- About this Journal
- Abstracting and Indexing
- Aims and Scope
- Article Processing Charges
- Articles in Press
- Author Guidelines
- Bibliographic Information
- Citations to this Journal
- Contact Information
- Editorial Board
- Editorial Workflow
- Free eTOC Alerts
- Publication Ethics
- Reviewers Acknowledgment
- Submit a Manuscript
- Subscription Information
- Table of Contents
Neurology Research International
Volume 2012 (2012), Article ID 432780, 5 pages
RNA-Binding Proteins in Amyotrophic Lateral Sclerosis and Neurodegeneration
1Biochemistry and Molecular Biophysics Graduate Group, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA
2Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, 805b Stellar-Chance Laboratories, 422 Curie Boulevard, Philadelphia, PA 19104, USA
Received 26 January 2012; Accepted 26 February 2012
Academic Editor: Jeff Bronstein
Copyright © 2012 Scott E. Ugras and James Shorter. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- C. Lagier-Tourenne and D. W. Cleveland, “Rethinking ALS: the FUS about TDP-43,” Cell, vol. 136, no. 6, pp. 1001–1004, 2009.
- H. Ilieva, M. Polymenidou, and D. W. Cleveland, “Non-cell autonomous toxicity in neurodegenerative disorders: ALS and beyond,” Journal of Cell Biology, vol. 187, no. 6, pp. 761–772, 2009.
- M. Neumann, D. M. Sampathu, L. K. Kwong et al., “Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis,” Science, vol. 314, no. 5796, pp. 130–133, 2006.
- T. J. Kwiatkowski Jr., D. A. Bosco, A. L. LeClerc et al., “Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis,” Science, vol. 323, no. 5918, pp. 1205–1208, 2009.
- C. Vance, B. Rogelj, T. Hortobagyi et al., “Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6,” Science, vol. 323, no. 5918, pp. 1208–1211, 2009.
- E. Kabashi, P. N. Valdmanis, P. Dion et al., “TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis,” Nature Genetics, vol. 40, no. 5, pp. 572–574, 2008.
- J. Sreedharan, I. P. Blair, V. B. Tripathi et al., “TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis,” Science, vol. 319, no. 5870, pp. 1668–1672, 2008.
- E. Buratti and F. E. Baralle, “The multiple roles of TDP-43 in pre-mRNA processing and gene expression regulation,” RNA Biology, vol. 7, no. 4, pp. 420–429, 2010.
- Y. Kawahara and A. Mieda-Sato, “TDP-43 promotes microRNA biogenesis as a component of the Drosha and Dicer complexes,” Proceedings of the National Academy of Sciences of the United States of America, vol. 109, no. 9, pp. 3347–3352, 2012.
- S. da Cruz and D. W. Cleveland, “Understanding the role of TDP-43 and FUS/TLS in ALS and beyond,” Current Opinion in Neurobiology, vol. 21, no. 6, pp. 904–919, 2011.
- E. B. Lee, V. M. Lee, and J. Q. Trojanowski, “Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration,” Nature Reviews Neuroscience, vol. 13, no. 1, pp. 38–50, 2012.
- D. W. Colby and S. B. Prusiner, “De novo generation of prion strains,” Nature Reviews Microbiology, vol. 9, no. 11, pp. 771–777, 2011.
- M. Cushman, B. S. Johnson, O. D. King, A. D. Gitler, and J. Shorter, “Prion-like disorders: blurring the divide between transmissibility and infectivity,” Journal of Cell Science, vol. 123, no. 8, pp. 1191–1201, 2010.
- J. Shorter, “Emergence and natural selection of drug-resistant prions,” Molecular Biosystems, vol. 6, no. 7, pp. 1115–1130, 2010.
- J. Shorter and S. Lindquist, “Prions as adaptive conduits of memory and inheritance,” Nature Reviews Genetics, vol. 6, no. 6, pp. 435–450, 2005.
- O. D. King, A. D. Gitler, and J. Shorter, “The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease,” Brain Research.
- M. Polymenidou and D. W. Cleveland, “The seeds of neurodegeneration: prion-like spreading in ALS,” Cell, vol. 147, no. 3, pp. 498–508, 2011.
- A. D. Gitler and J. Shorter, “RNA-binding proteins with prion-like domains in ALS and FTLD-U,” Prion, vol. 5, no. 3, pp. 179–187, 2011.
- R. A. Fuentealba, M. Udan, S. Bell et al., “Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43,” Journal of Biological Chemistry, vol. 285, no. 34, pp. 26304–26314, 2010.
- M. Udan and R. H. Baloh, “Implications of the prion-related Q/N domains in TDP-43 and FUS,” Prion, vol. 5, no. 1, pp. 1–5, 2011.
- B. S. Johnson, D. Snead, J. J. Lee, J. M. McCaffery, J. Shorter, and A. D. Gitler, “TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity,” Journal of Biological Chemistry, vol. 284, no. 30, pp. 20329–20339, 2009.
- Z. Sun, Z. Diaz, X. Fang et al., “Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS,” PLoS Biology, vol. 9, no. 4, Article ID e1000614, 2011.
- Y. Furukawa, K. Kaneko, S. Watanabe, K. Yamanaka, and N. Nukina, “A seeding reaction recapitulates intracellular formation of sarkosyl-insoluble transactivation response element (TAR) dna-binding protein-43 inclusions,” Journal of Biological Chemistry, vol. 286, no. 21, pp. 18664–18672, 2011.
- J. M. Ravits and A. R. La Spada, “ALS motor phenotype heterogeneity, focality, and spread: deconstructing motor neuron degeneration,” Neurology, vol. 73, no. 10, pp. 805–811, 2009.
- J. Couthouis, M. P. Hart, J. Shorter, et al., “A yeast functional screen predicts new candidate ALS disease genes,” Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 52, pp. 20881–20890, 2011.
- A. D. Gitler, “Beer and bread to brains and beyond: can yeast cells teach us about neurodegenerative disease?” Neurosignals, vol. 16, no. 1, pp. 52–62, 2008.
- M. Armakola, M. P. Hart, and A. D. Gitler, “TDP-43 toxicity in yeast,” Methods, vol. 53, no. 3, pp. 238–245, 2011.
- R. J. Braun, C. Sommer, D. Carmona-Gutierrez et al., “Neurotoxic 43-kDa TAR DNA-binding protein (TDP-43) triggers mitochondrion-dependent programmed cell death in yeast,” Journal of Biological Chemistry, vol. 286, no. 22, pp. 19958–19972, 2011.
- B. S. Johnson, J. M. McCaffery, S. Lindquist, and A. D. Gitler, “A yeast TDP-43 proteinopathy model: exploring the molecular determinants of TDP-43 aggregation and cellular toxicity,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 17, pp. 6439–6444, 2008.
- D. Kryndushkin, R. B. Wickner, and F. Shewmaker, “FUS/TLS forms cytoplasmic aggregates, inhibits cell growth and interacts with TDP-43 in a yeast model of amyotrophic lateral sclerosis,” Protein and Cell, vol. 2, no. 3, pp. 223–236, 2011.
- S. Ju, D. F. Tardiff, H. Han et al., “A yeast model of FUS/TLS-dependent cytotoxicity,” PLoS Biology, vol. 9, no. 4, Article ID e1001052, 2011.
- K. Fushimi, C. Long, N. Jayaram, X. Chen, L. Li, and J. Y. Wu, “Expression of human FUS/TLS in yeast leads to protein aggregation and cytotoxicity, recapitulating key features of FUS proteinopathy,” Protein and Cell, vol. 2, no. 2, pp. 141–149, 2011.
- A. C. Elden, H. J. Kim, M. P. Hart et al., “Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS,” Nature, vol. 466, no. 7310, pp. 1069–1075, 2010.
- D. F. Tardiff, M. L. Tucci, K. A. Caldwell, G. A. Caldwell, and S. Lindquist, “Different 8-hydroxyquinolines protect models of TDP-43 protein, alpha-synuclein, and polyglutamine proteotoxicity through distinct mechanisms,” Journal of Biological Chemistry, vol. 287, no. 6, pp. 4107–4120, 2012.
- B. J. Lee, A. E. Cansizoglu, K. E. Suel, T. H. Louis, Z. Zhang, and Y. M. Chook, “Rules for nuclear localization sequence recognition by karyopherin β2,” Cell, vol. 126, no. 3, pp. 543–558, 2006.
- D. Dormann, R. Rodde, D. Edbauer et al., “ALS-associated fused in sarcoma (FUS) mutations disrupt transportin-mediated nuclear import,” EMBO Journal, vol. 29, no. 16, pp. 2841–2857, 2010.
- M. Neumann, E. Bentmann, D. Dormann, et al., “FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations,” Brain, vol. 134, no. Pt9, pp. 2595–2609, 2011.
- J. I. Hoell, E. L Larsson, S. Runge, et al., “RNA targets of wild-type and mutant FET family proteins,” Nature Structural and Molecular Biology, vol. 18, no. 12, pp. 1428–1431, 2011.
- M. Polymenidou, C. Lagier-Tourenne, K. R. Hutt et al., “Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43,” Nature Neuroscience, vol. 14, no. 4, pp. 459–468, 2011.
- Y. M. Ayala, L. de Conti, S. E. Avendano-Vazquez et al., “TDP-43 regulates its mRNA levels through a negative feedback loop,” The EMBO Journal, vol. 30, no. 2, pp. 277–288, 2011.
- J. R. Tollervey, T. Curk, B. Rogelj et al., “Characterizing the RNA targets and position-dependent splicing regulation by TDP-43,” Nature Neuroscience, vol. 14, no. 4, pp. 452–458, 2011.
- M. DeJesus-Hernandez, I. R. Mackenzie, B. F. Boeve, et al., “Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS,” Neuron, vol. 72, no. 2, pp. 245–256, 2011.
- A. E. Renton, E. Majounie, A. Waite, et al., “A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD,” Neuron, vol. 72, no. 2, pp. 257–268, 2011.