메뉴 건너뛰기




Volumn 111, Issue 18, 2014, Pages 6804-6809

Control of dopaminergic neuron survival by the unfolded protein response transcription factor XBP1

Author keywords

[No Author keywords available]

Indexed keywords

NEUROTOXIN; OXIDOPAMINE; PARVOVIRUS VECTOR; X BOX BINDING PROTEIN 1;

EID: 84899844505     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1321845111     Document Type: Article
Times cited : (175)

References (52)
  • 1
    • 84861559058 scopus 로고    scopus 로고
    • Transmissible proteins: Expanding the prion heresy
    • Soto C (2012) Transmissible proteins: Expanding the prion heresy. Cell 149(5):968-977.
    • (2012) Cell , vol.149 , Issue.5 , pp. 968-977
    • Soto, C.1
  • 2
    • 33745919520 scopus 로고    scopus 로고
    • Epidemiology of Parkinson's disease
    • de Lau LM, Breteler MM (2006) Epidemiology of Parkinson's disease. Lancet Neurol 5(6):525-535.
    • (2006) Lancet Neurol , vol.5 , Issue.6 , pp. 525-535
    • De Lau, L.M.1    Breteler, M.M.2
  • 3
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: Mechanisms and models
    • Dauer W, Przedborski S (2003) Parkinson's disease: Mechanisms and models. Neuron 39(6):889-909.
    • (2003) Neuron , vol.39 , Issue.6 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 4
    • 79952451427 scopus 로고    scopus 로고
    • Mitophagy: The latest problem for Parkinson's disease
    • Vives-Bauza C, Przedborski S (2011) Mitophagy: The latest problem for Parkinson's disease. Trends Mol Med 17(3):158-165.
    • (2011) Trends Mol Med , vol.17 , Issue.3 , pp. 158-165
    • Vives-Bauza, C.1    Przedborski, S.2
  • 6
    • 79959500244 scopus 로고    scopus 로고
    • Mitochondria, calcium, and endoplasmic reticulum stress in Parkinson's disease
    • Calì T, Ottolini D, Brini M (2011) Mitochondria, calcium, and endoplasmic reticulum stress in Parkinson's disease. Biofactors 37(3):228-240.
    • (2011) Biofactors , vol.37 , Issue.3 , pp. 228-240
    • Calì, T.1    Ottolini, D.2    Brini, M.3
  • 7
    • 84875259777 scopus 로고    scopus 로고
    • An ERcentric view of Parkinson's disease
    • Mercado G, Valdés P, Hetz C (2013) An ERcentric view of Parkinson's disease. Trends Mol Med 19(3):165-175.
    • (2013) Trends Mol Med , vol.19 , Issue.3 , pp. 165-175
    • Mercado, G.1    Valdés, P.2    Hetz, C.3
  • 8
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: Controlling cell fate decisions under ER stress and beyond
    • Hetz C (2012) The unfolded protein response: Controlling cell fate decisions under ER stress and beyond. Nat Rev Mol Cell Biol 13(2):89-102.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , Issue.2 , pp. 89-102
    • Hetz, C.1
  • 9
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter P, Ron D (2011) The unfolded protein response: From stress pathway to homeostatic regulation. Science 334(6059):1081-1086.
    • (2011) Science , vol.334 , Issue.6059 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 10
    • 79952264011 scopus 로고    scopus 로고
    • Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
    • Tabas I Ron D (2011 Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress Nat Cell Biol 13 3 184-190
    • (2011) Nat Cell Biol , vol.13 , Issue.3 , pp. 184-190
    • Tabas, I.1    Ron, D.2
  • 12
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • Calfon M, et al. (2002) IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 415(6867):92-96.
    • (2002) Nature , vol.415 , Issue.6867 , pp. 92-96
    • Calfon, M.1
  • 13
    • 0037083755 scopus 로고    scopus 로고
    • IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein respon se
    • Lee K, et al. (2002) IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein respon se. Genes Dev 16(4):452-466.
    • (2002) Genes Dev , vol.16 , Issue.4 , pp. 452-466
    • Lee, K.1
  • 14
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly act ive transcription factor
    • 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 act ive transcription factor. Cell 107(7):881-891.
    • (2001) Cell , vol.107 , Issue.7 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 15
    • 80054722420 scopus 로고    scopus 로고
    • The unfolded protein response: Integrating stress signals through the stress sensor IRE1
    • Hetz C, Martinon F, Rodriguez D, Glimcher LH (2011) The unfolded protein response: Integrating stress signals through the stress sensor IRE1. Physiol Rev 91(4):1219-1243.
    • (2011) Physiol Rev , vol.91 , Issue.4 , pp. 1219-1243
    • Hetz, C.1    Martinon, F.2    Rodriguez, D.3    Glimcher, L.H.4
  • 16
    • 84863740827 scopus 로고    scopus 로고
    • The impact of the unfolded protein response on human disease
    • Wang S, Kaufman RJ (2012) The impact of the unfolded protein response on human disease. J Cell Biol 197(7):857-867.
    • (2012) J Cell Biol , vol.197 , Issue.7 , pp. 857-867
    • Wang, S.1    Kaufman, R.J.2
  • 17
    • 84891273860 scopus 로고    scopus 로고
    • Role of the unfolded protein response in organ physiology: Lessons from mouse models
    • Corn ejo VH, Pihán P, Vidal RL, Hetz C (2013) Role of the unfolded protein response in organ physiology: Lessons from mouse models. IUBMB Life 65(12):962-975.
    • (2013) IUBMB Life , vol.65 , Issue.12 , pp. 962-975
    • Corn Ejo, V.H.1    Pihán, P.2    Vidal, R.L.3    Hetz, C.4
  • 18
    • 84897094564 scopus 로고    scopus 로고
    • Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases
    • Hetz C, Mollereau B (2014) Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases. Nat Rev Neurosci 15(4):233-249.
    • (2014) Nat Rev Neurosci , vol.15 , Issue.4 , pp. 233-249
    • Hetz, C.1    Mollereau, B.2
  • 19
    • 84870838478 scopus 로고    scopus 로고
    • End oplasmic reticulum dysfunction in neurological disease
    • Roussel BD, et al. (2013) End oplasmic reticulum dysfunction in neurological disease. Lancet Neurol 12(1):105-118.
    • (2013) Lancet Neurol , vol.12 , Issue.1 , pp. 105-118
    • Roussel, B.D.1
  • 20
    • 4444237848 scopus 로고    scopus 로고
    • Identification of the protein disulfide isomerase family member PDIp in experimental Parkinson's disease and Lewy body pathology
    • Conn KJ, et al. (2004) Identification of the protein disulfide isomerase family member PDIp in experimental Parkinson's disease and Lewy body pathology. Brain Res 1022(1-2): 164-172.
    • (2004) Brain Res , vol.1022 , Issue.1-2 , pp. 164-172
    • Conn, K.J.1
  • 21
    • 70350043611 scopus 로고    scopus 로고
    • Homocysteine-induced endoplasmic reticulum protein (herp) is up-regulated in parkinson ian substantia nigra and present in the core of Lewy bodies
    • Slodzinski H, et al. (2009) Homocysteine-induced endoplasmic reticulum protein (herp) is up-regulated in parkinson ian substantia nigra and present in the core of Lewy bodies. Clin Neuropathol 28(5):333-343.
    • (2009) Clin Neuropathol , vol.28 , Issue.5 , pp. 333-343
    • Slodzinski, H.1
  • 22
    • 33846605587 scopus 로고    scopus 로고
    • Activation of the unfolded protein response in Parkinson's disease
    • Hoozemans JJ, et al. (2007) Activation of the unfolded protein response in Parkinson's disease. Biochem Biophys Res Commun 354(3):707-711.
    • (2007) Biochem Biophys Res Commun , vol.354 , Issue.3 , pp. 707-711
    • Hoozemans, J.J.1
  • 23
    • 84863230467 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress is important for the manifestations of -synucleinopathy in vivo
    • Colla E, et al. (2012) Endoplasmic reticulum stress is important for the manifestations of -synucleinopathy in vivo. J Neurosci 32(10):3306-3320.
    • (2012) J Neurosci , vol.32 , Issue.10 , pp. 3306-3320
    • Colla, E.1
  • 24
    • 84863229691 scopus 로고    scopus 로고
    • Accumulation of toxic -synuclein oligomer within endoplasmic reticulum occurs in -synucleinopathy in vivo
    • Colla E, et al. (2012) Accumulation of toxic -synuclein oligomer within endoplasmic reticulum occurs in -synucleinopathy in vivo. J Neurosci 32(10):3301-3305.
    • (2012) J Neurosci , vol.32 , Issue.10 , pp. 3301-3305
    • Colla, E.1
  • 25
    • 84888070126 scopus 로고    scopus 로고
    • Identification and rescue of -synuclein toxicity in Parkinson patient-derived neurons
    • C hung CY, et al. (2013) Identification and rescue of -synuclein toxicity in Parkinson patient-derived neurons. Science 342(6161):983-987.
    • (2013) Science , vol.342 , Issue.6161 , pp. 983-987
    • Hung, C.Y.C.1
  • 26
    • 0038143287 scopus 로고    scopus 로고
    • Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons
    • Holtz WA, O'Malley KL (2003) Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons. J Biol Chem 278(21):19367-19377.
    • (2003) J Biol Chem , vol.278 , Issue.21 , pp. 19367-19377
    • Holtz, W.A.1    O'Malley, K.L.2
  • 27
    • 0037114971 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease
    • Ryu EJ, et al. (2002) Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease. J Neurosci 22(24):10690-10698.
    • (2002) J Neurosci , vol.22 , Issue.24 , pp. 10690-10698
    • Ryu, E.J.1
  • 28
    • 63349104307 scopus 로고    scopus 로고
    • Protective effect against Parkinson's disease-related insults through the activation of XBP1
    • Sado M, et al. (2009) Protective effect against Parkinson's disease-related insults through the activation of XBP1. Brain Res 1257:16-24.
    • (2009) Brain Res , vol.1257 , pp. 16-24
    • Sado, M.1
  • 29
    • 28244466782 scopus 로고    scopus 로고
    • CHOP/GADD153 is a mediator of apoptotic death in substantia nigra dopamine neurons in an in vivo neurotoxin model of parkinsonism
    • Silva RM, et al. (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(4):974-986.
    • (2005) J Neurochem , vol.95 , Issue.4 , pp. 974-986
    • Silva, R.M.1
  • 30
    • 79953148080 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress sensor, ATF6, protects against neurotoxin-induced dopaminergic neuronal death
    • Egawa N, et al. (2011) The endoplasmic reticulum stress sensor, ATF6, protects against neurotoxin-induced dopaminergic neuronal death. J Biol Chem 286(10): 7947-7957.
    • (2011) J Biol Chem , vol.286 , Issue.10 , pp. 7947-7957
    • Egawa, N.1
  • 31
    • 84859717205 scopus 로고    scopus 로고
    • Neurotoxin-induced ER stress in mouse dopaminergic neurons involves down-regulation of TRPC1 and inhibition of AKT/mTOR signaling
    • Selvaraj S, et al. (2012) Neurotoxin-induced ER stress in mouse dopaminergic neurons involves down-regulation of TRPC1 and inhibition of AKT/mTOR signaling. J Clin Invest 122(4):1354-1367.
    • (2012) J Clin Invest , vol.122 , Issue.4 , pp. 1354-1367
    • Selvaraj, S.1
  • 32
    • 38649108109 scopus 로고    scopus 로고
    • Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis
    • Hetz C, et al. (2008) Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis. Proc Natl Acad Sci USA 105(2):757-762.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.2 , pp. 757-762
    • Hetz, C.1
  • 33
    • 45849137877 scopus 로고    scopus 로고
    • Regulation of hepatic lipogenesis by the transcription factor XBP1
    • Lee AH , Scapa EF, Cohen DE, Glimcher LH (2008) Regulation of hepatic lipogenesis by the transcription factor XBP1. Science 320(5882):1492-1496.
    • (2008) Science , vol.320 , Issue.5882 , pp. 1492-1496
    • Lee, A.H.1    Scapa, E.F.2    Cabelli, D.E.3    Glimcher, L.H.4
  • 34
    • 50249086073 scopus 로고    scopus 로고
    • XBP1 links ER stress to intestinal inflammation and confers genetic risk for human inflammatory bowel disease
    • Kaser A, et al. (2008) XBP1 links ER stress to intestinal inflammation and confers genetic risk for human inflammatory bowel disease. Cell 134(5):743-756.
    • (2008) Cell , vol.134 , Issue.5 , pp. 743-756
    • Kaser, A.1
  • 35
    • 84860471873 scopus 로고    scopus 로고
    • Targeting the UPR transcription factor XBP1 protects against Huntington's disease through the regulation of FoxO1 and autophagy
    • Vidal RL, et al. (2012) Targeting the UPR transcription factor XBP1 protects against Huntington's disease through the regulation of FoxO1 and autophagy. Hum Mol Genet 21(10):2245-2262.
    • (2012) Hum Mol Genet , vol.21 , Issue.10 , pp. 2245-2262
    • Vidal, R.L.1
  • 36
    • 84857852395 scopus 로고    scopus 로고
    • Activation of the unfolded protein response enhances motor recovery after spinal cord injury
    • Valenzuela V, et al. (2012) Activation of the unfolded protein response enhances motor recovery after spinal cord injury. Cell Death Dis 3:e272.
    • (2012) Cell Death Dis , vol.3
    • Valenzuela, V.1
  • 37
    • 70349627027 scopus 로고    scopus 로고
    • XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy
    • Hetz C, et al. (2009) XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy. Genes Dev 23(19):2294-2306.
    • (2009) Genes Dev , vol.23 , Issue.19 , pp. 2294-2306
    • Hetz, C.1
  • 38
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • Kroemer G, Marino G, Levine B (2010) Autophagy and the integrated stress response. Mol Cell 40(2):280-293.
    • (2010) Mol Cell , vol.40 , Issue.2 , pp. 280-293
    • Kroemer, G.1    Marino, G.2    Levine, B.3
  • 39
    • 0037118259 scopus 로고    scopus 로고
    • Neuronal alpha-synucleinopathy with severe movement disorder in mice expressing A53T human alpha-synuclein
    • Giasson BI, et al. (2002) Neuronal alpha-synucleinopathy with severe movement disorder in mice expressing A53T human alpha-synuclein. Neuron 34(4):521-533.
    • (2002) Neuron , vol.34 , Issue.4 , pp. 521-533
    • Giasson, B.I.1
  • 40
    • 84859577308 scopus 로고    scopus 로고
    • AAV-mediated delivery of the transcription factor XBP1s into the striatum reduces mutant Huntingtin aggregation in a mouse model of Huntington's disease
    • Zuleta A, Vida l RL, Armentano D, Parsons G, Hetz C (2012) AAV-mediated delivery of the transcription factor XBP1s into the striatum reduces mutant Huntingtin aggregation in a mouse model of Huntington's disease. Biochem Biophys Res Commun 420(3):558-563.
    • (2012) Biochem Biophys Res Commun , vol.420 , Issue.3 , pp. 558-563
    • Zuleta, A.1    Vida, L.R.L.2    Armentano, D.3    Parsons, G.4    Hetz, C.5
  • 41
    • 84868135034 scopus 로고    scopus 로고
    • ATF6alpha promotes astroglial activation and neuronal survival in a chronic mouse model of Parkinson's disease
    • Hashida K, et al. (2012) ATF6alpha promotes astroglial activation and neuronal survival in a chronic mouse model of Parkinson's disease. PLoS ONE 7(10):e47950.
    • (2012) PLoS ONE , vol.7 , Issue.10
    • Hashida, K.1
  • 42
    • 33751069967 scopus 로고    scopus 로고
    • Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins
    • Rutkowski DT, et al. (2006) Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins. PLoS Biol 4(11):e374.
    • (2006) PLoS Biol , vol.4 , Issue.11
    • Rutkowski, D.T.1
  • 43
    • 65649146419 scopus 로고    scopus 로고
    • ER stress protects from retinal degeneration
    • Mendes CS, et al. (2009) ER stress protects from retinal degeneration. EMBO J 28(9): 1296-1307.
    • (2009) EMBO J , vol.28 , Issue.9 , pp. 1296-1307
    • Mendes, C.S.1
  • 44
    • 77957826835 scopus 로고    scopus 로고
    • Protein misfolding induces hypoxic preconditioning via a subset of the unfolded protein response machinery
    • Mao XR, Crowder CM (2010) Protein misfolding induces hypoxic preconditioning via a subset of the unfolded protein response machinery. Mol Cell Biol 30(21):5033-5042.
    • (2010) Mol Cell Biol , vol.30 , Issue.21 , pp. 5033-5042
    • Mao, X.R.1    Crowder, C.M.2
  • 45
    • 79953001199 scopus 로고    scopus 로고
    • Preconditioning with endoplasmic reticulum stress mitigates retinal endothelial inflammation via activation of X-box binding protein
    • Li J, Wang JJ, Zhang SX (2011) Preconditioning with endoplasmic reticulum stress mitigates retinal endothelial inflammation via activation of X-box binding protein J Biol Chem 286(6):4912-4921.
    • (2011) J Biol Chem , vol.286 , Issue.6 , pp. 4912-4921
    • Li, J.1    Wang, J.J.2    Zhang, S.X.3
  • 46
    • 79955543079 scopus 로고    scopus 로고
    • Cardioprotection by endoplasmic reticulum stress-induced autophagy
    • Petrovski G, et al. (2011) Cardioprotection by endoplasmic reticulum stress-induced autophagy. Antioxid Redox Signal 14(11):2191-2200.
    • (2011) Antioxid Redox Signal , vol.14 , Issue.11 , pp. 2191-2200
    • Petrovski, G.1
  • 47
    • 84864866226 scopus 로고    scopus 로고
    • Hormesis: Protecting neurons against cellular stress in Parkinson disease
    • Matus S, Castillo K, Hetz C (2012) Hormesis: Protecting neurons against cellular stress in Parkinson disease. Autophagy 8(6):997-1001.
    • (2012) Autophagy , vol.8 , Issue.6 , pp. 997-1001
    • Matus, S.1    Castillo, K.2    Hetz, C.3
  • 48
    • 84862303631 scopus 로고    scopus 로고
    • ER stress inhibits neuronal death by promoting autophagy
    • Fouillet A, et al. (2012) ER stress inhibits neuronal death by promoting autophagy. Autophagy 8(6):915-926.
    • (2012) Autophagy , vol.8 , Issue.6 , pp. 915-926
    • Fouillet, A.1
  • 49
    • 84883387793 scopus 로고    scopus 로고
    • Targeting the unfolded protein response in disease
    • Hetz C, Chevet E, Harding HP (2013) Targeting the unfolded protein response in disease. Nat Rev Drug Discov 12(9):703-719.
    • (2013) Nat Rev Drug Discov , vol.12 , Issue.9 , pp. 703-719
    • Hetz, C.1    Chevet, E.2    Harding, H.P.3
  • 51
    • 0034328476 scopus 로고    scopus 로고
    • Scaleable chromatographic purification process for recombinant adeno-associated virus (rAAV
    • O'Riordan CR, Lachapelle AL, Vincent KA, Wadsworth SC (2000) Scaleable chromatographic purification process for recombinant adeno-associated virus (rAAV). J Gene Med 2(6):444-454.
    • (2000) J Gene Med , vol.2 , Issue.6 , pp. 444-454
    • O'Riordan, C.R.1    Lachapelle, A.L.2    Vincent, K.A.3    Wadsworth, S.C.4
  • 52
    • 84861188701 scopus 로고    scopus 로고
    • BH3-only proteins are part of a regulatory network that control the sustained signalling of the unfolded protein response sensor IRE1
    • Rodriguez DA, et al. (2012) BH3-only proteins are part of a regulatory network that control the sustained signalling of the unfolded protein response sensor IRE1. EMBO J 31(10):2322-2335.
    • (2012) EMBO J , vol.31 , Issue.10 , pp. 2322-2335
    • Rodriguez, D.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.