Profilin 1 mutants form aggregates that induce accumulation of prion-like TDP-43

REFERENCES

• Ayala YM, De Conti L, Avendano-Vazquez SE, Dhir A, Romano M, D'Ambrogio A, Tollervey J, Ule J, Baralle M, Buratti E, et al. TDP-43 regulates its mRNA levels through a negative feedback loop. EMBO J 2011; 30:277-88; PMID:21131904; http://dx.doi.org/10.1038/emboj.2010.310
   PubMed Web of Science ®Google Scholar
• Ayala YM, Zago P, D'Ambrogio A, Xu YF, Petrucelli L, Buratti E, Baralle FE. Structural determinants of the cellular localization and shuttling of TDP-43. J Cell Sci 2008; 121:3778-85; PMID:18957508; http://dx.doi.org/10.1242/jcs.038950
   PubMed Web of Science ®Google Scholar
• Buratti E, Baralle FE. Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease. Front Biosci 2008; 13:867-78; PMID:17981595; http://dx.doi.org/10.2741/2727
   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; 69:3584-96; PMID:7745706
   PubMed Web of Science ®Google Scholar
• Wang IF, Reddy NM, Shen CK. Higher order arrangement of the eukaryotic nuclear bodies. Proc Natl Acad Sci U S A 2002; 99:13583-8; PMID:12361981; http://dx.doi.org/10.1073/pnas.212483099
   PubMed Web of Science ®Google Scholar
• Ayala YM, Pantano S, D'Ambrogio A, Buratti E, Brindisi A, Marchetti C, Romano M, Baralle FE. Human, Drosophila, and C.elegans TDP43: nucleic acid binding properties and splicing regulatory function. J Mol Biol 2005; 348:575-88; PMID:15826655; http://dx.doi.org/10.1016/j.jmb.2005.02.038
   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; 276:36337-43; PMID:11470789; http://dx.doi.org/10.1074/jbc.M104236200
   PubMed 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; 280:37572-84; PMID:16157593; http://dx.doi.org/10.1074/jbc.M505557200
   PubMed Web of Science ®Google Scholar
• Wang IF, Wu LS, Shen CK. TDP-43: an emerging new player in neurodegenerative diseases. Trends Mol Med 2008; 14:479-85; PMID:18929508; http://dx.doi.org/10.1016/j.molmed.2008.09.001
   PubMed Web of Science ®Google Scholar
• Arai T, Hasegawa M, Akiyama H, Ikeda K, Nonaka T, Mori H, Mann D, Tsuchiya K, Yoshida M, Hashizume Y, et al. TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem Biophys Res Commun 2006; 351:602-11; PMID:17084815; http://dx.doi.org/10.1016/j.bbrc.2006.10.093
   PubMed Web of Science ®Google Scholar
• Neumann M, Sampathu DM, Kwong LK, Truax AC, Micsenyi MC, Chou TT, Bruce J, Schuck T, Grossman M, Clark CM, et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 2006; 314:130-3; PMID:17023659; http://dx.doi.org/10.1126/science.1134108
   PubMed Web of Science ®Google Scholar
• Hasegawa M, Arai T, Nonaka T, Kametani F, Yoshida M, Hashizume Y, Beach TG, Buratti E, Baralle F, Morita M, et al. Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Ann Neurol 2008; 64:60-70; PMID:18546284; http://dx.doi.org/10.1002/ana.21425
   PubMed Web of Science ®Google Scholar
• Lee EB, Lee VM, Trojanowski JQ. Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration. Nat Rev Neurosci 2012; 13:38-50
   Web of Science ®Google Scholar
• Kabashi E, Valdmanis PN, Dion P, Spiegelman D, McConkey BJ, Vande Velde C, Bouchard JP, Lacomblez L, Pochigaeva K, Salachas F, et al. TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis. Nat Genet 2008; 40:572-4; PMID:18372902; http://dx.doi.org/10.1038/ng.132
   PubMed Web of Science ®Google Scholar
• Sreedharan J, Blair IP, Tripathi VB, Hu X, Vance C, Rogelj B, Ackerley S, Durnall JC, Williams KL, Buratti E, et al. TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 2008; 319:1668-72; PMID:18309045; http://dx.doi.org/10.1126/science.1154584
   PubMed Web of Science ®Google Scholar
• Mackenzie IR, Rademakers R, Neumann M. TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia. Lancet Neurol 2010; 9:995-1007; PMID:20864052; http://dx.doi.org/10.1016/S1474-4422(10)70195-2
   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:R156-62; PMID:19808791; http://dx.doi.org/10.1093/hmg/ddp303
   PubMed Web of Science ®Google Scholar
• Guo W, Chen Y, Zhou X, Kar A, Ray P, Chen X, Rao EJ, Yang M, Ye H, Zhu L, et al. An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity. Nat Struct Mol Biol 2011; 18:822-30; PMID:21666678; http://dx.doi.org/10.1038/nsmb.2053
   PubMed Web of Science ®Google Scholar
• Wang IF, Chang HY, Hou SC, Liou GG, Way TD, James Shen CK. The self-interaction of native TDP-43 C terminus inhibits its degradation and contributes to early proteinopathies. Nat Commun 2012; 3:766; PMID:22473010; http://dx.doi.org/10.1038/ncomms1766
   PubMed Web of Science ®Google Scholar
• Nonaka T, Masuda-Suzukake M, Arai T, Hasegawa Y, Akatsu H, Obi T, Yoshida M, Murayama S, Mann DM, Akiyama H, et al. Prion-like properties of pathological TDP-43 aggregates from diseased brains. Cell Rep 2013; 4:124-34; PMID:23831027; http://dx.doi.org/10.1016/j.celrep.2013.06.007
   PubMed Web of Science ®Google Scholar
• Shimonaka S, Nonaka T, Suzuki G, Hisanaga S, Hasegawa M. Templated aggregation of TAR DNA-binding protein of 43 kDa (TDP-43) by seeding with TDP-43 peptide fibrils. J Biol Chem 2016; 291:8896-907; PMID:26887947; http://dx.doi.org/10.1074/jbc.M115.713552
   PubMed Web of Science ®Google Scholar
• Wang YT, Kuo PH, Chiang CH, Liang JR, Chen YR, Wang S, Shen JC, Yuan HS. The truncated C-terminal RNA recognition motif of TDP-43 protein plays a key role in forming proteinaceous aggregates. J Biol Chem 2013; 288:9049-57; PMID:23372158; http://dx.doi.org/10.1074/jbc.M112.438564
   PubMed Web of Science ®Google Scholar
• Kametani F, Obi T, Shishido T, Akatsu H, Murayama S, Saito Y, Yoshida M, Hasegawa M. Mass spectrometric analysis of accumulated TDP-43 in amyotrophic lateral sclerosis brains. Sci Rep 2016; 6:23281; PMID:26980269; http://dx.doi.org/10.1038/srep23281
   PubMed Web of Science ®Google Scholar
• Wu CH, Fallini C, Ticozzi N, Keagle PJ, Sapp PC, Piotrowska K, Lowe P, Koppers M, McKenna-Yasek D, Baron DM, et al. Mutations in the profilin 1 gene cause familial amyotrophic lateral sclerosis. Nature 2012; 488:499-503; PMID:22801503; http://dx.doi.org/10.1038/nature11280
   PubMed Web of Science ®Google Scholar
• Carlsson L, Nystrom LE, Sundkvist I, Markey F, Lindberg U. Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells. J Mol Biol 1977; 115:465-83; PMID:563468; http://dx.doi.org/10.1016/0022-2836(77)90166-8
   PubMed Web of Science ®Google Scholar
• Staiger CJ, Yuan M, Valenta R, Shaw PJ, Warn RM, Lloyd CW. Microinjected profilin affects cytoplasmic streaming in plant cells by rapidly depolymerizing actin microfilaments. Curr Biol 1994; 4:215-9; PMID:7922326; http://dx.doi.org/10.1016/S0960-9822(00)00050-6
   PubMed Web of Science ®Google Scholar
• Witke W. The role of profilin complexes in cell motility and other cellular processes. Trends Cell Biol 2004; 14:461-9; PMID:15308213; http://dx.doi.org/10.1016/j.tcb.2004.07.003
   PubMed Web of Science ®Google Scholar
• Figley MD, Bieri G, Kolaitis RM, Taylor JP, Gitler AD. Profilin 1 associates with stress granules and ALS-linked mutations alter stress granule dynamics. J Neurosci 2014; 34:8083-97; PMID:24920614; http://dx.doi.org/10.1523/JNEUROSCI.0543-14.2014
   PubMed Web of Science ®Google Scholar
• Smith BN, Vance C, Scotter EL, Troakes C, Wong CH, Topp S, Maekawa S, King A, Mitchell JC, Lund K, et al. Novel mutations support a role for profilin 1 in the pathogenesis of ALS. Neurobiol Aging 2015; 36:1602.e17-27; PMID:25499087; http://dx.doi.org/10.1016/j.neurobiolaging.2014.12.037
   PubMedGoogle Scholar
• Tanaka Y, Nonaka T, Suzuki G, Kametani F, Hasegawa M. Gain-of-function profilin 1 mutations linked to familial amyotrophic lateral sclerosis cause seed-dependent intracellular TDP-43 aggregation. Hum Mol Genet 2016; 25:1420-33; PMID:26908597; http://dx.doi.org/10.1093/hmg/ddw024
   PubMed Web of Science ®Google Scholar
• Ratti A, Buratti E. Physiological functions and pathobiology of TDP-43 and FUS/TLS proteins. J Neurochem 2016; Epub ahead of print; PMID:27015757
   PubMed Web of Science ®Google Scholar
• Martinez-Vicente M, Sovak G, Cuervo AM. Protein degradation and aging. Exp Gerontol 2005; 40:622-33; PMID:16125351; http://dx.doi.org/10.1016/j.exger.2005.07.005
   PubMed Web of Science ®Google Scholar
• Olzmann JA, Li L, Chin LS. Aggresome formation and neurodegenerative diseases: therapeutic implications. Curr Med Chem 2008; 15:47-60; PMID:18220762; http://dx.doi.org/10.2174/092986708783330692
   PubMed Web of Science ®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; 284:20329-39; PMID:19465477; http://dx.doi.org/10.1074/jbc.M109.010264
   PubMed Web of Science ®Google Scholar
• Freibaum BD, Chitta RK, High AA, Taylor JP. Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery. J Proteome Res 2010; 9:1104-20; PMID:20020773 http://dx.doi.org/10.1021/pr901076y
   PubMed Web of Science ®Google Scholar
• Yamashita M, Nonaka T, Hirai S, Miwa A, Okado H, Arai T, Hosokawa M, Akiyama H, Hasegawa M. Distinct pathways leading to TDP-43-induced cellular dysfunctions. Hum Mol Genet 2014; 23:4345-56; PMID:24698978; http://dx.doi.org/10.1093/hmg/ddu152
   PubMed Web of Science ®Google Scholar
• Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, et al. Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell 2006; 23:607-18; PMID:16916647; http://dx.doi.org/10.1016/j.molcel.2006.06.026
   PubMed Web of Science ®Google Scholar
• Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M. Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 2009; 325:834-40; PMID:19608861; http://dx.doi.org/10.1126/science.1175371
   PubMed Web of Science ®Google Scholar
• Ingre C, Landers JE, Rizik N, Volk AE, Akimoto C, Birve A, Hubers A, Keagle PJ, Piotrowska K, Press R, et al. A novel phosphorylation site mutation in profilin 1 revealed in a large screen of US, Nordic, and German amyotrophic lateral sclerosis/frontotemporal dementia cohorts. Neurobiol Aging 2013; 34:1708.e1-6; PMID:23141414; http://dx.doi.org/10.1016/j.neurobiolaging.2012.10.009
   PubMedGoogle Scholar