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2015 | 75 | 1 |

Tytuł artykułu

Role of the unfolded protein response in the pathogenesis of Parkinson’s disease

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Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Parkinson's disease is the second most common neurodegenerative disease which affects almost 1% of the population above the age of 60. It is is characterized by loss of dopaminergic neurons in the striatum and substantia nigra, coupled with the formation of intracellular Lewy bodies in degenerating neurons. Recent evidence suggests endoplasmic reticulum stress as a common and prominent occurrence in the progression of Parkinson's disease pathogenesis in the affected human brain. One of the cellular defense mechanism to combat endoplasmic reticulum stress due to excessive protein accumulation is through activation of the unfolded protein response pathway. In this review we focus on the impact and role of this unfolded protein response as a causative factor of Parkinson's disease leading to neurodegeneration.

Wydawca

-

Rocznik

Tom

75

Numer

1

Opis fizyczny

p.1-26,fig.,ref.

Twórcy

autor
  • Department of Genetic Engineering, SRM University, Chennai, TN, India
autor
  • School of Biosciences and Technology, Vellore Institute of Technology (VIT) University, Vellore, TN, India

Bibliografia

  • Andre R, Tabrizi SJ (2012) Misfolded PrP and a novel mechanism of proteasome inhibition. Prion 6: 32-36.
  • Araki K, Nagata K (2011) Protein folding and quality con­trol in the ER. Cold Spring Harb Perspect Biol 3: a007526.
  • Atkin JD, Farg MA, Turner BJ, Tomas D, Lysaght JA, Nunan J, Rembach A, Nagley P, Beart PM, Cheema SS , Horne MK (2006) Induction of the unfolded protein response in familial amyotrophic lateral sclerosis and association of protein-disulfide isomerase with superox­ide dismutase 1. J Biol Chem 281: 30152-30165.
  • Atkins C, Liu Q, Minthorn E, Zhang SY, Figueroa DJ, Moss K, Stanley TB, Sanders B, Goetz A, Gaul N, Choudhry AE, Alsaid H, Jucker BM, Axten JM, Kumar R (2013) Characterization of a novel PERK kinase inhibitor with antitumor and antiangiogenic activity. Cancer Res 73: 1993-2002.
  • Auluck PK, Chan HY, Trojanowski JQ, Lee VM, Bonini NM (2002) Chaperone suppression of a-synuclein toxic­ity in a Drosophila model for Parkinson's disease. Science. 295: 865-868.
  • Back SH, Kang SW, Han J, Chung HT (2012) Endoplasmic reticulum stress in the beta-cell pathogenesis of type 2 diabetes. Exp Diabetes Res 2012: 618396.
  • Barbeau A (1969) L-dopa therapy in Parkinson's disease: a critical review of nine years' experience. Can Med Assoc J 101: 59-68.
  • Bartels T, Choi JG, Selkoe DJ (2011) a-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature 477: 107-110.
  • Behrends C, Fulda S (2012) Receptor proteins in selective autophagy. Int J Cell Biol 2012: 673290.
  • Bekris LM, Mata IF, Zabetian CP (2010) The genetics of Parkinson disease. J Geriatr Psychiatry Neurol 23: 228­242.
  • Belal C, Ameli NJ, El Kommos A, Bezalel S, Al'Khafaji AM, Mughal MR, Mattson MP, Kyriazis GA, Tyrberg B, Chan SL (2012) The homocysteine-inducible endoplas­mic reticulum (ER) stress protein Herp counteracts mutant a-synuclein-induced ER stress via the homeo- static regulation of ER-resident calcium release channel proteins. Hum Mol Genet 21: 963-977.
  • Belin AC, Westerlund M (2008) Parkinson's disease: a genetic perspective. FEBS J 275: 1377-1383.
  • Bellucci A, Navarria L, Zaltieri M, Falarti E, Bodei S, Sigala S, Battistin L, Spillantini M, Missale C, Spano P (2011) Induction of the unfolded protein response by a-synuclein in experimental models of Parkinson's disease. J Neurochem 116: 588-605.
  • Betarbet R, Sherer TB, MacKenzie G, Garcia-Osuna M, Panov AV, Greenamyre JT (2000) Chronic systemic pes­ticide exposure reproduces features of Parkinson's dis­ease. Nat Neurosci 3: 1301-1306.
  • Blass S, Union A, Raymackers J, Schumann F, Ungethum U, Muller-Steinbach S, De Keyser F, Engel JM, Burmester GR (2001) The stress protein BiP is overexpressed and is a major B and T cell target in rheumatoid arthritis. Arthritis Rheum 44: 761-771.
  • Bogaert S, De Vos M, Olievier K, Peeters H, Elewaut D, Lambrecht B, Pouliot P, Laukens D (2011) Involvement of endoplasmic reticulum stress in inflammatory bowel disease: a different implication for colonic and ileal dis­ease? PLoS One 6: e25589.
  • Bowling AC, Beal MF (1995) Bioenergetic and oxidative stress in neurodegenerative diseases. Life Sci 56: 1151­1171.
  • Braakman I, Bulleid NJ (2011) Protein folding and modifi­cation in the mammalian endoplasmic reticulum. Annu Rev Biochem 80: 71-99.
  • Brewer JW, Diehl JA (2000) PERK mediates cell-cycle exit during the mammalian unfolded protein response. Proc Natl Acad Sci U S A 97: 12625-12630.
  • Brundin P, Li JY, Holton JL, Lindvall O, Revesz T (2008) Research in motion: the enigma of Parkinson's disease pathology spread. Nat Rev Neurosci 9: 741-745.
  • Bukau B, Weissman J, Horwich A (2006) Molecular chaperones and protein quality control. Cell 125: 443-451.
  • Burbulla LF, Schelling C, Kato H, Rapaport D, Woitalla D, Schiesling C, Schulte C, Sharma M, Illig T, Bauer P, Jung S, Nordheim A, Schols L, Riess O, Kruger R (2010) Dissecting the role of the mitochondrial chaperone morta- lin in Parkinson's disease: functional impact of disease- related variants on mitochondrial homeostasis. Hum Mol Genet 19: 4437-4452.
  • Calne DB, Teychenne PF, Claveria LE, Eastman R, Greenacre JK, Petrie A (1974) Bromocriptine in Parkinsonism. Br Med J 4: 442-444.
  • Carlsson A, Lindqvist M, Magnusson T (1957) 3,4-Dihy- droxyphenylalanine and 5-hydroxytryptophan as reser- pine antagonists. Nature 180: 1200.
  • Carnemolla A, Fossale E, Agostoni E, Michelazzi S, Calligaris R, De Maso L, Del Sal G, MacDonald ME, Persichetti F (2009) Rrs1 is involved in endoplasmic reticulum stress response in Huntington disease. J Biol Chem 284: 18167-18173.
  • Chandra S, Gallardo G, Fernandez-Chacon R, Schluter OM, Sudhof TC (2005) A-synuclein cooperates with CSPa in preventing neurodegeneration. Cell 123: 383-396.
  • Chartier-Harlin MC, Kachergus J, Roumier C, Mouroux V, Douay X, Lincoln S, Levecque C, Larvor L, Andrieux J, Hulihan M, Waucquier N, Defebvre L, Amouyel P, Farrer M, Destee A (2004) A-synuclein locus duplication as a cause of familial Parkinson's disease. Lancet 364: 1167­1169.
  • Colla E, Coune P, Liu Y, Pletnikova O, Troncoso JC, Iwatsubo T, Schneider BL, Lee MK (2012) Endoplasmic reticulum stress is important for the manifestations of a-synucleinopathy in vivo. J Neurosci 32: 3306-3320.
  • Conway KA, Harper JD, Lansbury PT (1998) Accelerated in vitro fibril formation by a mutant a-synuclein linked to early-onset Parkinson disease. Nat Med 4: 1318-1320.
  • Cooper AA, Gitler AD, Cashikar A, Haynes CM, Hill KJ, Bhullar B, Liu K, Xu K, Strathearn KE, Liu F, Cao S, Caldwell KA, Caldwell GA, Marsischky G, Kolodner RD, Labaer J, Rochet JC, Bonini NM, Lindquist S (2006) a-synuclein blocks ER-Golgi traffic and Rabl rescues neuron loss in Parkinson's models. Science 313: 324­328.
  • Cotzias GC, Papavasiliou PS, Gellene R (1969) Modification of Parkinsonism--chronic treatment with L-dopa. N Engl J Med 280: 337-345.
  • Cox JS, Walter P (1996) A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell 87: 391-404.
  • Cox JS, Shamu CE, Walter P (1993) Transcriptional induc­tion of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 73: 1197-1206.
  • Dauer W, Ho CC (2010) The biology and pathology of the familial Parkinson's disease protein LRRK2. Mov Disord 25 Suppl 1: S40-43.
  • Dawson TM, Dawson VL (2003) Rare genetic mutations shed light on the pathogenesis of Parkinson disease. J Clin Invest 111: 145-151.
  • De Lau LM, Breteler MM (2006) Epidemiology of Parkinson's disease. Lancet Neurol 5: 525-535.
  • Debono AG, Marsden CD, Asselman P, Parkes JD (1976) Bromocriptine and dopamine receptor stimulation. Br J Clin Pharmacol 3: 977-982.
  • Devi L, Raghavendran V, Prabhu BM, Avadhani NG, Anandatheerthavarada HK (2008) Mitochondrial import and accumulation of a-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain. J Biol Chem 283: 9089-9100.
  • Di Fonzo A, Dekker MC, Montagna P, Baruzzi A, Yonova EH, Correia Guedes L, Szczerbinska A, Zhao T, Dubbel- Hulsman LO, Wouters CH, de Graaff E, Oyen WJ, Simons EJ, Breedveld GJ, Oostra BA, Horstink MW, Bonifati V (2009) FBXO7 mutations cause autosomal recessive, early-onset parkinsonian-pyramidal syndrome. Neurology 72: 240-245.
  • Dong D, Ni M, Li J, Xiong S, Ye W, Virrey JJ, Mao C, Ye R, Wang M, Pen L, Dubeau L, Groshen S, Hofman FM, Lee AS (2008) Critical role of the stress chaperone GRP78/ BiP in tumor proliferation, survival, and tumor angiogen- esis in transgene-induced mammary tumor development. Cancer Res 68: 498-505.
  • Duda JE, Giasson BI, Chen Q, Gur TL, Hurtig HI, Stern MB, Gollomp SM, Ischiropoulos H, Lee VM, Trojanowski JQ (2000) Widespread nitration of pathological inclu­sions in neurodegenerative synucleinopathies. Am J Pathol 157: 1439-1445.
  • El-Agnaf OM, Salem SA, Paleologou KE, Curran MD, Gibson MJ, Court JA, Schlossmacher MG, Allsop D (2006) Detection of oligomeric forms of a-synuclein pro­tein in human plasma as a potential biomarker for Parkinson's disease. FASEB J 20: 419-425.
  • Farrer MJ (2006) Genetics of Parkinson disease: paradigm shifts and future prospects. Nat Rev Genet 7: 306-318.
  • Fauvet B, Mbefo MK, Fares MB, Desobry C, Michael S, Ardah MT, Tsika E, Coune P, Prudent M, Lion N, Eliezer D, Moore DJ, Schneider B, Aebischer P, El-Agnaf OM, Masliah E, Lashuel HA (2012) a-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer. J Biol Chem 287: 15345-15364.
  • Fedoroff N (2006) Redox regulatory mechanisms in cellular stress responses. Ann Bot 98: 289-300.
  • Fonseca SG, Gromada J, Urano F (2011) Endoplasmic reticulum stress and pancreatic beta-cell death. Trends Endocrinol Metab 22: 266-274.
  • Fortin DL, Troyer MD, Nakamura K, Kubo S, Anthony MD, Edwards RH (2004) Lipid rafts mediate the synaptic localization of a-synuclein. J Neurosci 24: 6715-6723.
  • Fujita E, Kouroku Y, Isoai A, Kumagai H, Misutani A, Matsuda C, Hayashi YK, Momoi T (2007) Two endoplas- mic reticulum-associated degradation (ERAD) systems for the novel variant of the mutant dysferlin: ubiquitin/ proteasome ERAD(I) and autophagy/lysosome ERAD(II). Hum Mol Genet 16: 618-629.
  • Fujiwara H, Hasegawa M, Dohmae N, Kawashima A, Masliah E, Goldberg MS, Shen J, Takio K, Iwatsubo T (2002) a-Synuclein is phosphorylated in synucleinopathy lesions. Nat Cell Biol 4: 160-164.
  • Funayama M, Hasegawa K, Kowa H, Saito M, Tsuji S, Obata F (2002) A new locus for Parkinson's disease (PARK8) maps to chromosome 12p11.2-q13.1. Ann Neurol 51: 296-301.
  • Gasser T, Muller-Myhsok B, Wszolek ZK, Oehlmann R, Calne DB, Bonifati V, Bereznai B, Fabrizio E, Vieregge P, Horstmann RD (1998) A susceptibility locus for Parkinson's disease maps to chromosome 2p13. Nat Genet 18: 262-265.
  • Gehrke S, Imai Y, Sokol N, Lu B (2010) Pathogenic LRRK2 negatively regulates microRNA-mediated translational repression. Nature 466: 637-641.
  • Gething MJ (1999) Role and regulation of the ER chaperone BiP. Semin Cell Dev Biol 10: 465-472.
  • Gorbatyuk MS, Knox T, LaVail MM, Gorbatyuk OS, Noorwez SM, Hauswirth WW, Lin JH, Muzyczka N, Lewin AS (2010) Restoration of visual function in P23H rhodopsin transgenic rats by gene delivery of BiP/Grp78. Proc Natl Acad Sci U S A 107: 5961-5966.
  • Gorlach A, Klappa P, Kietzmann T (2006) The endoplas- mic reticulum: folding, calcium homeostasis, signaling, and redox control. Antioxid Redox Signal 8: 1391­1418.
  • Greggio E, Cookson MR (2009) Leucine-rich repeat kinase 2 mutations and Parkinson's disease: three questions. ASN Neuro 1: pii: e00002.
  • Grunblatt E, Mandel S, Youdim MB (2000) Neuroprotective strategies in Parkinson's disease using the models of 6-hydroxydopamine and MPTP. Ann N Y Acad Sci 899: 262-273.
  • Halliday M, Mallucci GR (2014) Targeting the unfolded protein response in neurodegeneration: A new approach to therapy. Neuropharmacology 76 Pt A: 169-174.
  • Hamza TH, Zabetian CP, Tenesa A, Laederach A, Montimurro J, Yearout D, Kay DM, Doheny KF, Paschall J, Pugh E, Kusel VI, Collura R, Roberts J, Griffith A, Samii A, Scott WK, Nutt J, Factor SA, Payami H (2010) Common genetic variation in the HLA region is associated with late-onset sporadic Parkinson's disease. Nat Genet 42: 781-785.
  • Harding HP, Zhang Y, Ron D (1999) Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397: 271-274.
  • Harding HP, Novoa I, Zhang Y, Zeng H, Wek R, Schapira M, Ron D (2000) Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol Cell 6: 1099-1108.
  • Harding HP, Zhang Y, Zeng H, Novoa I, Lu PD, Calfon M, Sadri N, Yun C, Popko B, Paules R, Stojdl DF, Bell JC, Hettmann T, Leiden JM, Ron D (2003) An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol Cell 11: 619-633.
  • Hariz M (2014) Deep brain stimulation: new techniques. Parkinsonism Relat Disord 20 Suppl 1: S192-196.
  • Haze K, Yoshida H, Yanagi H, Yura T, Mori K (1999) Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Biol Cell 10: 3787-3799.
  • He B (2006) Viruses, endoplasmic reticulum stress, and interferon responses. Cell Death Differ 13: 393-403.
  • Healy DG, Falchi M, O'Sullivan SS, Bonifati V, Durr A, Bressman S, Brice A, Aasly J, Zabetian CP, Goldwurm S, Ferreira JJ, Tolosa E, Kay DM, Klein C, Williams DR, Marras C, Lang AE, Wszolek ZK, Berciano J, Schapira AH, Lynch T, Bhatia KP, Gasser T, Lees AJ, Wood NW (2008) Phenotype, genotype, and worldwide genetic pen- etrance of LRRK2-associated Parkinson's disease: a case- control study. Lancet Neurol 7: 583-590.
  • Henchcliffe C, Beal MF (2008) Mitochondrial biology and oxidative stress in Parkinson disease pathogenesis. Nat Clin Pract Neurol 4: 600-609.
  • Hetz C (2012) The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat Rev Mol Cell Biol 13: 89-102.
  • Hicks AA, Petursson H, Jonsson T, Stefansson H, Johannsdottir HS, Sainz J, Frigge ML, Kong A, Gulcher JR, Stefansson K, Sveinbjornsdottir S (2002) A suscepti­bility gene for late-onset idiopathic Parkinson's disease. Ann Neurol 52: 549-555.
  • Hollien J, Lin JH, Li H, Stevens N, Walter P, Weissman JS (2009) Regulated Ire1-dependent decay of messenger RNAs in mammalian cells. J Cell Biol 186: 323-331.
  • Holtz WA, O'Malley KL (2003) Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons. J Biol Chem 278: 19367-19377.
  • Hoozemans JJ, van Haastert ES, Eikelenboom P, de Vos RA, Rozemuller JM, Scheper W (2007) Activation of the unfolded protein response in Parkinson's disease. Biochem Biophys Res Commun 354: 707-711.
  • Hoozemans JJ, Veerhuis R, Van Haastert ES, Rozemuller JM, Baas F, Eikelenboom P, Scheper W (2005) The unfolded protein response is activated in Alzheimer's disease. Acta Neuropathol 110: 165-172.
  • Hoozemans JJ, van Haastert ES, Nijholt DA, Rozemuller AJ, Eikelenboom P, Scheper W (2009) The unfolded pro­tein response is activated in pretangle neurons in Alzheimer's disease hippocampus. Am J Pathol 174: 1241-1251.
  • Hoozemans JJ, van Haastert ES, Nijholt DA, Rozemuller AJ, Scheper W (2012) Activation of the unfolded protein response is an early event in Alzheimer's and Parkinson's disease. Neurodegener Dis 10: 212-215.
  • Horwich AL, Weber-Ban EU, Finley D (1999) Chaperone rings in protein folding and degradation. Proc Natl Acad Sci U S A 96: 11033-11040.
  • Hsu CH, Chan D, Greggio E, Saha S, Guillily MD, Ferree A, Raghavan K, Shen GC, Segal L, Ryu H, Cookson MR, Wolozin B (2010) MKK6 binds and regulates expression of Parkinson's disease-related protein LRRK2. J Neurochem 112: 1593-1604.
  • Hu P, Han Z, Couvillon AD, Kaufman RJ, Exton JH (2006) Autocrine tumor necrosis factor a links endoplasmic reticulum stress to the membrane death receptor pathway through IREla-mediated NF-kappaB activation and down-regulation of TRAF2 expression. Mol Cell Biol 26: 3071-3084.
  • Huot P, Johnston TH, Koprich JB, Fox SH, Brotchie JM (2013) The pharmacology of L-DOPA-induced dyskine­sia in Parkinson's disease. Pharmacol Rev 65: 171-222.
  • Hussain SG, Ramaiah KV (2007) Reduced eIF2alpha phos­phorylation and increased proapoptotic proteins in aging. Biochem Biophys Res Commun 355: 365-370.
  • Ibanez P, Bonnet AM, Debarges B, Lohmann E, Tison F, Pollak P, Agid Y, Durr A, Brice A (2004) Causal relation between a-synuclein gene duplication and familial Parkinson's disease. Lancet 364: 1169-1171.
  • Imai Y, Soda M, Inoue H, Hattori N, Mizuno Y, Takahashi R (2001) An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a sub­strate of Parkin. Cell 105: 891-902.
  • Imai Y, Soda M, Takahashi R (2000) Parkin suppresses unfold­ed protein stress-induced cell death through its E3 ubiquitin- protein ligase activity. J Biol Chem 275: 35661-35664.
  • Itano Y, Kitamura Y, Nomura Y (1994) 1-Methyl-4-phe- nylpyridinium (MPP+)-induced cell death in PC12 cells: inhibitory effects of several drugs. Neurochem Int 25: 419-424.
  • Jakes R, Spillantini MG, Goedert M (1994) Identification of two distinct synucleins from human brain. FEBS Lett 345: 27-32.
  • Jamora C, Dennert G, Lee AS (1996) Inhibition of tumor progression by suppression of stress protein GRP78/BiP induction in fibrosarcoma B/C10ME. Proc Natl Acad Sci U S A 93: 7690-7694.
  • Jankovic J, Aguilar LG (2008) Current approaches to the treatment of Parkinson's disease. Neuropsychiatr Dis Treat 4: 743-757.
  • Jin SM, Youle RJ (2013) The accumulation of misfolded proteins in the mitochondrial matrix is sensed by PINK1 to induce PARK2/Parkin-mediated mitophagy of polar­ized mitochondria. Autophagy 9: 1750-1757.
  • Kalia LV, Kalia SK, Chau H, Lozano AM, Hyman BT, McLean PJ (2011) Ubiquitinylation of a-synuclein by carboxyl terminus Hsp70-interacting protein (CHIP) is regulated by Bcl-2-associated athanogene 5 (BAG5). PLoS One 6: e14695.
  • Kalia LV, Kalia SK, McLean PJ, Lozano AM, Lang AE (2013) a-Synuclein oligomers and clinical implications for Parkinson disease. Ann Neurol 73: 155-169.
  • Kanao T, Venderova K, Park DS, Unterman T, Lu B, Imai Y (2010) Activation of FoxO by LRRK2 induces expression of proapoptotic proteins and alters survival of postmitotic dopaminergic neuron in Drosophila. Hum Mol Genet 19: 3747-3758.
  • Kaneko M, Niinuma Y, Nomura Y (2003) Activation signal of nuclear factor-kappa B in response to endoplasmic reticulum stress is transduced via IRE1 and tumor necro­sis factor receptor-associated factor 2. Biol Pharm Bull 26: 931-935.
  • Kang MJ, Ryoo HD (2009) Suppression of retinal degenera­tion in Drosophila by stimulation of ER-associated degra­dation. Proc Natl Acad Sci U S A 106: 17043-17048.
  • Kaser A, Adolph TE, Blumberg RS (2013) The unfolded protein response and gastrointestinal disease. Semin Immunopathol 35: 307-319.
  • Katayama T, Imaizumi K, Manabe T, Hitomi J, Kudo T, Tohyama M (2004) Induction of neuronal death by ER stress in Alzheimer's disease. J Chem Neuroanat 28: 67-78.
  • Kim I, Xu W, Reed JC (2008) Cell death and endoplasmic reticulum stress: disease relevance and therapeutic oppor­tunities. Nat Rev Drug Discov 7: 1013-1030.
  • Kitada T, Asakawa S, Hattori N, Matsumine H, Yamamura Y, Minoshima S, Yokochi M, Mizuno Y, Shimizu N (1998) Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392: 605-608.
  • Kohno K (2010) Stress-sensing mechanisms in the unfolded protein response: similarities and differences between yeast and mammals. J Biochem 147: 27-33.
  • Kondo S, Murakami T, Tatsumi K, Ogata M, Kanemoto S, Otori K, Iseki K, Wanaka A, Imaizumi K (2005) OASIS, a CREB/ATF-family member, modulates UPR signalling in astrocytes. Nat Cell Biol 7: 186-194.
  • Kopito RR, Ron D (2000) Conformational disease. Nat Cell Biol 2: E207-209.
  • Korolchuk VI, Menzies FM, Rubinsztein DC (2010) Mechanisms of cross-talk between the ubiquitin-protea- some and autophagy-lysosome systems. FEBS Lett 584: 1393-1398.
  • Krishnamoorthy T, Pavitt GD, Zhang F, Dever TE, Hinnebusch AG (2001) Tight binding of the phosphory- lated a subunit of initiation factor 2 (eIF2a) to the regula­tory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation. Mol Cell Biol 21: 5018-5030.
  • Kruger R, Kuhn W, Muller T, Woitalla D, Graeber M, Kosel S, Przuntek H, Epplen JT, Schols L, Riess O (1998) Ala30Pro mutation in the gene encoding a-synuclein in Parkinson's disease. Nat Genet 18: 106-108.
  • Kudo T, Kanemoto S, Hara H, Morimoto N, Morihara T, Kimura R, Tabira T, Imaizumi K, Takeda M (2008) A molecular chaperone inducer protects neurons from ER stress. Cell Death Differ 15: 364-375.
  • Lai E, Teodoro T, Volchuk A (2007) Endoplasmic reticulum stress: signaling the unfolded protein response. Physiology (Bethesda) 22: 193-201.
  • Langston JW, Ballard P, Tetrud JW, Irwin I (1983) Chronic Parkinsonism in humans due to a product of meperidine- analog synthesis. Science 219: 979-980.
  • Lautier C, Goldwurm S, Durr A, Giovannone B, Tsiaras WG, Pezzoli G, Brice A, Smith RJ (2008) Mutations in the GIGYF2 (TNRC15) gene at the PARK11 locus in familial Parkinson disease. Am J Hum Genet 82: 822-833.
  • Lee K, Tirasophon W, Shen X, Michalak M, Prywes R, Okada T, Yoshida H, Mori K, Kaufman RJ (2002) IRE1- mediated unconventional mRNA splicing and S2P- mediated ATF6 cleavage merge to regulate XBP1 in sig­naling the unfolded protein response. Genes Dev 16: 452-466.
  • Liu CY, Xu Z, Kaufman RJ (2003) Structure and intermo­lecular interactions of the luminal dimerization domain of human IREla. J Biol Chem 278: 17680-17687.
  • Liu Z, Wang X, Yu Y, Li X, Wang T, Jiang H, Ren Q, Jiao Y, Sawa A, Moran T, Ross CA, Montell C, Smith WW (2008) A Drosophila model for LRRK2-linked parkin­sonism. Proc Natl Acad Sci U S A 105: 2693-2698.
  • Ma K, Vattem KM, Wek RC (2002) Dimerization and release of molecular chaperone inhibition facilitate acti­vation of eukaryotic initiation factor-2 kinase in response to endoplasmic reticulum stress. J Biol Chem 277: 18728-18735.
  • MacLeod D, Dowman J, Hammond R, Leete T, Inoue K, Abeliovich A (2006) The familial Parkinsonism gene LRRK2 regulates neurite process morphology. Neuron 52: 587-593.
  • Makioka K, Yamazaki T, Fujita Y, Takatama M, Nakazato Y, Okamoto K (2010) Involvement of endoplasmic reticu- lum stress defined by activated unfolded protein response in multiple system atrophy. J Neurol Sci 297: 60-65.
  • Maly DJ, Papa FR (2014) Druggable sensors of the unfolded protein response. Nat Chem Biol 10: 892-901.
  • Martin I, Dawson VL, Dawson TM (2011) Recent advances in the genetics of Parkinson's disease. Annu Rev Genomics Hum Genet 12: 301-325.
  • Martinus RD, Garth GP, Webster TL, Cartwright P, Naylor DJ, Hoj PB, Hoogenraad NJ (1996) Selective induction of mitochondrial chaperones in response to loss of the mitochondrial genome. Eur J Biochem 240: 98-103.
  • Mata IF, Ross OA, Kachergus J, Huerta C, Ribacoba R, Moris G, Blazquez M, Guisasola LM, Salvador C, Martinez C, Farrer M, Alvarez V (2006) LRRK2 muta­tions are a common cause of Parkinson's disease in Spain. Eur J Neurol 13: 391-394.
  • Mata IF, Shi M, Agarwal P, Chung KA, Edwards KL, Factor SA, Galasko DR, Ginghina C, Griffith A, Higgins DS, Kay DM, Kim H, Leverenz JB, Quinn JF, Roberts JW, Samii A, Snapinn KW, Tsuang DW, Yearout D, Zhang J, Payami H, Zabetian CP (2010) SNCA variant associated with Parkinson disease and plasma a-synuclein level. Arch Neurol 67: 1350-1356.
  • Mimori S, Okuma Y, Kaneko M, Kawada K, Hosoi T, Ozawa K, Nomura Y, Hamana H (2012) Protective effects of 4-phenylbutyrate derivatives on the neuronal cell death and endoplasmic reticulum stress. Biol Pharm Bull 35: 84-90.
  • Moisoi N, Klupsch K, Fedele V, East P, Sharma S, Renton A, Plun-Favreau H, Edwards RE, Teismann P, Esposti MD, Morrison AD, Wood NW, Downward J, Martins LM (2009) Mitochondrial dysfunction triggered by loss of HtrA2 results in the activation of a brain-specific transcrip­tional stress response. Cell Death Differ 16: 449-464.
  • Moreno JA, Radford H, Peretti D, Steinert JR, Verity N, Martin MG, Halliday M, Morgan J, Dinsdale D, Ortori CA, Barrett DA, Tsaytler P, Bertolotti A, Willis AE, Bushell M, Mallucci GR (2012) Sustained translational repression by eIF2alpha-P mediates prion neurodegenera­tion. Nature 485: 507-511.
  • Mori K (2000) Tripartite management of unfolded proteins in the endoplasmic reticulum. Cell 101: 451-454.
  • Murata M, Hasegawa K, Kanazawa I (2007) Zonisamide improves motor function in Parkinson disease: a random­ized, double-blind study. Neurology 68: 45-50.
  • Murata M, Horiuchi E, Kanazawa I (2001) Zonisamide has beneficial effects on Parkinson's disease patients. Neurosci Res 41: 397-399.
  • Naidoo N, Ferber M, Master M, Zhu Y, Pack AI (2008) Aging impairs the unfolded protein response to sleep deprivation and leads to proapoptotic signaling. J Neurosci 28: 6539-6548.
  • Ng CH, Mok SZ, Koh C, Ouyang X, Fivaz ML, Tan EK, Dawson VL, Dawson TM, Yu F, Lim KL (2009) Parkin protects against LRRK2 G2019S mutant-induced dop­aminergic neurodegeneration in Drosophila. J Neurosci 29: 11257-11262.
  • Nijholt DA, de Graaf TR, van Haastert ES, Oliveira AO, Berkers CR, Zwart R, Ovaa H, Baas F, Hoozemans JJ, Scheper W (2011) Endoplasmic reticulum stress activates autophagy but not the proteasome in neuronal cells: implications for Alzheimer's disease. Cell Death Differ 18: 1071-1081.
  • Nijholt DA, van Haastert ES, Rozemuller AJ, Scheper W, Hoozemans JJ (2012) The unfolded protein response is associated with early tau pathology in the hippocampus of tauopathies. J Pathol 226: 693-702.
  • Nuss JE, Choksi KB, DeFord JH, Papaconstantinou J (2008) Decreased enzyme activities of chaperones PDI and BiP in aged mouse livers. Biochem Biophys Res Commun 365: 355-361.
  • O'Connor T, Sadleir KR, Maus E, Velliquette RA, Zhao J, Cole SL, Eimer WA, Hitt B, Bembinster LA, Lammich S, Lichtenthaler SF, Hebert SS, De Strooper B, Haass C, Bennett DA, Vassar R (2008) Phosphorylation of the translation initiation factor eIF2alpha increases BACE1 levels and promotes amyloidogenesis. Neuron 60: 988­1009.
  • Obeso JA, Rodriguez-Oroz MC, Benitez-Temino B, Blesa FJ, Guridi J, Marin C, Rodriguez M (2008) Functional organization of the basal ganglia: therapeutic implica­tions for Parkinson's disease. Mov Disord 23 Suppl 3: S548-559.
  • Obeso JA, Rodriguez-Oroz MC, Goetz CG, Marin C, Kordower JH, Rodriguez M, Hirsch EC, Farrer M, Schapira AH, Halliday G (2010) Missing pieces in the Parkinson's disease puzzle. Nat Med 16: 653-661.
  • Omura T, Asari M, Yamamoto J, Kamiyama N, Oka K, Hoshina C, Maseda C, Awaya T, Tasaki Y, Shiono H,
  • Shimizu K, Matsubara K (2012) HRD1 levels increased by zonisamide prevented cell death and caspase-3 activa­tion caused by endoplasmic reticulum stress in SH-SY5Y cells. J Mol Neurosci 46: 527-535.
  • Omura T, Kaneko M, Okuma Y, Matsubara K, Nomura Y (2013) Endoplasmic reticulum stress and Parkinson's dis­ease: the role of HRD1 in averting apoptosis in neurode­generative disease. Oxid Med Cell Longev 2013: 239854.
  • Ono K, Ikemoto M, Kawarabayashi T, Ikeda M, Nishinakagawa T, Hosokawa M, Shoji M, Takahashi M, Nakashima M (2009) A chemical chaperone, sodium 4-phenylbutyric acid, attenuates the pathogenic potency in human a-synuclein A30P + A53T transgenic mice. Parkinsonism Relat Disord 15: 649-654.
  • Orenstein SJ, Kuo SH, Tasset I, Arias E, Koga H, Fernandez- Carasa I, Cortes E, Honig LS, Dauer W, Consiglio A, Raya A, Sulzer D, Cuervo AM (2013) Interplay of LRRK2 with chaperone-mediated autophagy. Nat Neurosci 16: 394-406.
  • Ozcan U, Cao Q, Yilmaz E, Lee AH, Iwakoshi NN, Ozdelen E, Tuncman G, Gorgun C, Glimcher LH, Hotamisligil GS (2004) Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes. Science 306: 457-461.
  • Paisan-Ruiz C, Jain S, Evans EW, Gilks WP, Simon J, van der Brug M, Lopez de Munain A, Aparicio S, Gil AM, Khan N, Johnson J, Martinez JR, Nicholl D, Carrera IM, Pena AS, de Silva R, Lees A, Marti-Masso JF, Perez-Tur J, Wood NW, Singleton AB (2004) Cloning of the gene containing mutations that cause PARK8-linked Parkinson's disease. Neuron 44: 595-600.
  • Paisan-Ruiz C, Bhatia KP, Li A, Hernandez D, Davis M, Wood NW, Hardy J, Houlden H, Singleton A, Schneider SA (2009) Characterization of PLA2G6 as a locus for dystonia-parkinsonism. Ann Neurol 65: 19-23.
  • Pankratz N, Nichols WC, Uniacke SK, Halter C, Murrell J, Rudolph A, Shults CW, Conneally PM, Foroud T (2003) Genome-wide linkage analysis and evidence of gene-by- gene interactions in a sample of 362 multiplex Parkinson disease families. Hum Mol Genet 12: 2599-2608.
  • Pankratz N, Wilk JB, Latourelle JC, DeStefano AL, Halter C, Pugh EW, Doheny KF, Gusella JF, Nichols WC, Foroud T, Myers RH (2009) Genomewide association study for susceptibility genes contributing to familial Parkinson disease. Hum Genet 124: 593-605.
  • Parihar MS, Parihar A, Fujita M, Hashimoto M, Ghafourifar P (2008) Mitochondrial association of a-synuclein causes oxidative stress. Cell Mol Life Sci 65: 1272-1284.
  • Paz Gavilan M, Vela J, Castano A, Ramos B, del Rio JC, Vitorica J, Ruano D (2006) Cellular environment facili­tates protein accumulation in aged rat hippocampus. Neurobiol Aging 27: 973-982.
  • Plowey ED, Cherra SJ, 3rd, Liu YJ, Chu CT (2008) Role of autophagy in G2019S-LRRK2-associated neurite short­ening in differentiated SH-SY5Y cells. J Neurochem. 105, 1048-1056.
  • Plun-Favreau H, Klupsch K, Moisoi N, Gandhi S, Kjaer S, Frith D, Harvey K, Deas E, Harvey RJ, McDonald N, Wood NW, Martins LM, Downward J (2007) The mito- chondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1. Nat Cell Biol 9: 1243­1252.
  • Polymeropoulos MH, Lavedan C, Leroy E, Ide SE, Dehejia A, Dutra A, Pike B, Root H, Rubenstein J, Boyer R, Stenroos ES, Chandrasekharappa S, Athanassiadou A, Papapetropoulos T, Johnson WG, Lazzarini AM, Duvoisin RC, Di Iorio G, Golbe LI, Nussbaum RL (1997) Mutation in the a-synuclein gene identified in families with Parkinson's disease. Science 276: 2045-2047.
  • Pridgeon JW, Olzmann JA, Chin LS, Li L (2007) PINK1 protects against oxidative stress by phosphorylating mito­chondrial chaperone TRAP1. PLoS Biol 5: e172.
  • Qiu Q, Zheng Z, Chang L, Zhao YS, Tan C, Dandekar A, Zhang Z, Lin Z, Gui M, Li X, Zhang T, Kong Q, Li H, Chen S, Chen A, Kaufman RJ, Yang WL, Lin HK, Zhang D, Perlman H, Thorp E, Zhang K, Fang D (2013) Toll-like receptor-mediated IREla activation as a therapeutic target for inflammatory arthritis. EMBO J 32: 2477-2490.
  • Radke S, Chander H, Schafer P, Meiss G, Kruger R, Schulz JB, Germain D (2008) Mitochondrial protein quality con­trol by the proteasome involves ubiquitination and the protease Omi. J Biol Chem 283: 12681-12685.
  • Rajan RS, Tsumoto K, Tokunaga M, Tokunaga H, Kita Y, Arakawa T (2011) Chemical and pharmacological chap- erones: application for recombinant protein production and protein folding diseases. Curr Med Chem 18: 1-15.
  • Rakovic A, Grunewald A, Voges L, Hofmann S, Orolicki S, Lohmann K, Klein C (2011) PINK1-Interacting Proteins: Proteomic Analysis of Overexpressed PINK1. Parkinsons Dis 2011: 153979.
  • Rao RV, Bredesen DE (2004) Misfolded proteins, endoplas- mic reticulum stress and neurodegeneration. Curr Opin Cell Biol 16: 653-662.
  • Rapoport TA (2007) Protein translocation across the eukary- otic endoplasmic reticulum and bacterial plasma mem­branes. Nature 450: 663-669.
  • Raven JF, Baltzis D, Wang S, Mounir Z, Papadakis AI, Gao HQ, Koromilas AE (2008) PKR and PKR-like endoplas- mic reticulum kinase induce the proteasome-dependent degradation of cyclin D1 via a mechanism requiring eukaryotic initiation factor 2a phosphorylation. J Biol Chem 283: 3097-3108.
  • Romero-Ramirez L, Cao H, Nelson D, Hammond E, Lee AH, Yoshida H, Mori K, Glimcher LH, Denko NC, Giaccia AJ, Le QT, Koong AC (2004) XBP1 is essential for survival under hypoxic conditions and is required for tumor growth. Cancer Res 64: 5943-5947.
  • Romisch K (2004) A cure for traffic jams: small molecule chaperones in the endoplasmic reticulum. Traffic 5: 815-820.
  • Roybal CN, Yang S, Sun CW, Hurtado D, Vander Jagt DL, Townes TM, Abcouwer SF (2004) Homocysteine increas­es the expression of vascular endothelial growth factor by a mechanism involving endoplasmic reticulum stress and transcription factor ATF4. J Biol Chem 279: 14844­14852.
  • Rutkevich LA, Williams DB (2011) Participation of lectin chaperones and thiol oxidoreductases in protein folding within the endoplasmic reticulum. Curr Opin Cell Biol 23: 157-166.
  • Rutkowski DT, Kaufman RJ (2004) A trip to the ER: coping with stress. Trends Cell Biol 14: 20-28.
  • Rutkowski DT, Wu J, Back SH, Callaghan MU, Ferris SP, Iqbal J, Clark R, Miao H, Hassler JR, Fornek J, Katze MG, Hussain MM, Song B, Swathirajan J, Wang J, Yau GD, Kaufman RJ (2008) UPR pathways combine to pre­vent hepatic steatosis caused by ER stress-mediated sup­pression of transcriptional master regulators. Dev Cell 15: 829-840.
  • Ryu EJ, Harding HP, Angelastro JM, Vitolo OV, Ron D, Greene LA (2002) Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease. J Neurosci 22: 10690-10698.
  • Saha S, Guillily MD, Ferree A, Lanceta J, Chan D, Ghosh J, Hsu CH, Segal L, Raghavan K, Matsumoto K, Hisamoto N, Kuwahara T, Iwatsubo T, Moore L, Goldstein L, Cookson M, Wolozin B (2009) LRRK2 modulates vul­nerability to mitochondrial dysfunction in Caenorhabditis elegans. J Neurosci 29: 9210-9218.
  • Samann J, Hegermann J, von Gromoff E, Eimer S, Baumeister R, Schmidt E (2009) Caenorhabditits elegans LRK-1 and PINK-1 act antagonistically in stress response and neurite outgrowth. J Biol Chem 284: 16482-16491.
  • Satake W, Nakabayashi Y, Mizuta I, Hirota Y, Ito C, Kubo M, Kawaguchi T, Tsunoda T, Watanabe M, Takeda A, Tomiyama H, Nakashima K, Hasegawa K, Obata F, Yoshikawa T, Kawakami H, Sakoda S, Yamamoto M, Hattori N, Murata M, Nakamura Y, Toda T (2009)
  • Genome-wide association study identifies common vari­ants at four loci as genetic risk factors for Parkinson's disease. Nat Genet 41: 1303-1307.
  • Sawada N, Yao J, Hiramatsu N, Hayakawa K, Araki I, Takeda M, Kitamura M (2008) Involvement of hypoxia- triggered endoplasmic reticulum stress in outlet obstruc­tion-induced apoptosis in the urinary bladder. Lab Invest 88: 553-563.
  • Schapira AH, Jenner P (2011) Etiology and pathogenesis of Parkinson's disease. Mov Disord 26: 1049-1055.
  • Schroder M, Kaufman RJ (2005) ER stress and the unfolded protein response. Mutat Res 569: 29-63.
  • Selkoe DJ (2003) Folding proteins in fatal ways. Nature 426: 900-904.
  • Selvaraj S, Sun Y, Watt JA, Wang S, Lei S, Birnbaumer L, Singh BB (2012) Neurotoxin-induced ER stress in mouse dopaminergic neurons involves downregulation of TRPC1 and inhibition of AKT/mTOR signaling. J Clin Invest 122: 1354-1367.
  • Sen D, Balakrishnan B, Jayandharan GR (2014) Cellular unfolded protein response against viruses used in gene therapy. Front Microbiol 5: 250.
  • Shamu CE, Walter P (1996) Oligomerization and phospho­rylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J 15: 3028-3039.
  • Sharon R, Bar-Joseph I, Frosch MP, Walsh DM, Hamilton JA, Selkoe DJ (2003) The formation of highly soluble oligomers of a-synuclein is regulated by fatty acids and enhanced in Parkinson's disease Neuron. 37: 583-595.
  • Shavali S, Brown-Borg HM, Ebadi M, Porter J (2008) Mitochondrial localization of a-synuclein protein in a-synuclein overexpressing cells. Neurosci Lett 439: 125-128.
  • Shimura H, Hattori N, Kubo S, Mizuno Y, Asakawa S, Minoshima S, Shimizu N, Iwai K, Chiba T, Tanaka K, Suzuki T (2000) Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat Genet 25: 302­305.
  • Sidhu A, Wersinger C, Moussa CE, Vernier P (2004) The role of a-synuclein in both neuroprotection and neurode­generation. Ann N Y Acad Sci 1035: 250-270.
  • Silva RM, Ries V, Oo TF, Yarygina O, Jackson-Lewis V, Ryu EJ, Lu PD, Marciniak SJ, Ron D, Przedborski S, Kholodilov N, Greene LA, Burke RE (2005) CHOP/ GADD153 is a mediator of apoptotic death in substantia nigra dopamine neurons in an in vivo neurotoxin model of parkinsonism. J Neurochem 95: 974-986.
  • Singleton AB, Farrer M, Johnson J, Singleton A, Hague S, Kachergus J, Hulihan M, Peuralinna T, Dutra A, Nussbaum R, Lincoln S, Crawley A, Hanson M, Maraganore D, Adler C, Cookson MR, Muenter M, Baptista M, Miller D, Blancato J, Hardy J, Gwinn-Hardy K (2003) a-Synuclein locus triplication causes Parkinson's disease. Science 302: 841.
  • Smith MH, Ploegh HL, Weissman JS (2011). Road to ruin: targeting proteins for degradation in the endoplasmic reticulum. Science 334: 1086-1090.
  • Smith WW, Jiang H, Pei Z, Tanaka Y, Morita H, Sawa A, Dawson VL, Dawson TM, Ross CA (2005) Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant a-synuclein-induced toxicity. Hum Mol Genet 14: 3801-3811.
  • Soto C (2003) Unfolding the role of protein misfolding in neurodegenerative diseases. Nat Rev Neurosci 4: 49-60.
  • Spillantini MG, Schmidt ML, Lee VM, Trojanowski JQ, Jakes R, Goedert M (1997): A-synuclein in Lewy bodies. Nature 388: 839-840.
  • Stefanis L, Larsen KE, Rideout HJ, Sulzer D, Greene LA (2001) Expression of A53T mutant but not wild-type a-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dop- amine release, and autophagic cell death. J Neurosci 21: 9549-9560.
  • Strauss KM, Martins LM, Plun-Favreau H, Marx FP, Kautzmann S, Berg D, Gasser T, Wszolek Z, Muller T, Bornemann A, Wolburg H, Downward J, Riess O, Schulz JB, Kruger R (2005) Loss of function mutations in the gene encoding Omi/HtrA2 in Parkinson's disease. Hum Mol Genet: 14: 2099-2111.
  • Stutzbach LD, Xie SX, Naj AC, Albin R, Gilman S, Lee VM, Trojanowski JQ, Devlin B, Schellenberg GD (2013) The unfolded protein response is activated in disease-affected brain regions in progressive supranuclear palsy and Alzheimer's disease. Acta Neuropathol Commun 1: 31-43.
  • Sugeno N, Takeda A, Hasegawa T, Kobayashi M, Kikuchi A, Mori F, Wakabayashi K, Itoyama Y (2008) Serine 129 phosphorylation of a-synuclein induces unfolded protein response-mediated cell death. J Biol Chem 283: 23179­23188.
  • Sun X, Liu J, Crary JF, Malagelada C, Sulzer D, Greene LA, Levy OA (2013) ATF4 protects against neuronal death in cellular Parkinson's disease models by maintaining levels of parkin. J Neurosci 33: 2398-2407.
  • Tabas I, Ron D (2011) Integrating the mechanisms of apop- tosis induced by endoplasmic reticulum stress. Nat Cell Biol 13: 184-190.
  • Tanaka Y, Engelender S, Igarashi S, Rao RK, Wanner T, Tanzi RE, Sawa A, V LD, Dawson TM, Ross CA (2001) Inducible expression of mutant a-synuclein decreases proteasome activity and increases sensitivity to mito­chondria-dependent apoptosis. Hum Mol Genet 10: 919­926.
  • Taylor JP, Hardy J, Fischbeck KH (2002) Toxic proteins in neurodegenerative disease. Science: 296: 1991-1995.
  • Tokuda T, Qureshi MM, Ardah MT, Varghese S, Shehab SA, Kasai T, Ishigami N, Tamaoka A, Nakagawa M, El-Agnaf OM (2010) Detection of elevated levels of a-synuclein oligomers in CSF from patients with Parkinson disease. Neurology 75: 1766-1772.
  • Tong Y, Pisani A, Martella G, Karouani M, Yamaguchi H, Pothos EN, Shen J (2009) R1441C mutation in LRRK2 impairs dopaminergic neurotransmission in mice. Proc Natl Acad Sci U S A 106: 14622-14627.
  • Tyedmers J, Mogk A, Bukau B (2010) Cellular strategies for controlling protein aggregation. Nat Rev Mol Cell Biol 11: 777-788.
  • Ullman E, Fan Y, Stawowczyk M, Chen HM, Yue Z, Zong WX (2008) Autophagy promotes necrosis in apoptosis- deficient cells in response to ER stress. Cell Death Differ 15: 422-425.
  • Ungerstedt U, Ljungberg T, Steg G (1974) Behavioral, physiological, and neurochemical changes after 6-hy- droxydopamine-induced degeneration of the nigro-striatal dopamine neurons. Adv Neurol: 5: 421-426.
  • Urano F, Wang X, Bertolotti A, Zhang Y, Chung P, Harding HP, Ron D (2000) Coupling of stress in the ER to activa­tion of JNK protein kinases by transmembrane protein kinase IRE1. Science 287: 664-666.
  • Valdes P, Mercado G, Vidal RL, Molina C, Parsons G, Court FA, Martinez A, Galleguillos D, Armentano D, Schneider BL, Hetz C (2014) Control of dopaminergic neuron sur­vival by the unfolded protein response transcription fac­tor XBP1. Proc Natl Acad Sci U S A 111: 6804-6809.
  • Varshney A, Ehrlich BE (2003) Intracellular Ca2+ signaling and human disease: the hunt begins with Huntington's. Neuron 39: 195-197.
  • Vattem KM, Wek RC (2004) Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells. Proc Natl Acad Sci U S A 101: 11269-11274.
  • Viana RJ, Nunes AF, Rodrigues CM (2012) Endoplasmic reticulum enrollment in Alzheimer's disease. Mol Neurobiol 46: 522-534.
  • Walkinshaw G, Waters CM (1994) Neurotoxin-induced cell death in neuronal PC12 cells is mediated by induction of apoptosis. Neuroscience 63: 975-987.
  • Wang L, Popko B, Roos RP (2010) The unfolded protein response in familial amyotrophic lateral sclerosis. Hum Mol Genet 20: 1008-1015.
  • Wang W, Perovic I, Chittuluru J, Kaganovich A, Nguyen LT, Liao J, Auclair JR, Johnson D, Landeru A, Simorellis AK, Ju S, Cookson MR, Asturias FJ, Agar JN, Webb BN, Kang C, Ringe D, Petsko GA, Pochapsky TC, Hoang QQ (2011) A soluble a-synuclein construct forms a dynamic tetramer. Proc Natl Acad Sci U S A 108: 17797-17802.
  • Wang XZ, Lawson B, Brewer JW, Zinszner H, Sanjay A, Mi LJ, Boorstein R, Kreibich G, Hendershot LM, Ron D (1996) Signals from the stressed endoplasmic reticulum induce C/EBP-homologous protein (CHOP/GADD153). Mol Cell Biol 16: 4273-4280.
  • Wider C, Foroud T, Wszolek ZK (2010) Clinical implica­tions of gene discovery in Parkinson's disease and parkin­sonism. Mov Disord 25 Suppl 1: S15-20.
  • Xu C, Bailly-Maitre B, Reed JC (2005) Endoplasmic reticu­lum stress: cell life and death decisions. J Clin Invest 115: 2656-2664.
  • Yamasaki S, Yagishita N, Tsuchimochi K, Nishioka K, Nakajima T (2005) Rheumatoid arthritis as a hyper-endo- plasmic-reticulum-associated degradation disease. Arthritis Res Ther 7: 181-186.
  • Ye J, Rawson RB, Komuro R, Chen X, Dave UP, Prywes R, Brown MS, Goldstein JL (2000) ER stress induces cleav­age of membrane-bound ATF6 by the same proteases that process SREBPs. Mol Cell 6: 1355-1364.
  • Yorimitsu T, Nair U, Yang Z, Klionsky DJ (2006) Endoplasmic reticulum stress triggers autophagy. J Biol Chem281:30299-30304.
  • Yoshida H, Matsui T, Yamamoto A, Okada T, Mori K (2001) XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcrip­tion factor. Cell 107: 881-891.
  • Yuan H, Zhang ZW, Liang LW, Shen Q, Wang XD, Ren SM, Ma HJ, Jiao SJ, Liu P (2010) Treatment strategies for Parkinson's disease. Neurosci Bull 26: 66-76.
  • Yuan Y, Cao P, Smith MA, Kramp K, Huang Y, Hisamoto N, Matsumoto K, Hatzoglou M, Jin H, Feng Z (2011)
  • Dysregulated LRRK2 signaling in response to endoplas- mic reticulum stress leads to dopaminergic neuron degen­eration in C. elegans. PLoS One 6: e22354.
  • Zarranz JJ, Alegre J, Gomez-Esteban JC, Lezcano E, Ros R, Ampuero I, Vidal L, Hoenicka J, Rodriguez O, Atares B, Llorens V, Gomez Tortosa E, del Ser T, Munoz DG, de Yebenes JG (2004) The new mutation, E46K, of a-synuclein causes Parkinson and Lewy body dementia. Ann Neurol 55: 164-173.
  • Zhang K, Kaufman RJ (2006) The unfolded protein response: a stress signaling pathway critical for health and disease. Neurology 66: S102-109.
  • Zhang L, Wang A (2012) Virus-induced ER stress and the unfolded protein response. Front Plant Sci 3: 293.
  • Zhang LH, Zhang X (2010) Roles of GRP78 in physiology and cancer. J Cell Biochem 110: 1299-1305.
  • Zhao Q, Wang J, Levichkin IV, Stasinopoulos S, Ryan MT, Hoogenraad NJ (2002) A mitochondrial specific stress response in mammalian cells. EMBO J 21: 4411-4419.
  • Zhou D, Palam LR, Jiang L, Narasimhan J, Staschke KA, Wek RC (2008) Phosphorylation of eIF2 directs ATF5 translational control in response to diverse stress condi­tions. J Biol Chem 283: 7064-7073.
  • Zhu J, Chu CT (2010) Mitochondrial dysfunction in Parkinson's disease. J Alzheimers Dis 20 Suppl 2: S325- 334.
  • Zimprich A, Muller-Myhsok B, Farrer M, Leitner P, Sharma M, Hulihan M, Lockhart P, Strongosky A, Kachergus J, Calne DB, Stoessl J, Uitti RJ, Pfeiffer RF, Trenkwalder C, Homann N, Ott E, Wenzel K, Asmus F, Hardy J, Wszolek Z, Gasser T (2004) The PARK8 locus in autosomal dominant parkinsonism: confirmation of linkage and fur­ther delineation of the disease-containing interval. Am J Hum Genet: 74: 11-19.
  • Zinszner H, Kuroda M, Wang X, Batchvarova N, Lightfoot RT, Remotti H, Stevens JL, Ron D (1998) CHOP is impli­cated in programmed cell death in response to impaired function of the endoplasmic reticulum. Genes Dev 12: 982-995.

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