The ubiquitin-proteasome system in spongiform degenerative disorders

Biochimica et Biophysica Acta - Molecular Basis of Disease

Volumn 1782, Issue 12, 2008, Pages 700-712

  Whatley, Brandi R ^a   Li, Lian ^a   Chin, Lih Shen ^a  

^a EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

melanocyte stimulating hormone; MSH; acquired immune deficiency syndrome; AD; Agouti related protein; AgRP; AIDS; Alzheimer's disease; amyloid precursor protein; APP; ASPA; aspartoacylase gene; Atrn; attractin; Autophagy; bovine spongiform encephalopathy; BSE; Canavan's spongiform leukodystrophy; CD; cellular prion protein; CJD; Creutzfeldt Jakob disease; CYTB; cytochrome b; deubiquitinating enzyme; diffuse Lewy body disease; DLBD; DUB; electron microscopy; electron transport chain; EM; Endocytic trafficking; endosomal sorting complex required for transport; ERK; ESCRT; ETC; extracellular signal related kinase; fatal familial insomnia; FFI; Gerstmann Str ussler Scheinker disease; glycosylphosphatidylinositol; GPI; GSS; hepatocyte growth factor regulated receptor tyrosine kinase substrate; HIV; Hrs; human immunodeficiency virus; ILV; intralumenal vesicle; mahogunin ring finger 1; manganese superoxide dismutase; Mc(1, 3, 4)r; melanocortin (1, 3, 4) receptor; Mgrn1; Moloney murine leukemia virus; MoMuLV; multivesicular body; MVB; N acetyl l aspartate; NAA; NF E2 related factor; Nrf2; Oxidative stress; prion gene; prion protein; PRNP; PrP; PrPC; PrPSc; reactive oxygen species; ROS; scrapie related prion protein; SOD2; transmissible spongiform encephalopathy; Transmissible spongiform encephalopathy (TSE); TSE; Tsg101; tumor susceptibility gene 101; ubiquitin proteasome system; UPS

Indexed keywords

ASPARTOACYLASE; ATTRACTIN; MAHOGUNIN RING FINGER 1; PROTEASOME; RING FINGER PROTEIN; SIGNAL PEPTIDE; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

ACQUIRED IMMUNE DEFICIENCY SYNDROME; ALZHEIMER DISEASE; AUTOSOMAL RECESSIVE INHERITANCE; BRAIN TISSUE; CANAVAN DISEASE; CELL DEATH; CELL FUNCTION; CELL VACUOLE; CENTRAL NERVOUS SYSTEM; CREUTZFELDT JAKOB DISEASE; DIFFUSE LEWY BODY DISEASE; GENE MUTATION; GLIOSIS; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS INFECTION; IMMUNOHISTOCHEMISTRY; IMMUNOREACTIVITY; INTRACELLULAR TRANSPORT; KURU; MOLECULAR MECHANICS; NERVE CELL NECROSIS; NERVE DEGENERATION; NERVOUS TISSUE; NONHUMAN; OXIDATIVE STRESS; PATHOGENESIS; PRION DISEASE; PRIORITY JOURNAL; REVIEW; SIGNAL TRANSDUCTION; UBIQUITINATION;

ANIMALS; HUMANS; NEURODEGENERATIVE DISEASES; PRION DISEASES; PROTEASOME ENDOPEPTIDASE COMPLEX; UBIQUITIN;

AGOUTI; ANIMALIA; BOVINAE; HUMAN IMMUNODEFICIENCY VIRUS; ISLA VISTA VIRUS;

EID: 56449083405     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2008.08.006     Document Type: Review

References (211)

1. Lampert P.W., Gajdusek D.C., and Gibbs J.C.J. Subacute spongiform virus encephalopathies. Scrapie, Kuru and Creutzfeldt-Jakob disease: a review. Am. J. Pathol. 68 (1972) 626-652
2. Masters C.L., and Richardson E.P.J. Subacute spongiform encephalopathy (Creutzfeldt-Jakob disease). The nature and progression of spongiform change. Brain 101 (1978) 333-344
3. Smith T.W., Anwer U., DeGirolami U., and Drachman D.A. Vacuolar change in Alzheimer's disease. Arch. Neurol. 44 (1987) 1225-1228
4. Hansen L.A., Masliah E., Terry R.D., and Mirra S.S. A neuropathological subset of Alzheimer's disease with concomitant Lewy body disease and spongiform change. Acta Neuropathol. 78 (1989) 194-201
5. Liberski P.P., Sikorska B., Bratosiewicz-Wasik J., Carleton Gajdusek D., and Brown P. Neuronal cell death in transmissible spongiform encephalopathies (prion diseases) revisited: from apoptosis to autophagy. Int. J. Biochem. Cell Biol. 36 (2004) 2473-2490
6. Hubbs A.F., Benkovic S.A., Miller D.B., O'Callaghan J.P., Battelli L., Schwegler-Berry D., and Ma Q. Vacuolar leukoencephalopathy with widespread astrogliosis in mice lacking transcription factor Nrf2. Am. J. Pathol. 170 (2007) 2068-2076
7. Melov S., Schneider J.A., Day B.J., Hinerfeld D., Coskun P., Mirra S.S., Crapo J.D., and Wallace D.C. A novel neurological phenotype in mice lacking mitochondrial manganese superoxide dismutase. Nat. Genet. 18 (1998) 159-163
8. Tsukamoto T., Hirano N., Iwasaki Y., Haga S., Terunuma H., and Yamamoto T. Vacuolar degeneration in mice infected with a coronavirus JHM-CC strain. Neurology 40 (1990) 904-910
9. Iseki E., Li F., and Kosaka K. Close relationship between spongiform change and ubiquitin-positive granular structures in diffuse Lewy body disease. J. Neurol. Sci. 146 (1997) 53-57
10. Jendroska K., Hoffmann O., Schelosky L., Lees A.J., Poewe W., and Daniel S.E. Absence of disease related prion protein in neurodegenerative disorders presenting with Parkinson's syndrome. J. Neurol. Neurosurg. Psychiatry 57 (1994) 1249-1251
11. Artigas J., Niedobitek F., Grosse G., Heise W., and Gosztonyi G. Spongiform encephalopathy in AIDS dementia complex: report of five cases. J. Acquir. Immune Defic. Syndr. 2 (1989) 374-381
12. Burns D.K., Risser R.C., and White C.L. The neuropathology of human immunodeficiency virus infection. The Dallas, Texas, experience. Arch. Pathol. Lab. Med. 115 (1991) 1112-1124
13. de la Monte S.M., Moore T., and Tessa H.-W.E. Vacuolar encephalopathy of AIDS. N. Engl. J. Med. 315 (1986) 1549-1550
14. Goldwater P.N., and Paton J.C. Apparent non-involvement of prions in the pathogenesis of spongiform change in HIV-infected brain. J. Neuropathol. Exp. Neurol. 48 (1989) 184-186
15. Rhodes R.H. Histopathology of the central nervous system in the acquired immunodeficiency syndrome. Hum. Pathol. 18 (1987) 636-643
16. Schwenk J., Cruz-Sanchez F., Gosztonyi G., and Cervos-Navarro J. Spongiform encephalopathy in a patient with acquired immune deficiency syndrome (AIDS). Acta Neuropathol. 74 (1987) 389-392
17. Baslow M.H. Canavan's spongiform leukodystrophy: a clinical anatomy of a genetic metabolic CNS disease. J. Mol. Neurosci. 15 (2001) 61-69
18. Jacomy H., and Talbot P.J. Vacuolating encephalitis in mice infected by human coronavirus OC43. Virology 315 (2003) 20-33
19. Raghavan R., Cheney P.D., Raymond L.A., Joag S.V., Stephens E.B., Adany I., Pinson D.M., Li Z., Marcario J.K., Jia F., Wang C., Foresman L., Berman N.E.J., and Narayan O. Morphological correlates of neurological dysfunction in macaques infected with neurovirulent simian immunodeficiency virus. Neuropathol. Appl. Neurobiol. 25 (1999) 285-294
20. Stoica G., Tasca S.I., and Wong P.K.Y. Motor neuronal loss and neurofilament-ubiquitin alteration in MoMuLV-ts1 encephalopathy. Acta Neuropathol. 99 (2000) 238-244
21. Bronson R.T., Donahue L.R., Samples R., Kim J.H., and Naggert J.K. Mice with mutations in the mahogany gene Atrn have cerebral spongiform changes. J. Neuropathol. Exp. Neurol. 60 (2001) 724-730
22. He L., Lu X.-Y., Jolly A.F., Eldridge A.G., Watson S.J., Jackson P.K., Barsh G.S., and Gunn T.M. Spongiform degeneration in mahoganoid mutant mice. Science 299 (2003) 710-712
23. Kitada K., Akimitsu T., Shigematsu Y., Kondo A., Maihara T., Yokoi N., Kuramoto T., Sasa M., and Serikawa T. Accumulation of N-acetyl-l-aspartate in the brain of the tremor rat, a mutant exhibiting absence-like seizure and spongiform degeneration in the central nervous system. J. Neurochem. 74 (2000) 2512-2519
24. Li F.-Y., Cuddon P.A., Song J., Wood S.L., Patterson J.S., Shelton G.D., and Duncan I.D. Canine spongiform leukoencephalomyelopathy is associated with a missense mutation in cytochrome b. Neurobiol. Dis. 21 (2006) 35-42
25. Rehm S., Mehraein P., Anzil A.P., and Deerberg F. A new rat mutant with defective overhairs and spongy degeneration of the central nervous system: clinical and pathologic studies. Lab. Anim. Sci. 32 (1982) 70-73
26. Ironside J., McCardle L., Hayward P., and Bell J. Ubiquitin immunocytochemistry in human spongiform encephalopathies. Neuropathol. Appl. Neurobiol. 19 (1993) 134-140
27. Laszlo L., Lowe J., Self T., Kenward N., Landon M., McBride T., Farquhar C., McConnell I., Brown J., Hope J., and Mayer R.J. Lysosomes as key organelles in the pathogenesis of prion encephalopathies. J. Pathol. 166 (1992) 333-341
28. Weissman A.M. Themes and variations on ubiquitylation. Nat. Rev. Mol. Cell Biol. 2 (2001) 169-178
29. Haglund K., Di Fiore P.P., and Dikic I. Distinct monoubiquitin signals in receptor endocytosis. Trends Biochem. Sci. 28 (2003) 598-604
30. Thrower J.S., Hoffman L., Rechsteiner M., and Pickart C.M. Recognition of the polyubiquitin proteolytic signal. EMBO J. 19 (2000) 94-102
31. Courbard J.-R., Fiore F., Adélaïde J., Borg J.-P., Birnbaum D., and Ollendorf V. Interaction between two ubiquitin-protein isopeptide ligases of different classes, CBLC and AIP4/ITCH. J. Biol. Chem. 277 (2002) 45267-45275
32. Fang S., and Weissman A.M. A field guide to ubiquitylation. Cell. Mol. Life Sci. 61 (2004) 1546-1561
33. Magnifico A., Ettenberg S., Yang C., Mariano J., Tiwari S., Fang S., Lipkowitz S., and Weissman A.M. WW domain HECT E3s target Cbl RING finger E3s for proteasomal degradation. J. Biol. Chem. 278 (2003) 43169-43177
34. Ardley H.C., Scott G.B., Rose S.A., Tan N.G.S., and Robinson P.A. UCH-L1 aggresome formation in response to proteasome impairment indicates a role in inclusion formation in Parkinson's disease. J. Neurochem. 90 (2004) 379-391
35. Chastagner P., Israël A., and Brou C. Itch/AIP4 mediates Deltex degradation through the formation of K29-linked polyubiquitin chains. EMBO Rep. 7 (2006) 1147-1153
36. Hershko A., and Ciechanover A. The ubiquitin system. Annu. Rev. Biochem. 67 (1998) 425-479
37. Olzmann J.A., and Chin L.-S. Parkin-mediated K63-linked polyubiquitination: a signal for targeting misfolded proteins to the aggresome-autophagy pathway. Autophagy 4 (2008) 85-87
38. Rideout H.J., Larsen K.E., Sulzer D., and Stefanis L. Proteasomal inhibition leads to formation of ubiquitin/alpha-synuclein-immunoreactive inclusions in PC12 cells. J. Neurochem. 78 (2001) 899-908
39. Yedidia Y., Horonchik L., Tzaban S., Yanai A., and Taraboulos A. Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein. EMBO J. 20 (2001) 5383-5391
40. Angers A., Ramjaun A.R., and McPherson P.S. The HECT domain ligase Itch ubiquitinates endophilin and localizes to the trans-Golgi network and endosomal system. J. Biol. Chem. 279 (2004) 11471-11479
41. Barriere H., Nemes C., Du K., and Lukacs G.L. Plasticity of polyubiquitin recognition as lysosomal targeting signals by the endosomal sorting machinery. Mol. Biol. Cell 18 (2007) 3952-3965
42. Duan L., Miura Y., Dimri M., Majumder B., Dodge I.L., Reddi A.L., Ghosh A., Fernandes N., Zhou P., Mullane-Robinson K., Rao N., Donoghue S., Rogers R.A., Bowtell D., Naramura M., Gu H., Band V., and Band H. Cbl-mediated ubiquitinylation is required for lysosomal sorting of epidermal growth factor receptor but is dispensable for endocytosis. J. Biol. Chem. 278 (2003) 28950-28960
43. Hoeller D., Crosetto N., Blagoev B., Raiborg C., Tikkanen R., Wagner S., Kowanetz K., Breitling R., Mann M., Stenmark H., and Dikic I. Regulation of ubiquitin-binding proteins by monoubiquitination. Nat. Cell Biol. 8 (2006) 163-169
44. Marchese A., Raiborg C., Santini F., Keen J.H., Stenmark H., and Benovic J.L. The E3 ubiquitin ligase AIP4 mediates ubiquitination and sorting of the G protein-coupled receptor CXCR4. Dev. Cell 5 (2003) 709-722
45. Olzmann J.A., Li L., Chudaev M.V., Chen J., Perez F.A., Palmiter R.D., and Chin L.-S. Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6. J. Cell Biol. 178 (2007) 1025-1038
46. Raiborg C., Rusten T.E., and Stenmark H. Protein sorting into multivesicular endosomes. Curr. Opin. Cell Biol. 15 (2003) 446-455
47. Johnson R.T. Prion diseases. Lancet Neurol. 4 (2005) 635-642
48. Glatzel M., Stoeck K., Seeger H., Luhrs T., and Aguzzi A. Human prion diseases: molecular and clinical aspects. Arch. Neurol. 62 (2005) 545-552
49. Piccardo P., Safar J., Ceroni M., Gajdusek D.C., Gibbs, and Jr. C.J. Immunohistochemical localization of prion protein in spongiform encephalopathies and normal brain tissue. Neurology 40 (1990) 518-522
50. Voigtländer T., Klöppel S., Birner P., Jarius C., Flicker H., Verghese-Nikolakaki S., Sklaviadis T., Guentchev M., and Budka H. Marked increase of neuronal prion protein immunoreactivity in Alzheimer's disease and human prion diseases. Acta Neuropathol. 101 (2001) 417-423
51. Watts J.C., and Westaway D. The prion protein family: diversity, rivalry, and dysfunction. Biochim. Biophys. Acta 1772 (2007) 654-672
52. Büeler H., Aguzzi A., Sailer A., Greiner R.A., Autenried P., Aguet M., and Weissmann C. Mice devoid of PrP are resistant to scrapie. Cell 73 (1993) 1339-1347
53. Pietri M., Caprini A., Mouillet-Richard S., Pradines E., Ermonval M., Grassi J., Kellermann O., and Schneider B. Overstimulation of PrPC signaling pathways by prion peptide 106-126 causes oxidative injury of bioaminergic neuronal cells. J. Biol. Chem. 281 (2006) 28470-28479
54. Prusiner S.B., Groth D., Serban A., Koehler R., Foster D., Torchia M., Burton D., Yang S.-L., and DeArmond S.J. Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 10608-10612
55. Sailer A., Büeler H., Fischer M., Aguzzi A., and Weissmann C. No propagation of prions in mice devoid of PrP. Cell 77 (1994) 967-968
56. Fornai F., Ferrucci M., Gesi M., di Poggio A.B., Giorgi F.S., Biagioni F., and Paparelli A. A hypothesis on prion disorders: are infectious, inherited, and sporadic causes so distinct?. Brain Res. Bull. 69 (2006) 95-100
57. Weissmann C., Büeler H., Fischer M., Sailer A., Aguzzi A., and Aguet M. PrP-deficient mice are resistant to scrapie. Ann. N. Y. Acad. Sci. 724 (1994) 235-240
58. Sc levels but delayed onset of disease in scrapie-inoculated mice heterozygous for a disrupted PrP gene. Mol. Med. 1 (1994) 19-30
59. Kang S.-C., Brown D.R., Whiteman M., Li R., Pan T., Perry G., Wisniewski T., Sy M.-S., and Wong B.-S. Prion protein is ubiquitinated after developing protease resistance in the brains of scrapie-infected mice. J. Pathol. 203 (2004) 603-608
60. Skinner P.J., Abbassi H., Chesebro B., Race R.E., Reilly C., and Haase A.T. Gene expression alterations in brains of mice infected with three strains of scrapie. BMC Genomics 7 (2006) 114
61. Kovács G.G., Preusser M., Strohschneider M., and Budka H. Subcellular localization of disease-associated prion protein in the human brain. Am. J. Pathol. 166 (2005) 287-294
62. Kim J.-I., Choi S.-I., Kim N.-H., Jin J.-K., Choi E.-K., Carp R.I., and Kim Y.-S. Oxidative stress and neurodegeneration in prion diseases. Ann. N. Y. Acad. Sci. 928 (2001) 182-186
63. Arnold J.E., Tipler C., Laszlo L., Hope J., Landon M., and Mayer R.J. The abnormal isoform of the prion protein accumulates in late-endosome-like organelles in scrapie-infected mouse brain. J. Pathol. 176 (1995) 403-411
64. Caughey B., Raymond G.J., Ernst D., and Race R.E. N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): implications regarding the site of conversion of PrP to the protease-resistant state. J. Virol. 65 (1991) 6597-6603
65. Magalhães A.C., Silva J.A., Lee K.S., Martins V.R., Prado V.F., Ferguson S.S.G., Gomez M.V., Brentani R.R., and Prado M.A.M. Endocytic intermediates involved with the intracellular trafficking of a fluorescent cellular prion protein. J. Biol. Chem. 277 (2002) 33311-33318
66. Mironov, Jr. A., Latawiec D., Wille H., Bouzamondo-Bernstein E., Legname G., Williamson R.A., Burton D., DeArmond S.J., Prusiner S.B., and Peters P.J. Cytosolic prion protein in neurons. J. Neurosci. 23 (2003) 7183-7193
67. Shyng S.L., Huber M.T., and Harris D.A. A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells. J. Biol. Chem. 268 (1993) 15922-15928
68. Kopacek J., Sakaguchi S., Shigematsu K., Nishida N., Atarashi R., Nakaoke R., Moriuchi R., Niwa M., and Katamine S. Upregulation of the genes encoding lysosomal hydrolases, a perforin-like protein, and peroxidases in the brains of mice affected with an experimental prion disease. J. Virol. 74 (2000) 411-417
69. Kovács G.G., Gelpi E., Ströbel T., Ricken G., Nyengaard J.R., Bernheimer H., and Budka H. Involvement of the endosomal-lysosomal system correlates with regional pathology in Creutzfeldt-Jakob disease. J. Neuropathol. Exp. Neurol. 66 (2007) 628-636
70. Hicke L. Gettin' down with ubiquitin: turning off cell-surface receptors, transporters, and channels. Trends Cell Biol. 9 (1999) 107-112
71. Marmor M.D., and Yarden Y. Role of protein ubiquitylation in regulating endocytosis of receptor tyrosine kinases. Oncogene 23 (2004) 2057-2070
72. Parkin E.T., Watt N.T., Hussain I., Eckman E.A., Eckman C.B., Manson J.C., Baybutt H.N., Turner A.J., and Hooper N.M. Cellular prion protein regulates beta-secretase cleavage of the Alzheimer's amyloid precursor protein. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 11062-11067
73. Bossy-Wetzel E., Schwarzenbacher R., and Lipton S.A. Molecular pathways to neurodegeneration. Nat. Med. 10 (2004) S2-S9
74. Berke S.J.S., and Paulson H.L. Protein aggregation and the ubiquitin proteasome pathway: gaining the UPPer hand on neurodegeneration. Curr. Opin. Genet. Dev. 13 (2003) 253-261
75. Keller J.N., Hanni K.B., and Markesbery W.R. Impaired proteasome function in Alzheimer's disease. J. Neurochem. 75 (2000) 436-439
76. Salon M.L., Morelli L., Castaño E.M., Soto E.F., and Pasquini J.M. Defective ubiquitination of cerebral proteins in Alzheimer's disease. J. Neurosci. Res. 62 (2000) 302-310
77. McNaught K.S.P., Belizaire R., Isacson O., Jenner P., and Olanow C.W. Altered proteasomal function in sporadic Parkinson's disease. Exp. Neurol. 179 (2003) 38-46
78. Lin M.T., and Beal M.F. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443 (2006) 787-795
79. Rego A.C., and Oliveira C.R. Mitochondrial dysfunction and reactive oxygen species in excitotoxicity and apoptosis: implications for the pathogenesis of neurodegenerative diseases. Neurochem. Res. 28 (2003) 1563-1574
80. Nixon R.A. Endosome function and dysfunction in Alzheimer's disease and other neurodegenerative diseases. Neurobiol. Aging 26 (2005) 373-382
81. Bilello J.A., Pitts O.M., and Hoffman P.M. Characterization of a progressive neurodegenerative disease induced by a temperature-sensitive Moloney murine leukemia virus infection. J. Virol. 59 (1986) 234-241
82. Wong P.K.Y., and Yuen P.H. Cell types in the central nervous system infected by murine retroviruses: implications for the mechanisms of neurodegeneration. Histol. Histopathol. 9 (1994) 845-858
83. Clase A.C., Dimcheff D.E., Favara C., Dorward D., McAtee F.J., Parrie L.E., Ron D., and Portis J.L. Oligodendrocytes are a major target of the toxicity of spongiogenic murine retroviruses. Am. J. Pathol. 169 (2006) 1026-1038
84. Dimcheff D.E., Faasse M.A., McAtee F.J., and Portis J.L. Endoplasmic reticulum (ER) stress induced by a neurovirulent mouse retrovirus is associated with prolonged BiP binding and retention of a viral protein in the ER. J. Biol. Chem. 279 (2004) 33782-33790
85. Kay D.G., Gravel C., Pothier F., Laperriere A., Robitaille Y., and Jolicoeur P. Neurological disease induced in transgenic mice expressing the env gene of the Cas-Br-E murine retrovirus. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 4538-4542
86. Lynch W.P., and Sharpe A.H. Differential glycosylation of the Cas-Br-E env protein is associated with retrovirus-induced spongiform neurodegeneration. J. Virol. 74 (2000) 1558-1565
87. Martin-Serrano J., Perez-Caballero D., and Bieniasz P.D. Context-dependent effects of L domains and ubiquitination on viral budding. J. Virol. 78 (2004) 5554-5563
88. Gelman B.B., and Schuenke K. Brain aging in acquired immunodeficiency syndrome: increased ubiquitin-protein conjugate is correlated with decreased synaptic protein but not amyloid plaque accumulation. J. Neurovirol. 10 (2004) 98-108
89. Li Z., Arnaud L., Rockwell P., and Figueiredo-Pereira M.E. A single amino acid substitution in a proteasome subunit triggers aggregation of ubiquitinated proteins in stressed neuronal cells. J. Neurochem. 90 (2004) 19-28
90. Zhang M., Thurig S., Tsirigotis M., Wong P.K.Y., Reuhl K.R., and Gray D.A. Effects of mutant ubiquitin on ts1 retrovirus-mediated neuropathology. J. Virol. 77 (2003) 7193-7201
91. Jiang Y., Scofield V.L., Yan M., Qiang W., Liu N., Reid A.J., Lynn W.S., and Wong P.K.Y. Retrovirus-induced oxidative stress with neuroimmunodegeneration is suppressed by antioxidant treatment with a refined monosodium α-luminol (Galavit). J. Virol. 80 (2006) 4557-4569
92. Piedimonte G., Guetard D., Magnani M., Corsi D., Picerno I., Spataro P., Kramer L., Montroni M., Silvestri G., Roca J.F.T., and Montagnier L. Oxidative protein damage and degradation in lymphocytes from patients infected with human immunodeficiency virus. J. Infect. Dis. 176 (1997) 655-664
93. Blot V., Perugi F., Gay B., Prevost M.-C., Briant L., Tangy F., Abriel H., Staub O., Dokhélar M.-C., and Pique C. Nedd4.1-mediated ubiquitination and subsequent recruitment of Tsg101 ensure HTLV-1 Gag trafficking towards the multivesicular body pathway prior to virus budding. J. Cell Sci. 117 (2004) 2357-2367
94. Bouamr F., Houck-Loomis B.R., De Los Santos M., Casaday R.J., Johnson M.C., and Goff S.P. The C-terminal portion of the Hrs protein interacts with Tsg101 and interferes with human immunodeficiency virus type 1 Gag particle production. J. Virol. 81 (2007) 2909-2922
95. Dimcheff D.E., Askovic S., Baker A.H., Johnson-Fowler C., and Portis J.L. Endoplasmic reticulum stress is a determinant of retrovirus-induced spongiform neurodegeneration. J. Virol. 77 (2003) 12617-12629
96. Fang Y., Wu N., Gan X., Yan W., Morrell J.C., and Gould S.J. Higher-order oligomerization targets plasma membrane proteins and HIV gag to exosomes. PLoS Biol. 5 (2007) e158
97. Segura-Morales C., Pescia C., Chatellard-Causse C., Sadoul R., Bertrand E., and Basyuk E. Tsg101 and Alix interact with murine leukemia virus Gag and cooperate with Nedd4 ubiquitin ligases during budding. J. Biol. Chem. 280 (2005) 27004-27012
98. Klugmann M., Leichtlein C.B., Symes C.W., Serikawa T., Young D., and During M.J. Restoration of aspartoacylase activity in CNS neurons does not ameliorate motor deficits and demyelination in a model of Canavan disease. Mol. Ther. 11 (2005) 745-753
99. Pederzolli C.D., Mescka C.P., Scapin F., Rockenbach F.J., Sgaravatti A.M., Sgarbi M.B., Wyse A.T.S., Wannmacher C.M.D., Wajner M., and Dutra-Filho C.S. N-acetylaspartic acid promotes oxidative stress in cerebral cortex of rats. Int. J. Dev. Neurosci. 25 (2007) 317-324
100. L proteins in SH-SY5Y neuroblastoma and in Parkinson disease cybrid cells through oxidative stress. J. Neurosci. Res. 61 (2000) 693-700
101. Duke D.C., Moran L.B., Kalaitzakis M.E., Deprez M., Dexter D.T., Pearce R.K.B., and Graeber M.B. Transcriptome analysis reveals link between proteasomal and mitochondrial pathways in Parkinson's disease. Neurogenetics 7 (2006) 139-148
102. Jahngen-Hodge J., Obin M.S., Gong X., Shang F., Thomas J., Nowell R., Gong J., Abasi H., Blumberg J., and Taylor A. Regulation of ubiquitin-conjugating enzymes by glutathione following oxidative stress. J. Biol. Chem. 272 (1997) 28218-28226
103. Aslan M., and Ozben T. Oxidants in receptor tyrosine kinase signal transduction pathways. Antioxid. Redox Signal. 5 (2003) 781-788
104. Chen Y., McMillan-Ward E., Kong J., Israels S.J., and Gibson S.B. Oxidative stress induces autophagic cell death independent of apoptosis in transformed and cancer cells. Cell Death Differ. 15 (2008) 171-182
105. Adamo A.M., Pasquini L.A., Moreno M.B., Oteiza P.I., Soto E.F., and Pasquini J.M. Effect of oxidant systems on the ubiquitylation of proteins in the central nervous system. J. Neurosci. Res. 55 (1999) 523-531
106. Gunn T.M., Inui T., Kitada K., Ito S., Wakamatsu K., He L., Bouley D.M., Serikawa T., and Barsh G.S. Molecular and phenotypic analysis of Attractin mutant mice. Genetics 158 (2001) 1683-1695
107. Kondo A., Sendoh S., Miyata K., and Takamatsu J. Spongy degeneration in the zitter rat: ultrastructural and immunohistochemical studies. J. Neurocytol. 24 (1995) 533-544
108. Barsh G., Gunn T., He L., Schlossman S., and Duke-Cohan J. Biochemical and genetic studies of pigment-type switching. Pigment. Cell Res. 13 (2000) 48-53
109. Muto Y., and Sato K. Pivotal role of attractin in cell survival under oxidative stress in the zitter rat brain with genetic spongiform encephalopathy. Mol. Brain Res. 111 (2003) 111-122
110. He L., Eldridge A.G., Jackson P.K., Gunn T.M., and Barsh G.S. Accessory proteins for melanocortin signaling: attractin and mahogunin. Ann. N. Y. Acad. Sci. 994 (2003) 288-298
111. Miller K.A., Gunn T.M., Carrasquillo M.M., Lamoreux M.L., Galbraith D.B., and Barsh G.S. Genetic studies of the mouse mutations mahogany and mahoganoid. Genetics 146 (1997) 1407-1415
112. Paz J., Yao H., Lim H.S., Lu X.-Y., and Zhang W. The neuroprotective role of attractin in neurodegeneration. Neurobiol. Aging 28 (2007) 1446-1456
113. Nakadate K., Noda T., Sakakibara S.-I., Kumamoto K., Matsuura T., Joyce J., and Ueda S. Progressive dopaminergic neurodegeneration of substantia nigra in the zitter mutant rat. Acta Neuropathol. 112 (2006) 64-73
114. Sun K., Johnson B.S., and Gunn T.M. Mitochondrial dysfunction precedes neurodegeneration in mahogunin (Mgrn1) mutant mice. Neurobiol. Aging 28 (2007) 1840-1852
115. Phan L.K., Lin F., LeDuc C.A., Chung W.K., and Leibel R.L. The mouse mahoganoid coat color mutation disrupts a novel C3HC4 RING domain protein. J. Clin. Invest. 110 (2002) 1449-1459
116. Bagher P., Jiao J., Owen Smith C., Cota C.D., and Gunn T.M. Characterization of Mahogunin Ring Finger-1 expression in mice. Pigment. Cell Res. 19 (2006) 635-643
117. Gomi H., Ikeda T., Kunieda T., Itohara S., Prusiner S.B., and Yamanouchi K. Prion protein (PrP) is not involved in the pathogenesis of spongiform encephalopathy in zitter rats. Neurosci. Lett. 166 (1994) 171-174
118. Kim B.Y., Olzmann J.A., Barsh G.S., Chin L.-S., and Li L. Spongiform neurodegeneration-associated E3 ligase Mahogunin ubiquitylates TSG101 and regulates endosomal trafficking. Mol. Biol. Cell 18 (2007) 1129-1142
119. Yang Y., and Yu X. Regulation of apoptosis: the ubiquitous way. FASEB J. 17 (2003) 790-799
120. Creagh E.M., Murphy B.M., Duriez P.J., Duckett C.S., and Martin S.J. Smac/Diablo antagonizes ubiquitin ligase activity of inhibitor of apoptosis proteins. J. Biol. Chem. 279 (2004) 26906-26914
121. MacFarlane M., Merrison W., Bratton S.B., and Cohen G.M. Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro. J. Biol. Chem. 277 (2002) 36611-36616
122. Marshansky V., Wang X., Bertrand R., Luo H., Duguid W., Chinnadurai G., Kanaan N., Vu M.D., and Wu J. Proteasomes modulate balance among proapoptotic and antiapoptotic Bcl-2 family members and compromise functioning of the electron transport chain in leukemic cells. J. Immunol. 166 (2001) 3130-3142
123. Morizane Y., Honda R., Fukami K., and Yasuda H. X-linked inhibitor of apoptosis functions as ubiquitin ligase toward mature caspase-9 and cytosolic Smac/DIABLO. J. Biochem. 137 (2005) 125-132
124. Fbw7 antagonizes apoptotic JNK signaling. Science 303 (2004) 1374-1378
125. Suh J., Lee Y.A., and Gwag B.J. Induction and attenuation of neuronal apoptosis by proteasome inhibitors in murine cortical cell cultures. J. Neurochem. 95 (2005) 684-694
126. Tait S.W.G., de Vries E., Maas C., Keller A.M., D'santos C.S., and Borst J. Apoptosis induction by Bid requires unconventional ubiquitination and degradation of its N-terminal fragment. J. Cell Biol. 179 (2007) 1453-1466
127. van Gurp M., Festjens N., van Loo G., Saelens X., and Vandenabeele P. Mitochondrial intermembrane proteins in cell death. Biochem. Biophys. Res. Commun. 304 (2003) 487-497
128. Donovan M., and Cotter T.G. Control of mitochondrial integrity by Bcl-2 family members and caspase-independent cell death. Biochim. Biophys. Acta 1644 (2004) 133-147
129. Li Q., Ching A.K.-K., Chan B.C.-L., Chow S.K.-Y., Lim P.-L., Ho T.C.-Y., Ip W.-K., Wong C.-K., Lam C.W.-K., Lee K.K.-H., Chan J.Y.-H., and Chui Y.-L. A death receptor-associated anti-apoptotic protein, BRE, inhibits mitochondrial apoptotic pathway. J. Biol. Chem. 279 (2004) 52106-52116
130. Peruzzi F., Prisco M., Morrione A., Valentinis B., and Baserga R. Anti-apoptotic signaling of the insulin-like growth factor-I receptor through mitochondrial translocation of c-Raf and Nedd4. J. Biol. Chem. 276 (2001) 25990-25996
131. Ding Q., and Keller J.N. Proteasome inhibition in oxidative stress neurotoxicity: implications for heat shock proteins. J. Neurochem. 77 (2001) 1010-1017
132. Papa L., Gomes E., and Rockwell P. Reactive oxygen species induced by proteasome inhibition in neuronal cells mediate mitochondrial dysfunction and a caspase-independent cell death. Apoptosis 12 (2007) 1389-1405
133. Rinaldi T., Pick E., Gambadoro A., Zilli S., Maytal-Kivity V., Frontali L., and Glickman M.H. Participation of the proteasomal lid subunit Rpn11 in mitochondrial morphology and function is mapped to a distinct C-terminal domain. Biochem. J. 381 (2004) 275-285
134. Sullivan P.G., Dragicevic N.B., Deng J.-H., Bai Y., Dimayuga E., Ding Q., Chen Q., Bruce-Keller A.J., and Keller J.N. Proteasome inhibition alters neural mitochondrial homeostasis and mitochondria turnover. J. Biol. Chem. 279 (2004) 20699-20707
135. Carrard G., Bulteau A.-L., Petropoulos I., and Friguet B. Impairment of proteasome structure and function in aging. Int. J. Biochem. Cell Biol. 34 (2002) 1461-1474
136. Li Y.-P., Chen Y., Li A.S., and Reid M.B. Hydrogen peroxide stimulates ubiquitin-conjugating activity and expression of genes for specific E2 and E3 proteins in skeletal muscle myotubes. Am. J. Physiol. Cell Physiol. 285 (2003) C806-C812
137. Shamoto-Nagai M., Maruyama W., Kato Y., Isobe K.-I., Tanaka M., Naoi M., and Osawa T. An inhibitor of mitochondrial complex I, rotenone, inactivates proteasome by oxidative modification and induces aggregation of oxidized proteins in SH-SY5Y cells. J. Neurosci. Res. 74 (2003) 589-597
138. Zeevalk G.D., and Bernard L.P. Energy status, ubiquitin proteasomal function, and oxidative stress during chronic and acute complex I inhibition with rotenone in mesencephalic cultures. Antioxid. Redox Signal. 7 (2005) 662-672
139. Altmann K., and Westermann B. Role of essential genes in mitochondrial morphogenesis in Saccharomyces cerevisiae. Mol. Biol. Cell 16 (2005) 5410-5417
140. Dürr M., Escobar-Henriques M., Merz S., Geimer S., Langer T., and Westermann B. Nonredundant roles of mitochondria-associated F-box proteins Mfb1 and Mdm30 in maintenance of mitochondrial morphology in yeast. Mol. Biol. Cell 17 (2006) 3745-3755
141. Fritz S., Weinbach N., and Westermann B. Mdm30 is an F-box protein required for maintenance of fusion-competent mitochondria in yeast. Mol. Biol. Cell 14 (2003) 2303-2313
142. Nakamura N., and Hirose S. Regulation of mitochondrial morphology by Usp30, a deubiquitinating enzyme present in the mitochondrial outer membrane. Mol. Biol. Cell (2008) E07-11-1103
143. Nakamura N., Kimura Y., Tokuda M., Honda S., and Hirose S. MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology. EMBO Rep. 7 (2006) 1019-1022
144. Papa L., and Rockwell P. Persistent mitochondrial dysfunction and oxidative stress hinder neuronal cell recovery from reversible proteasome inhibition. Apoptosis (2008)
145. Berlett B.S., and Stadtman E.R. Protein oxidation in aging, disease, and oxidative stress. J. Biol. Chem. 272 (1997)
146. Klein J.A., and Ackerman S.L. Oxidative stress, cell cycle, and neurodegeneration. J. Clin. Invest. 111 (2003) 785-793
147. Barrientos A., and Moraes C.T. Titrating the effects of mitochondrial complex I impairment in the cell physiology. J. Biol. Chem. 274 (1999) 16188-16197
148. Chen Q., Vazquez E.J., Moghaddas S., Hoppel C.L., and Lesnefsky E.J. Production of reactive oxygen species by mitochondria: central role of complex III. J. Biol. Chem. 278 (2003) 36027-36031
149. Nicholls D.G. Mitochondrial function and dysfunction in the cell: its relevance to aging and aging-related disease. Int. J. Biochem. Cell Biol. 34 (2002) 1372-1381
150. Nohl H., Gille L., Kozlov A., and Staniek K. Are mitochondria a spontaneous and permanent source of reactive oxygen species?. Redox. Rep. 8 (2003) 135-141
151. Abou-Sleiman P.M., Muqit M.M.K., and Wood N.W. Expanding insights of mitochondrial dysfunction in Parkinson's disease. Nat. Rev. Neurosci. 7 (2006) 207-219
152. Chan T.S., Teng S., Wilson J.X., Galati G., Khan S., and O'Brien P.J. Coenzyme Q cytoprotective mechanisms for mitochondrial complex I cytopathies involves NAD(P)H: quinone oxidoreductase 1(NQO1). Free Radic. Res. 36 (2002) 421-427
153. Li Q., Sato E.F., Kira Y., Nishikawa M., Utsumi K., and Inoue M. A possible cooperation of SOD1 and cytochrome c in mitochondria-dependent apoptosis. Free Radic. Biol. Med. 40 (2006) 173-181
154. Chinopoulos C., and Adam-Vizi V. Mitochondria deficient in complex I activity are depolarized by hydrogen peroxide in nerve terminals: relevance to Parkinson's disease. J. Neurochem. 76 (2001) 302-306
155. Chinopoulos C., Tretter L., and Adam-Vizi V. Depolarization of in situ mitochondria due to hydrogen peroxide-induced oxidative stress in nerve terminals. Inhibition of α-ketoglutarate dehydrogenase. J. Neurochem. 73 (1999) 220-228
156. Zhang J.-G., Tirmenstein M.A., Nicholls-Grzemski F.A., and Fariss M.W. Mitochondrial electron transport inhibitors cause lipid peroxidation-dependent and -independent cell death: Protective role of antioxidants. Arch. Biochem. Biophys. 393 (2001) 87-96
157. Ross C.A., and Poirier M.A. Protein aggregation and neurodegenerative disease. Nat. Med. 10 (2004) S10-S17
158. Biasini E., Fioriti L., Ceglia I., Invernizzi R., Bertoli A., Chiesa R., and Forloni G. Proteasome inhibition and aggregation in Parkinson's disease: a comparative study in untransfected and transfected cells. J. Neurochem. 88 (2004) 545-553
159. Rideout H.J., and Stefanis L. Proteasomal inhibition-induced inclusion formation and death in cortical neurons require transcription and ubiquitination. Mol. Cell. Neurosci. 21 (2002) 223-238
160. Finkel T. Reactive oxygen species and signal transduction. IUBMB Life 52 (2001) 3-6
161. Liu W., Gnanasambandam R., Benjamin J., Kaur G., Getman P.B., Siegel A.J., Shortridge R.D., and Singh S. Mutations in cytochrome c oxidase subunit VIa cause neurodegeneration and motor dysfunction in Drosophila. Genetics 176 (2007) 937-946
162. Wong B.-S., Brown D.R., Pan T., Whiteman M., Liu T., Bu X., Li R., Gambetti P., Olesik J., Rubenstein R., and Sy M.-S. Oxidative impairment in scrapie-infected mice is associated with brain metals perturbations and altered antioxidant activities. J. Neurochem. 79 (2001) 689-698
163. Gomi H., Ueno I., and Yamanouchi K. Antioxidant enzymes in the brain of zitter rats: abnormal metabolism of oxygen species and its relevance to pathogenic changes in the brain of zitter rats with genetic spongiform encephalopathy. Brain Res. 653 (1994) 66-72
164. Hinerfeld D., Traini M.D., Weinberger R.P., Cochran B., Doctrow S.R., Harry J., and Melov S. Endogenous mitochondrial oxidative stress: neurodegeneration, proteomic analysis, specific respiratory chain defects, and efficacious antioxidant therapy in superoxide dismutase 2 null mice. J. Neurochem. 88 (2004) 657-667
165. Bence N.F., Sampat R.M., and Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292 (2001) 1552-1555
166. Kristiansen M., Deriziotis P., Dimcheff D.E., Jackson G.S., Ovaa H., Naumann H., Clarke A.R., van Leeuwen F.W.B., Menéndez-Benito V., Dantuma N.P., Portis J.L., Collinge J., and Tabrizi S.J. Disease-associated prion protein oligomers inhibit the 26S proteasome. Mol. Cell 26 (2007) 175-188
167. Dear D.V., Young D.S., Kazlauskaite J., Meersman F., Oxley D., Webster J., Pinheiro T.J.T., Gill A.C., Bronstein I., and Lowe C.R. Effects of post-translational modifications on prion protein aggregation and the propagation of scrapie-like characteristics in vitro. Biochim. Biophys. Acta 1774 (2007) 792-802
168. Ding W.-X., and Yin X.-M. Sorting, recognition and activation of the misfolded protein degradation pathways through macroautophagy and the proteasome. Autophagy (2008) 141-150
169. Keller J.N., Dimayuga E., Chen Q., Thorpe J., Gee J., and Ding Q. Autophagy, proteasomes, lipofuscin, and oxidative stress in the aging brain. Int. J. Biochem. Cell Biol. 36 (2004) 2376-2391
170. Kristiansen M., Messenger M.J., Klohn P.-C., Brandner S., Wadsworth J.D.F., Collinge J., and Tabrizi S.J. Disease-related prion protein forms aggresomes in neuronal cells leading to caspase activation and apoptosis. J. Biol. Chem. 280 (2005) 38851-38861
171. Wong B.-S., Liu T., Li R., Pan T., Petersen R.B., Smith M.A., Gambetti P., Perry G., Manson J.C., Brown D.R., and Sy M.-S. Increased levels of oxidative stress markers detected in the brains of mice devoid of prion protein. J. Neurochem. 76 (2001) 565-572
172. Jolicoeur P., Hu C., Mak T.W., Martinou J.-C., and Kay D.G. Protection against murine leukemia virus-induced spongiform myeloencephalopathy in mice overexpressing Bcl-2 but not in mice deficient for interleukin-6, inducible nitric oxide synthetase, ICE, Fas, Fas ligand, or TNF-R1 genes. J. Virol. 77 (2003) 13161-13170
173. Ding W.-X., Ni H.-M., Gao W., Yoshimori T., Stolz D.B., Ron D., and Yin X.-M. Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability. Am. J. Pathol. 171 (2007) 513-524
174. Tan J.M.M., Wong E.S.P., Kirkpatrick D.S., Pletnikova O., Ko H.S., Tay S.-P., Ho M.W.L., Troncoso J., Gygi S.P., Lee M.K., Dawson V.L., Dawson T.M., and Lim K.-L. Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases. Hum. Mol. Genet. 17 (2008) 431-439
175. Olzmann J.A., Chin L.S., and Li L. Aggresome formation and neurodegenerative diseases: therapeutic implications. Curr. Med. Chem. 15 (2008) 47-60
176. Mizushima N. Autophagy: process and function. Genes Dev. 21 (2007) 2861-2873
177. Chen Y., and Gibson S.B. Is mitochondrial generation of reactive oxygen species a trigger for autophagy?. Autophagy 4 (2008) 246-248
178. Chen Y., McMillan-Ward E., Kong J., Israels S.J., and Gibson S.B. Mitochondrial electron-transport-chain inhibitors of complexes I and II induce autophagic cell death mediated by reactive oxygen species. J. Cell Sci. 120 (2007) 4155-4166
179. Scherz-Shouval R., and Elazar Z. ROS, mitochondria and the regulation of autophagy. Trends Cell Biol. 17 (2007) 422-427
180. Hara T., Nakamura K., Matsui M., Yamamoto A., Nakahara Y., Suzuki-Migishima R., Yokoyama M., Mishima K., Saito I., Okano H., and Mizushima N. Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 441 (2006) 885-889
181. Komatsu M., Waguri S., Chiba T., Murata S., Iwata J.-i., Tanida I., Ueno T., Koike M., Uchiyama Y., Kominami E., and Tanaka K. Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 441 (2006) 880-884
182. Mizushima N., Levine B., Cuervo A.M., and Klionsky D.J. Autophagy fights disease through cellular self-digestion. Nature 451 (2008) 1069-1075
183. Liberski P.P., Gajdusek D.C., and Brown P. How do neurons degenerate in prion diseases or transmissible spongiform encephalopathies (TSEs): neuronal autophagy revisited. Acta Neurobiol. Exp. 62 (2002) 141-147
184. Sikorska B., Liberski P.P., Giraud P., Kopp N., and Brown P. Autophagy is a part of ultrastructural synaptic pathology in Creutzfeldt-Jakob disease: a brain biopsy study. Int. J. Biochem. Cell Biol. 36 (2004) 2563-2573
185. Dron M., Bailly Y., Beringue V., Haeberle A.-M., Griffond B., Risold P.-Y., Tovey M.G., Laude H., and Dandoy-Dron F. Scrg1 is induced in TSE and brain injuries, and associated with autophagy. Eur. J. Neurosci. 22 (2005) 133-146
186. Moreira P.I., Siedlak S.L., Wang X., Santos M.S., Oliveira C.R., Tabaton M., Nunomura A., Szweda L.I., Aliev G., Smith M.A., Zhu X., and Perry G. Autophagocytosis of mitochondria is prominent in Alzheimer disease. J. Neuropathol. Exp. Neurol. 66 (2007) 525-532
187. Rubinsztein D.C. The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 443 (2006) 780-786
188. Kim I., Rodriguez-Enriquez S., and Lemasters J.J. Selective degradation of mitochondria by mitophagy. Arch. Biochem. Biophys. 462 (2007) 245-253
189. Fisk H.A., and Yaffe M.P. A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae. J. Cell Biol. 145 (1999) 1199-1208
190. Rapoport S., Dubiel W., and Müller M. Proteolysis of mitochondria in reticulocytes maturation is ubiquitin-dependent and is accompanied high rate of ATP hydrolysis. FEBS Lett. 180 (1985) 249-252
191. Thompson W.E., Ramalho-Santos J., and Sutovsky P. Ubiquitination of prohibitin in mammalian sperm mitochondria: possible roles in the regulation of mitochondrial inheritance and sperm quality control. Biol. Reprod. 69 (2003) 254-260
192. Terman A., Gustafsson B., and Brunk U.T. Autophagy, organelles and ageing. J. Pathol. 211 (2007) 134-143
193. Terman A., and Sandberg S. Proteasome inhibition enhances lipofuscin formation. Ann. N.Y. Acad. Sci. 973 (2002) 309-312
194. Katzmann D.J., Odorizzi G., and Emr S.D. Receptor downregulation and multivesicular-body sorting. Nat. Rev. Mol. Cell Biol. 3 (2002) 893-905
195. Bonifacino J.S., and Traub L.M. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 72 (2003) 395-447
196. Hurley J.H., and Emr S.D. The ESCRT complexes: structure and mechanism of a membrane-trafficking network. Annu. Rev. Biophys. Biomol. Struct. 35 (2006) 277-298
197. Alwan H.A.J., van Zoelen E.J.J., and van Leeuwen J.E.M. Ligand-induced lysosomal epidermal growth factor receptor (EGFR) degradation is preceded by proteasome-dependent EGFR de-ubiquitination. J. Biol. Chem. 278 (2003) 35781-35790
198. Filimonenko M., Stuffers S., Raiborg C., Yamamoto A., Malerod L., Fisher E.M.C., Isaacs A., Brech A., Stenmark H., and Simonsen A. Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease. J. Cell Biol. 179 (2007) 485-500
199. Lee J.-A., Beigneux A., Ahmad S.T., Young S.G., and Gao F.-B. ESCRT-III dysfunction causes autophagosome accumulation and neurodegeneration. Curr. Biol. 17 (2007) 1561-1567
200. van Niel G., Porto-Carreiro I., Simoes S., and Raposo G. Exosomes: a common pathway for a specialized function. J. Biochem. 140 (2006) 13-21
201. Campana V., Sarnataro D., and Zurzolo C. The highways and byways of prion protein trafficking. Trends Cell Biol. 15 (2005) 102-111
202. Tatzelt J., and Schatzl H.M. Molecular basis of cerebral neurodegeneration in prion diseases. FEBS J. 274 (2007) 606-611
203. Fevrier B., Vilette D., Archer F., Loew D., Faigle W., Vidal M., Laude H., and Raposo G. Cells release prions in association with exosomes. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 9683-9688
204. Martin-Serrano J., Zang T., and Bieniasz P.D. Role of ESCRT-I in retroviral budding. J. Virol. 77 (2003) 4794-4804
205. Morita E., and Sundquist W.I. Retrovirus budding. Annu. Rev. Cell Dev. Biol. 20 (2004) 395-425
206. Mazzé F.M., and Degrève L. The role of viral and cellular proteins in the budding of human immunodeficiency virus. Acta Virol. 50 (2006) 75-85
207. Jäger S., Gottwein E., and Kräusslich H.-G. Ubiquitination of human immunodeficiency virus type 1 Gag is highly dependent on Gag membrane association. J. Virol. 81 (2007) 9193-9201
208. Fevrier B., and Raposo G. Exosomes: endosomal-derived vesicles shipping extracellular messages. Curr. Opin. Cell Biol. 16 (2004) 415-421
209. Leblanc P., Alais S., Porto-Carreiro I., Lehmann S., Grassi J., Raposo G., and Darlix J.L. Retrovirus infection strongly enhances scrapie infectivity release in cell culture. EMBO J. 25 (2006) 2674-2685
210. Watson A.L., László L., and Doherty F.J. The degradative fate of ubiquitin-protein conjugates in nucleated and enucleated cells. Acta Biol. Hung. 42 (1991) 49-56
211. Maier O., Hoekstra D., and Baron W. Polarity development in oligodendrocytes: Sorting and trafficking of myelin components. J. Mol. Neurosci. 35 (2008) 35-53