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  • Aung, T., Rezaie, T., Okada, K., Viswanathan, A.C., Child, A.H., Brice, G., et al. (2005) Clinical features and course of patients with glaucoma with the E50K mutation in the optineurin gene. Invest Ophthalmol Vis Sci 46: 28162822.
  • Ayscough, K.R., Stryker, J., Pokala, N., Sanders, M., Crews, P., and Drubin, D.G. (1997) High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A. J Cell Biol 137: 399416.
  • Bond, L.M., Peden, A.A., Kendrick-Jones, J., Sellers, J.R., and Buss, F. (2011) Myosin VI and its binding partner optineurin are involved in secretory vesicle fusion at the plasma membrane. Mol Biol Cell 22: 5465.
  • Chi, Z.L., Akahori, M., Obazawa, M., Minami, M., Noda, T., Nakaya, N., et al. (2010) Overexpression of optineurin E50K disrupts Rab8 interaction and leads to a progressive retinal degeneration in mice. Hum Mol Genet 19: 26062615.
  • Chibalina, M.V., Poliakov, A., Kendrick-Jones, J., and Buss, F. (2010) Myosin VI and optineurin are required for polarized EGFR delivery and directed migration. Traffic 11: 12901303.
  • De Marco, N., Buono, M., Troise, F., and Diez-Roux, G. (2006) Optineurin increases cell survival and translocates to the nucleus in a Rab8-dependent manner upon an apoptotic stimulus. J Biol Chem 281: 1614716156.
  • Deng, H.X., Chen, W., Hong, S.T., Boycott, K.M., Gorrie, G.H., Siddique, N., et al. (2011a) Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia. Nature 477: 211215.
  • Deng, H.X., Bigio, E.H., Zhai, H., Fecto, F., Ajroud, K., Shi, Y., et al. (2011b) Differential involvement of optineurin in amyotrophic lateral sclerosis with or without SOD1 mutations. Arch Neurol 68: 10571061.
  • Derkatch, I.L., Bradley, M.E., Hong, J.Y., and Liebman, S.W. (2001) Prions affect the appearance of other prions: the story of [PIN(+)]. Cell 106: 171182.
  • Elden, A.C., Kim, H.J., Hart, M.P., Chen-Plotkin, A.S., Johnson, B.S., Fang, X., et al. (2010) Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS. Nature 466: 10691075.
  • Ganusova, E.E., Ozolins, L.N., Bhagat, S., Newnam, G.P., Wegrzyn, R.D., Sherman, M.Y., and Chernoff, Y.O. (2006) Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast. Mol Cell Biol 26: 617629.
  • Gitler, A.D., and Shorter, J. (2011) RNA-binding proteins with prion-like domains in ALS and FTLD-U. Prion 5: 179187.
  • Gong, H., Romanova, N.V., Allen, K.D., Chandramowlishwaran, P., Gokhale, K., Newnam, G.P., et al. (2012) Polyglutamine toxicity is controlled by prion composition and gene dosage in yeast. PLoS Genet 8: e1002634.
  • Hattula, K., and Peranen, J. (2000) FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis. Curr Biol 10: 16031606.
  • Hortobagyi, T., Troakes, C., Nishimura, A.L., Vance, C., van Swieten, J.C., Seelaar, H., et al. (2011) Optineurin inclusions occur in a minority of TDP-43 positive ALS and FTLD-TDP cases and are rarely observed in other neurodegenerative disorders. Acta Neuropathol 121: 519527.
  • Iida, A., Hosono, N., Sano, M., Kamei, T., Oshima, S., Tokuda, T., et al. (2012) Novel deletion mutations of OPTN in amyotrophic lateral sclerosis in Japanese. Neurobiol Aging 33: 1843.e191843.e24.
  • Ince, P.G., Highley, J.R., Kirby, J., Wharton, S.B., Takahashi, H., Strong, M.J., and Shaw, P.J. (2011) Molecular pathology and genetic advances in amyotrophic lateral sclerosis: an emerging molecular pathway and the significance of glial pathology. Acta Neuropathol 122: 657671.
  • Johnson, B.S., Snead, D., Lee, J.J., McCaffery, J.M., Shorter, J., and Gitler, A.D. (2009) TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity. J Biol Chem 284: 2032920339.
  • Johnston, J.A., Ward, C.L., and Kopito, R.R. (1998) Aggresomes: a cellular response to misfolded proteins. J Cell Biol 143: 18831898.
  • Ju, S., Tardiff, D.F., Han, H., Divya, K., Zhong, Q., Maquat, L.E., et al. (2011) A yeast model of FUS/TLS-dependent cytotoxicity. PLoS Biol 9: e1001052.
  • Kabashi, E., Valdmanis, P.N., Dion, P., Spiegelman, D., McConkey, B.J., Vande Velde, C., et al. (2008) TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis. Nat Genet 40: 572574.
  • Kachaner, D., Genin, P., Laplantine, E., and Weil, R. (2012) Toward an integrative view of Optineurin functions. Cell Cycle 11: 28082818.
  • Kaganovich, D., Kopito, R., and Frydman, J. (2008) Misfolded proteins partition between two distinct quality control compartments. Nature 454: 10881095.
  • Kama, R., Robinson, M., and Gerst, J.E. (2007) Btn2, a Hook1 ortholog and potential Batten disease-related protein, mediates late endosome-Golgi protein sorting in yeast. Mol Cell Biol 27: 605621.
  • Karch, C.M., Prudencio, M., Winkler, D.D., Hart, P.J., and Borchelt, D.R. (2009) Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS. Proc Natl Acad Sci USA 106: 77747779.
  • Khurana, V., and Lindquist, S. (2010) Modelling neurodegeneration in Saccharomyces cerevisiae: why cook with baker's yeast? Nat Rev Neurosci 11: 436449.
  • Kryndushkin, D., and Shewmaker, F. (2011) Modeling ALS and FTLD proteinopathies in yeast: an efficient approach for studying protein aggregation and toxicity. Prion 5: 250257.
  • Kryndushkin, D., Wickner, R.B., and Shewmaker, F. (2011) FUS/TLS forms cytoplasmic aggregates, inhibits cell growth and interacts with TDP-43 in a yeast model of amyotrophic lateral sclerosis. Protein Cell 2: 223236.
  • Kryndushkin, D.S., Shewmaker, F., and Wickner, R.B. (2008) Curing of the [URE3] prion by Btn2p, a Batten disease-related protein. EMBO J 27: 27252735.
  • Kwiatkowski, T.J., Jr, Bosco, D.A., Leclerc, A.L., Tamrazian, E., Vanderburg, C.R., Russ, C., et al. (2009) Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 323: 12051208.
  • Lagier-Tourenne, C., and Cleveland, D.W. (2009) Rethinking ALS: the FUS about TDP-43. Cell 136: 10011004.
  • Lagier-Tourenne, C., Polymenidou, M., and Cleveland, D.W. (2010) TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration. Hum Mol Genet 19: R46R64.
  • Li, Y., Kang, J., and Horwitz, M.S. (1998) Interaction of an adenovirus E3 14.7-kilodalton protein with a novel tumor necrosis factor alpha-inducible cellular protein containing leucine zipper domains. Mol Cell Biol 18: 16011610.
  • Lobley, A., Whitmore, L., and Wallace, B.A. (2002) DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 18: 211212.
  • Luiro, K., Yliannala, K., Ahtiainen, L., Maunu, H., Jarvela, I., Kyttala, A., and Jalanko, A. (2004) Interconnections of CLN3, Hook1 and Rab proteins link Batten disease to defects in the endocytic pathway. Hum Mol Genet 13: 30173027.
  • McGlinchey, R.P., Kryndushkin, D., and Wickner, R.B. (2011) Suicidal [PSI+] is a lethal yeast prion. Proc Natl Acad Sci USA 108: 53375341.
  • Malinovska, L., Kroschwald, S., Munder, M.C., Richter, D., and Alberti, S. (2012) Molecular chaperones and stress-inducible protein sorting factors coordinate the spatio-temporal distribution of protein aggregates. Mol Biol Cell 23: 30413056.
  • Maruyama, H., Morino, H., Ito, H., Izumi, Y., Kato, H., Watanabe, Y., et al. (2010) Mutations of optineurin in amyotrophic lateral sclerosis. Nature 465: 223226.
  • Mathur, V., Taneja, V., Sun, Y., and Liebman, S.W. (2010) Analyzing the birth and propagation of two distinct prions, [PSI+] and [Het-s](y), in yeast. Mol Biol Cell 21: 14491461.
  • Meng, Q., Lv, J., Ge, H., Zhang, L., Xue, F., Zhu, Y., and Liu, P. (2012) Overexpressed mutant optineurin(E50K) induces retinal ganglion cells apoptosis via the mitochondrial pathway. Mol Biol Rep 39: 58675873.
  • Meriin, A.B., Zhang, X., He, X., Newnam, G.P., Chernoff, Y.O., and Sherman, M.Y. (2002) Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1. J Cell Biol 157: 9971004.
  • Muchowski, P.J., Schaffar, G., Sittler, A., Wanker, E.E., Hayer-Hartl, M.K., and Hartl, F.U. (2000) Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils. Proc Natl Acad Sci USA 97: 78417846.
  • Nagabhushana, A., Chalasani, M.L., Jain, N., Radha, V., Rangaraj, N., Balasubramanian, D., and Swarup, G. (2010) Regulation of endocytic trafficking of transferrin receptor by optineurin and its impairment by a glaucoma-associated mutant. BMC Cell Biol 11: 4.
  • Okita, S., Morigaki, R., Koizumi, H., Kaji, R., Nagahiro, S., and Goto, S. (2011) Cell type-specific localization of optineurin in the striatal neurons of mice: implications for neuronal vulnerability in Huntington's disease. Neuroscience 202: 363370.
  • Olzmann, J.A., Li, L., and Chin, L.S. (2008) Aggresome formation and neurodegenerative diseases: therapeutic implications. Curr Med Chem 15: 4760.
  • Osawa, T., Mizuno, Y., Fujita, Y., Takatama, M., Nakazato, Y., and Okamoto, K. (2011) Optineurin in neurodegenerative diseases. Neuropathology 31: 569574.
  • Park, B., Ying, H., Shen, X., Park, J.S., Qiu, Y., Shyam, R., and Yue, B.Y. (2010) Impairment of protein trafficking upon overexpression and mutation of optineurin. PLoS ONE 5: e11547.
  • Park, B.C., Shen, X., Samaraweera, M., and Yue, B.Y. (2006) Studies of optineurin, a glaucoma gene: Golgi fragmentation and cell death from overexpression of wild-type and mutant optineurin in two ocular cell types. Am J Pathol 169: 19761989.
  • Rezaie, T., Child, A., Hitchings, R., Brice, G., Miller, L., Coca-Prados, M., et al. (2002) Adult-onset primary open-angle glaucoma caused by mutations in optineurin. Science 295: 10771079.
  • Rosen, D.R., Siddique, T., Patterson, D., Figlewicz, D.A., Sapp, P., Hentati, A., et al. (1993) Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362: 5962.
  • Ross, C.A., and Poirier, M.A. (2004) Protein aggregation and neurodegenerative disease. Nat Med 10 (Suppl.): S10S17.
  • Sahlender, D.A., Roberts, R.C., Arden, S.D., Spudich, G., Taylor, M.J., Luzio, J.P., et al. (2005) Optineurin links myosin VI to the Golgi complex and is involved in Golgi organization and exocytosis. J Cell Biol 169: 285295.
  • Shen, X., Ying, H., Qiu, Y., Park, J.S., Shyam, R., Chi, Z.L., et al. (2011) Processing of optineurin in neuronal cells. J Biol Chem 286: 36183629.
  • Shewmaker, F., Wickner, R.B., and Tycko, R. (2006) Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure. Proc Natl Acad Sci USA 103: 1975419759.
  • Specht, S., Miller, S.B., Mogk, A., and Bukau, B. (2011) Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae. J Cell Biol 195: 617629.
  • Sreedharan, J., Blair, I.P., Tripathi, V.B., Hu, X., Vance, C., Rogelj, B., et al. (2008) TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 319: 16681672.
  • Su, L.J., Auluck, P.K., Outeiro, T.F., Yeger-Lotem, E., Kritzer, J.A., Tardiff, D.F., et al. (2010) Compounds from an unbiased chemical screen reverse both ER-to-Golgi trafficking defects and mitochondrial dysfunction in Parkinson's disease models. Dis Model Mech 3: 194208.
  • Sun, Z., Diaz, Z., Fang, X., Hart, M.P., Chesi, A., Shorter, J., and Gitler, A.D. (2011) Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS. PLoS Biol 9: e1000614.
  • Szebenyi, G., Wigley, W.C., Hall, B., Didier, A., Yu, M., Thomas, P., and Kramer, H. (2007) Hook2 contributes to aggresome formation. BMC Cell Biol 8: 19.
  • Treusch, S., and Lindquist, S. (2012) An intrinsically disordered yeast prion arrests the cell cycle by sequestering a spindle pole body component. J Cell Biol 197: 369379.
  • Vance, C., Rogelj, B., Hortobagyi, T., De Vos, K.J., Nishimura, A.L., Sreedharan, J., et al. (2009) Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science 323: 12081211.
  • Vishveshwara, N., Bradley, M.E., and Liebman, S.W. (2009) Sequestration of essential proteins causes prion associated toxicity in yeast. Mol Microbiol 73: 11011114.
  • Wang, Y., Meriin, A.B., Zaarur, N., Romanova, N.V., Chernoff, Y.O., Costello, C.E., and Sherman, M.Y. (2009) Abnormal proteins can form aggresome in yeast: aggresome-targeting signals and components of the machinery. FASEB J 23: 451463.
  • Weimer, J.M., Chattopadhyay, S., Custer, A.W., and Pearce, D.A. (2005) Elevation of Hook1 in a disease model of Batten disease does not affect a novel interaction between Ankyrin G and Hook1. Biochem Biophys Res Commun 330: 11761181.
  • Wild, P., Farhan, H., McEwan, D.G., Wagner, S., Rogov, V.V., Brady, N.R., et al. (2011) Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth. Science 333: 228233.
  • Winderickx, J., Delay, C., De Vos, A., Klinger, H., Pellens, K., Vanhelmont, T., et al. (2008) Protein folding diseases and neurodegeneration: lessons learned from yeast. Biochim Biophys Acta 1783: 13811395.
  • Wong, E.S., Tan, J.M., Soong, W.E., Hussein, K., Nukina, N., Dawson, V.L., et al. (2008) Autophagy-mediated clearance of aggresomes is not a universal phenomenon. Hum Mol Genet 17: 25702582.
  • Ying, H., and Yue, B.Y. (2012) Cellular and molecular biology of optineurin. Int Rev Cell Mol Biol 294: 223258.
  • Zhou, P., Derkatch, I.L., and Liebman, S.W. (2001) The relationship between visible intracellular aggregates that appear after overexpression of Sup35 and the yeast prion-like elements [PSI(+)] and [PIN(+)]. Mol Microbiol 39: 3746.
  • Zinman, L., and Cudkowicz, M. (2011) Emerging targets and treatments in amyotrophic lateral sclerosis. Lancet Neurol 10: 481490.