Google Scholar
• Gitcho MA, Baloh RH, Chakraverty S, Mayo K, Norton JB, Levitch D, et al. TDP-43 A315T mutation in familial motor neuron disease. Ann Neurol 2008; 63:535 - 538
   PubMed Web of Science ®Google Scholar
• Yokoseki A, Shiga A, Tan CF, Tagawa A, Kaneko H, Koyama A, et al. TDP-43 mutation in familial amyotrophic lateral sclerosis. Ann Neurol 2008; 63:538 - 542
   PubMed Web of Science ®Google Scholar
• Sreedharan J, Blair IP, Tripathi VB, Hu X, Vance C, Rogelj B, et al. TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 2008; 319:1668 - 1672
   PubMed Web of Science ®Google Scholar
• Van Deerlin VM, Leverenz JB, Bekris LM, Bird TD, Yuan W, Elman LB, et al. TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis. Lancet Neurol 2008; 7:409 - 416
   PubMed Web of Science ®Google Scholar
• Kabashi E, Valdmanis PN, Dion P, Spiegelman D, McConkey BJ, Vande Velde C, et al. TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis. Nat Genet 2008; 40:572 - 574
   PubMed Web of Science ®Google Scholar
• Kwiatkowski TJ Jr, Bosco DA, Leclerc AL, Tamrazian E, Vanderburg CR, Russ C, et al. Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 2009; 323:1205 - 1208
   PubMed Web of Science ®Google Scholar
• Vance C, Rogelj B, Hortobagyi T, De Vos KJ, Nishimura AL, Sreedharan J, et al. Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science 2009; 323:1208 - 1211
   PubMed Web of Science ®Google Scholar
• Doi H, Okamura K, Bauer PO, Furukawa Y, Shimizu H, Kurosawa M, et al. RNA-binding protein TLS is a major nuclear aggregate-interacting protein in huntingtin exon 1 with expanded polyglutamine-expressing cells. J Biol Chem 2008; 283:6489 - 6500
   PubMed Web of Science ®Google Scholar
• Fuentealba RA, Udan M, Bell S, Wegorzewska I, Shao J, Diamond MI, et al. Interaction with polyglutamine aggregates reveals a Q/N rich domain in TDP-43. J Biol Chem 2010; 285:26304 - 26314
   PubMed Web of Science ®Google Scholar
• Cushman M, Johnson BS, King OD, Gitler AD, Shorter J. Prion-like disorders: blurring the divide between transmissibility and infectivity. J Cell Sci 2010; 123:1191 - 1201
   PubMed Web of Science ®Google Scholar
• Griffith JS. Self-replication and scrapie. Nature 1967; 215:1043 - 1044
   PubMed Web of Science ®Google Scholar
• Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216:136 - 144
   PubMed Web of Science ®Google Scholar
• Wickner RB, Edskes HK, Roberts BT, Baxa U, Pierce MM, Ross ED, et al. Prions: proteins as genes and infectious entities. Genes Dev 2004; 18:470 - 485
   Google Scholar
• Halfmann R, Alberti S, Lindquist S. Prions, protein homeostasis and phenotypic diversity. Trends Cell Biol 2010; 20:125 - 133
   PubMed Web of Science ®Google Scholar
• Wickner RB, Shewmaker F, Kryndushkin D, Edskes HK. Protein inheritance (prions) based on parallel in-register beta-sheet amyloid structures. Bioessays 2008; 30:955 - 964
   PubMed Web of Science ®Google Scholar
• Tyedmers J, Madariaga ML, Lindquist S. Prion switching in response to environmental stress. PLoS Biol 2008; 6:294
   PubMed Web of Science ®Google Scholar
• Michelitsch MD, Weissman JS. A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions. Proc Natl Acad Sci USA 2000; 97:11910 - 11915
   PubMed Web of Science ®Google Scholar
• Alberti S, Halfmann R, King O, Kapila A, Lindquist S. A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 2009; 137:146 - 158
   PubMed Web of Science ®Google Scholar
• Si K, Lindquist S, Kandel ER. A neuronal isoform of the aplysia CPEB has prion-like properties. Cell 2003; 115:879 - 891
   PubMed Web of Science ®Google Scholar
• Salazar AM, Silverman EJ, Menon KP, Zinn K. Regulation of synaptic Pumilio function by an aggregation-prone domain. J Neurosci 2010; 30:515 - 522
   Google Scholar
• Harrison PM, Gerstein M. A method to assess compositional bias in biological sequences and its application to prion-like glutamine/asparagine-rich domains in eukaryotic proteomes. Genome Biol 2003; 4:40
   PubMed Web of Science ®Google Scholar
• Anderson P, Kedersha N. RNA granules: post-transcriptional and epigenetic modulators of gene expression. Nat Rev Mol Cell Biol 2009; 10:430 - 436
   PubMed Web of Science ®Google Scholar
• Gilks N, Kedersha N, Ayodele M, Shen L, Stoecklin G, Dember LM, et al. Stress granule assembly is mediated by prion-like aggregation of TIA-1. Mol Biol Cell 2004; 15:5383 - 5398
   PubMed Web of Science ®Google Scholar
• Reijns MA, Alexander RD, Spiller MP, Beggs JD. A role for Q/N-rich aggregation-prone regions in P-body localization. J Cell Sci 2008; 121:2463 - 2472
   PubMed Web of Science ®Google Scholar
• He Y, Smith R. Nuclear functions of heterogeneous nuclear ribonucleoproteins A/B. Cell Mol Life Sci 2009; 66:1239 - 1256
   PubMed Web of Science ®Google Scholar
• Ou SH, Wu F, Harrich D, Garcia-Martinez LF, Gaynor RB. Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs. J Virol 1995; 69:3584 - 3596
   PubMed Web of Science ®Google Scholar
• Pesiridis GS, Lee VM, Trojanowski JQ. Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis. Hum Mol Genet 2009; 18:156 - 162
   PubMed Web of Science ®Google Scholar
• Buratti E, Baralle FE. Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9. J Biol Chem 2001; 276:36337 - 36343
   PubMed Web of Science ®Google Scholar
• Winton MJ, Igaz LM, Wong MM, Kwong LK, Trojanowski JQ, Lee VM. Disturbance of nuclear and cytoplasmic Tar DNA binding protein (TDP-43) induces disease-like redistribution, sequestration and aggregate formation. J Biol Chem 2008; 19:13302 - 13309
   Web of Science ®Google Scholar
• Buratti E, Brindisi A, Giombi M, Tisminetzky S, Ayala YM, Baralle FE. TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: an important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing. J Biol Chem 2005; 280:37572 - 37584
   PubMed Web of Science ®Google Scholar
• Ayala YM, Pantano S, D'Ambrogio A, Buratti E, Brindisi A, Marchetti C, et al. Human, Drosophila and C. elegans TDP43: nucleic acid binding properties and splicing regulatory function. J Mol Biol 2005; 348:575 - 588
   PubMed Web of Science ®Google Scholar
• Abhyankar MM, Urekar C, Reddi PP. A novel CpG-free vertebrate insulator silences the testis-specific SP-10 gene in somatic tissues: role for TDP-43 in insulator function. J Biol Chem 2007; 282:36143 - 36154
   PubMed Web of Science ®Google Scholar
• Yamanaka T, Miyazaki H, Oyama F, Kurosawa M, Washizu C, Doi H, et al. Mutant Huntingtin reduces HSP70 expression through the sequestration of NF-Y transcription factor. EMBO J 2008; 27:827 - 839
   PubMed Web of Science ®Google Scholar
• Furukawa Y, Kaneko K, Matsumoto G, Kurosawa M, Nukina N. Cross-seeding fibrillation of Q/N-rich proteins offers new pathomechanism of polyglutamine diseases. J Neurosci 2009; 29:5153 - 5162
   Google Scholar
• Johnson BS, Snead D, Lee JJ, McCaffery JM, Shorter J, Gitler AD. TDP-43 is intrinsically aggregation-prone and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity. J Biol Chem 2009; 284:20329 - 20339
   PubMed Web of Science ®Google Scholar
• Johnson BS, McCaffery JM, Lindquist S, Gitler AD. A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity. Proc Natl Acad Sci USA 2008; 105:6439 - 6444
   PubMed Web of Science ®Google Scholar
• Igaz LM, Kwong LK, Chen-Plotkin A, Winton MJ, Unger TL, Xu Y, et al. Expression of TDP-43 C-terminal fragments in vitro recapitulates pathological features of TDP-43 proteinopathies. J Biol Chem 2009; 284:8516 - 8524
   PubMed Web of Science ®Google Scholar
• Zhang YJ, Xu YF, Cook C, Gendron TF, Roettges P, Link CD, et al. Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity. Proc Natl Acad Sci USA 2009; 106:7607 - 7612
   PubMed Web of Science ®Google Scholar
• Andersson MK, Stahlberg A, Arvidsson Y, Olofsson A, Semb H, Stenman G, et al. The multifunctional FUS, EWS and TAF15 proto-oncoproteins show cell type-specific expression patterns and involvement in cell spreading and stress response. BMC Cell Biol 2008; 9:37
   PubMed Web of Science ®Google Scholar
• Colombrita C, Zennaro E, Fallini C, Weber M, Sommacal A, Buratti E, et al. TDP-43 is recruited to stress granules in conditions of oxidative insult. J Neurochem 2009; 111:1051 - 1061
   PubMed Web of Science ®Google Scholar
• Freibaum BD, High AA, Chitta R, Taylor JP. Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery. J Proteome Res 2010; 9:1104 - 1120
   PubMed Web of Science ®Google Scholar
• Dormann D, Rodde R, Edbauer D, Bentmann E, Fischer I, Hruscha A, et al. ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import. EMBO J 2010; 29:2841 - 2857
   PubMed Web of Science ®Google Scholar
• Gal J, Zhang J, Kwinter DM, Zhai J, Jia H, Jia J, et al. Nuclear localization sequence of FUS and induction of stress granules by ALS mutants. Neurobiol Aging 2010; In press
   PubMed Web of Science ®Google Scholar
• Bosco DA, Lemay N, Ko HK, Zhou H, Burke C, Kwiatkowski TJ Jr, et al. Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules. Hum Mol Genet 2010; 19:4160 - 4175
   PubMed Web of Science ®Google Scholar
• D'Ambrogio A, Buratti E, Stuani C, Guarnaccia C, Romano M, Ayala YM, et al. Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo. Nucleic Acids Res 2009; 37:4116 - 4126
   PubMed Web of Science ®Google Scholar
• Josephs KA, Whitwell JL, Knopman DS, Hu WT, Stroh DA, Baker M, et al. Abnormal TDP-43 immunoreactivity in AD modifies clinicopathologic and radiologic phenotype. Neurology 2008; 70:1850 - 1857
   PubMed Web of Science ®Google Scholar
• Nakashima-Yasuda H, Uryu K, Robinson J, Xie SX, Hurtig H, Duda JE, et al. Co-morbidity of TDP-43 proteinopathy in Lewy body related diseases. Acta Neuropathol 2007; 114:221 - 229
   PubMed Web of Science ®Google Scholar
• King A, Sweeney F, Bodi I, Troakes C, Maekawa S, Al-Sarraj S. Abnormal TDP-43 expression is identified in the neocortex in cases of dementia pugilistica, but is mainly confined to the limbic system when identified in high and moderate stages of Alzheimer's disease. Neuropathology 2010; 30:408 - 419
   PubMed Web of Science ®Google Scholar
• Weihl CC, Temiz P, Miller SE, Watts G, Smith C, Forman M, et al. TDP-43 accumulation in inclusion body myopathy muscle suggests a common pathogenic mechanism with frontotemporal dementia. J Neurol Neurosurg Psychiatry 2008; 79:1186 - 1189
   PubMed Web of Science ®Google Scholar
• Elden AC, Kim HJ, Hart MP, Chen-Plotkin AS, Johnson BS, Fang X, et al. Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS. Nature 2010; 466:1069 - 1075
   PubMed Web of Science ®Google Scholar
• Frost B, Diamond MI. Prion-like mechanisms in neurodegenerative diseases. Nat Rev Neurosci 2010; 11:155 - 159
   PubMed Web of Science ®Google Scholar
• Brundin P, Melki R, Kopito R. Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat Rev Mol Cell Biol 2010; 11:301 - 307
   PubMed Web of Science ®Google Scholar