Unravelling the role of defective genes

Progress in Brain Research

Volumn 183, Issue C, 2010, Pages 43-57

  Cookson, Mark R ^a  

^a NATIONAL INSTITUTE ON AGING   (United States)

Author keywords

DJ 1; Genetics; LRRK2; Parkin; PINK1; Synuclein

Indexed keywords

ARTICLE; DOMINANT GENE; GENE FUNCTION; GENE LOCUS; GENE MUTATION; GENE SEGREGATION; GENETIC ASSOCIATION; GENETIC VARIABILITY; LRRK2 GENE; PARKINSONISM; PHENOTYPE; PRIORITY JOURNAL; PROTEIN FUNCTION; RECESSIVE GENE; RISK FACTOR; SNCA GENE;

EID: 77955359853     PISSN: 00796123     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0079-6123(10)83003-1     Document Type: Chapter

References (95)

1. Beilina A., Van Der Brug M., Ahmad R., Kesavapany S., Miller D.W., Petsko G.A., et al. Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability. Proceedings of the National Academy of Sciences of the United States of America 2005, 102(16):5703-5708.
2. Blackinton J., Lakshminarasimhan M., Thomas K.J., Ahmad R., Greggio E., Raza A.S., et al. Formation of a stabilized cysteine sulfinic acid is critical for the mitochondrial function of the parkinsonism protein DJ-1. The Journal of Biological Chemistry 2009, 284(10):6476-6485.
3. Bonifati V., Rizzu P., van Baren M.J., Schaap O., Breedveld G.J., Krieger E., et al. Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism. Science 2003, 299(5604):256-259.
4. Bruijn L.I., Miller T.M., Cleveland D.W. Unraveling the mechanisms involved in motor neuron degeneration in ALS. Annual Review of Neuroscience 2004, 27:723-749.
5. Canet-Aviles R.M., Wilson M.A., Miller D.W., Ahmad R., McLendon C., Bandyopadhyay S., et al. The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization. Proceedings of the National Academy of Sciences of the United States of America 2004, 101(24):9103-9108.
6. Chartier-Harlin M.C., Kachergus J., Roumier C., Mouroux V., Douay X., Lincoln S., et al. Alpha-synuclein locus duplication as a cause of familial Parkinson's disease. Lancet 2004, 364(9440):1167-1169.
7. Clark I.E., Dodson M.W., Jiang C., Cao J.H., Huh J.R., Seol J.H., et al. Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 2006, 441(7097):1162-1166.
8. Conway K.A., Lee S.J., Rochet J.C., Ding T.T., Williamson R.E., Lansbury P.T. Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy. Proceedings of the National Academy of Sciences of the United States of America 2000, 97(2):571-576.
9. Cookson M.R. The biochemistry of Parkinson's disease. Annual Review of Biochemistry 2005, 74:29-52.
10. Cookson M.R., Hardy J., Lewis P.A. Genetic neuropathology of Parkinson's disease. International Journal of Clinical and Experimental Pathology 2008, 1(3):217-231.
11. Cookson M.R., Lockhart P.J., McLendon C., O'Farrell C., Schlossmacher M., Farrer M.J. RING finger 1 mutations in Parkin produce altered localization of the protein. Human Molecular Genetics 2003, 12(22):2957-2965.
12. Dagda R.K., Cherra S.J., Kulich S.M., Tandon A., Park D., Chu C.T. Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission. The Journal of Biological Chemistry 2009, 284(20):13843-13855.
13. Danzer K.M., Haasen D., Karow A.R., Moussaud S., Habeck M., Giese A., et al. Different species of alpha-synuclein oligomers induce calcium influx and seeding. Journal of Neuroscience 2007, 27(34):9220-9232.
14. Di Fonzo A., Rohe C.F., Ferreira J., Chien H.F., Vacca L., Stocchi F., et al. A frequent LRRK2 gene mutation associated with autosomal dominant Parkinson's disease. Lancet 2005, 365(9457):412-415.
15. Dodson M.W., Guo M. Pink1, Parkin, DJ-1 and mitochondrial dysfunction in Parkinson's disease. Current Opinion in Neurobiology 2007, 17(3):331-337.
16. Exner N., Treske B., Paquet D., Holmstrom K., Schiesling C., Gispert S., et al. Loss-of-function of human PINK1 results in mitochondrial pathology and can be rescued by parkin. Journal of Neuroscience 2007, 27(45):12413-12418.
17. Farrer M.J., Stone J.T., Lin C.H., Dachsel J.C., Hulihan M.M., Haugarvoll K., et al. Lrrk2 G2385R is an ancestral risk factor for Parkinson's disease in Asia. Parkinsonism & Related Disorders 2007, 13(2):89-92.
18. Funayama M., Hasegawa K., Ohta E., Kawashima N., Komiyama M., Kowa H., et al. An LRRK2 mutation as a cause for the parkinsonism in the original PARK8 family. Annals of Neurology 2005, 57(6):918-921.
19. Galter D., Westerlund M., Carmine A., Lindqvist E., Sydow O., Olson L. LRRK2 expression linked to dopamine-innervated areas. Annals of Neurology 2006, 59(4):714-719.
20. Gautier C.A., Kitada T., Shen J. Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress. Proceedings of the National Academy of Sciences of the United States of America 2008, 105(32):11364-11369.
21. Geisler S., Holmstrom K.M., Skujat D., Fiesel F.C., Rothfuss O.C., Kahle P.J., et al. PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1. Nature Cell Biology 2010, 12(2):119-131.
22. Giasson B.I., Uryu K., Trojanowski J.Q., Lee V.M. Mutant and wild type human alpha-synucleins assemble into elongated filaments with distinct morphologies in vitro. The Journal of Biological Chemistry 1999, 274(12):7619-7622.
23. Gilks W.P., Abou-Sleiman P.M., Gandhi S., Jain S., Singleton A., Lees A.J., et al. A common LRRK2 mutation in idiopathic Parkinson's disease. Lancet 2005, 365(9457):415-416.
24. Gloeckner C.J., Boldt K., von Zweydorf F., Helm S., Wiesent L., Sarioglu H., et al. Phosphopeptide analysis reveals two discrete clusters of phosphorylation in the N-terminus and the Roc domain of the Parkinson-disease associated protein kinase LRRK2. Journal of Proteome Research 2010, 9(4):1738-1745.
25. Godenschwege T., Forde R., Davis C.P., Paul A., Beckwith K., Duttaroy A. Mitochondrial superoxide radicals differentially affect muscle activity and neural function. Genetics 2009, 183(1):175-184.
26. Greenbaum E.A., Graves C.L., Mishizen-Eberz A.J., Lupoli M.A., Lynch D.R., Englander S.W., et al. The E46K mutation in alpha-synuclein increases amyloid fibril formation. The Journal of Biological Chemistry 2005, 280(9):7800-7807.
27. Greene J.C., Whitworth A.J., Kuo I., Andrews L.A., Feany M.B., Pallanck L.J. Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants. Proceedings of the National Academy of Sciences of the United States of America 2003, 100(7):4078-4083.
28. Greggio E., Cookson M.R. Leucine-rich repeat kinase 2 mutations and Parkinson's disease: Three questions. ASN Neuro 2009, 1:1.
29. Greggio E., Jain S., Kingsbury A., Bandopadhyay R., Lewis P., Kaganovich A., et al. Kinase activity is required for the toxic effects of mutant LRRK2/dardarin. Neurobiology of Disease 2006, 23(2):329-341.
30. Greggio E., Lewis P.A., van der Brug M.P., Ahmad R., Kaganovich A., Ding J., et al. Mutations in LRRK2/dardarin associated with Parkinson disease are more toxic than equivalent mutations in the homologous kinase LRRK1. Journal of Neurochemistry 2007, 102(1):93-102.
31. Greggio E., Taymans J.M., Zhen E.Y., Ryder J., Vancraenenbroeck R., Beilina A., et al. The Parkinson's disease kinase LRRK2 autophosphorylates its GTPase domain at multiple sites. Biochemical and Biophysical Research Communications 2009, 389(3):449-454.
32. Greggio E., Zambrano I., Kaganovich A., Beilina A., Taymans J.M., Daniels V., et al. The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation. The Journal of Biological Chemistry 2008, 283(24):16906-16914.
33. Haque M.E., Thomas K.J., D'Souza C., Callaghan S., Kitada T., Slack R.S., et al. Cytoplasmic Pink1 activity protects neurons from dopaminergic neurotoxin MPTP. Proceedings of the National Academy of Sciences of the United States of America 2008, 105(5):1716-1721.
34. Hardy J. Expression of normal sequence pathogenic proteins for neurodegenerative disease contributes to disease risk: 'permissive templating' as a general mechanism underlying neurodegeneration. Biochemical Society Transactions 2005, 33(Pt 4):578-581.
35. Haugarvoll K., Wszolek Z.K. Clinical features of LRRK2 parkinsonism. Parkinsonism & Related Disorders 2009, 15(Suppl. 3):S205-S208.
36. Hayashi T., Ishimori C., Takahashi-Niki K., Taira T., Kim Y.C., Maita H., et al. DJ-1 binds to mitochondrial complex I and maintains its activity. Biochemical and Biophysical Research Communications 2009, 390(3):667-672.
37. Iaccarino C., Crosio C., Vitale C., Sanna G., Carri M.T., Barone P. Apoptotic mechanisms in mutant LRRK2-mediated cell death. Human Molecular Genetics 2007, 16(11):1319-1326.
38. Ibanez P., Bonnet A.M., Debarges B., Lohmann E., Tison F., Pollak P., et al. Causal relation between alpha-synuclein gene duplication and familial Parkinson's disease. Lancet 2004, 364(9440):1169-1171.
39. Jorgensen N.D., Peng Y., Ho C.C., Rideout H.J., Petrey D., Liu P., et al. The WD40 domain is required for LRRK2 neurotoxicity. PLoS One 2009, 4(12):e8463.
40. Junn E., Jang W.H., Zhao X., Jeong B.S., Mouradian M.M. Mitochondrial localization of DJ-1 leads to enhanced neuroprotection. Journal of Neuroscience Research 2009, 87(1):123-129.
41. Kachergus J., Mata I.F., Hulihan M., Taylor J.P., Lincoln S., Aasly J., et al. Identification of a novel LRRK2 mutation linked to autosomal dominant parkinsonism: Evidence of a common founder across European populations. American Journal of Human Genetics 2005, 76(4):672-680.
42. Kamikawaji S., Ito G., Iwatsubo T. Identification of the autophosphorylation sites of LRRK2. Biochemistry 2009, 48(46):10963-10975.
43. Kay D.M., Kramer P., Higgins D., Zabetian C.P., Payami H. Escaping Parkinson's disease: A neurologically healthy octogenarian with the LRRK2 G2019S mutation. Movement Disorders 2005, 20(8):1077-1078.
44. Kim Y., Park J., Kim S., Song S., Kwon S.K., Lee S.H., et al. PINK1 controls mitochondrial localization of Parkin through direct phosphorylation. Biochemical and Biophysical Research Communications 2008, 377(3):975-980.
45. Kitada T., Asakawa S., Hattori N., Matsumine H., Yamamura Y., Minoshima S., et al. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 1998, 392(6676):605-608.
46. Klein C., Lohmann-Hedrich K., Rogaeva E., Schlossmacher M.G., Lang A.E. Deciphering the role of heterozygous mutations in genes associated with parkinsonism. Lancet Neurology 2007, 6(7):652-662.
47. Korr D., Toschi L., Donner P., Pohlenz H.D., Kreft B., Weiss B. LRRK1 protein kinase activity is stimulated upon binding of GTP to its Roc domain. Cellular Signalling 2006, 18(6):910-920.
48. Kostka M., Hogen T., Danzer K.M., Levin J., Habeck M., Wirth A., et al. Single particle characterization of iron-induced pore-forming alpha-synuclein oligomers. The Journal of Biological Chemistry 2008, 283(16):10992-11003.
49. Krebiehl G., Ruckerbauer S., Burbulla L.F., Kieper N., Maurer B., Waak J., et al. Reduced basal autophagy and impaired mitochondrial dynamics due to loss of Parkinson's disease-associated protein DJ-1. PLoS One 2010, 5(2):e9367.
50. Kruger R., Kuhn W., Muller T., Woitalla D., Graeber M., Kosel S., et al. Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease. Nature Genetics 1998, 18(2):106-108.
51. Kruger R., Sharma M., Riess O., Gasser T., Van Broeckhoven C., Theuns J., et al. A large-scale genetic association study to evaluate the contribution of Omi/HtrA2 (PARK13) to Parkinson's disease. Neurobiology of Aging. 2009, 10.1016/j.neurobiolaging.2009.11.021.
52. Kruger R., Vieira-Saecker A.M., Kuhn W., Berg D., Muller T., Kuhnl N., et al. Increased susceptibility to sporadic Parkinson's disease by a certain combined alpha-synuclein/apolipoprotein E genotype. Annals of Neurology 1999, 45(5):611-617.
53. Lewis P.A., Greggio E., Beilina A., Jain S., Baker A., Cookson M.R. The R1441C mutation of LRRK2 disrupts GTP hydrolysis. Biochemical and Biophysical Research Communications 2007, 357(3):668-671.
54. Li Y., Liu W., Oo T.F., Wang L., Tang Y., Jackson-Lewis V., et al. Mutant LRRK2(R1441G) BAC transgenic mice recapitulate cardinal features of Parkinson's disease. Nature Neuroscience 2009, 12(7):826-828.
55. Li H.M., Niki T., Taira T., Iguchi-Ariga S.M., Ariga H. Association of DJ-1 with chaperones and enhanced association and colocalization with mitochondrial Hsp70 by oxidative stress. Free Radical Research 2005, 39(10):1091-1099.
56. Li X., Tan Y.C., Poulose S., Olanow C.W., Huang X.Y., Yue Z. Leucine-rich repeat kinase 2 (LRRK2)/PARK8 possesses GTPase activity that is altered in familial Parkinson's disease R1441C/G mutants. Journal of Neurochemistry 2007, 103(1):238-247.
57. Lin X., Parisiadou L., Gu X.L., Wang L., Shim H., Sun L., et al. Leucine-rich repeat kinase 2 regulates the progression of neuropathology induced by Parkinson's-disease-related mutant alpha-synuclein. Neuron 2009, 64(6):807-827.
58. Liu M., Dobson B., Glicksman M.A., Yue Z., Stein R.L. Kinetic mechanistic studies of wild-type leucine-rich repeat kinase2: Characterization of the kinase and GTPase activities. Biochemistry 2010, 49(9):2008-2017.
59. MacLeod D., Dowman J., Hammond R., Leete T., Inoue K., Abeliovich A. The familial Parkinsonism gene LRRK2 regulates neurite process morphology. Neuron 2006, 52(4):587-593.
60. Miller D.W., Ahmad R., Hague S., Baptista M.J., Canet-Aviles R., McLendon C., et al. L166P mutant DJ-1, causative for recessive Parkinson's disease, is degraded through the ubiquitin-proteasome system. The Journal of Biological Chemistry 2003, 278(38):36588-36595.
61. Mortiboys H., Thomas K.J., Koopman W.J., Klaffke S., Abou-Sleiman P., Olpin S., et al. Mitochondrial function and morphology are impaired in parkin-mutant fibroblasts. Annals of Neurology 2008, 64(5):555-565.
62. Narendra D.P., Jin S.M., Tanaka A., Suen D.F., Gautier C.A., Shen J., et al. PINK1 is selectively stabilized on impaired mitochondria to activate Parkin. PLoS Biology 2010, 8(1):e1000298.
63. Narendra D., Tanaka A., Suen D.F., Youle R.J. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. The Journal of Cell Biology 2008, 183(5):795-803.
64. Narhi L., Wood S.J., Steavenson S., Jiang Y., Wu G.M., Anafi D., et al. Both familial Parkinson's disease mutations accelerate alpha-synuclein aggregation. The Journal of Biological Chemistry 1999, 274(14):9843-9846.
65. Nichols W.C., Pankratz N., Hernandez D., Paisan-Ruiz C., Jain S., Halter C.A., et al. Genetic screening for a single common LRRK2 mutation in familial Parkinson's disease. Lancet 2005, 365(9457):410-412.
66. Paisan-Ruiz C., Jain S., Evans E.W., Gilks W.P., Simon J., van der Brug M., et al. Cloning of the gene containing mutations that cause PARK8-linked Parkinson's disease. Neuron 2004, 44(4):595-600.
67. Palacino J.J., Sagi D., Goldberg M.S., Krauss S., Motz C., Wacker M., et al. Mitochondrial dysfunction and oxidative damage in parkin-deficient mice. The Journal of Biological Chemistry 2004, 279(18):18614-18622.
68. Park J., Lee S.B., Lee S., Kim Y., Song S., Kim S., et al. Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature 2006, 441(7097):1157-1161.
69. Parsian A., Racette B., Zhang Z.H., Chakraverty S., Rundle M., Goate A., et al. Mutation, sequence analysis, and association studies of alpha-synuclein in Parkinson's disease. Neurology 1998, 51(6):1757-1759.
70. Petit A., Kawarai T., Paitel E., Sanjo N., Maj M., Scheid M., et al. Wild-type PINK1 prevents basal and induced neuronal apoptosis, a protective effect abrogated by Parkinson disease-related mutations. The Journal of Biological Chemistry 2005, 280(40):34025-34032.
71. Polymeropoulos M.H., Lavedan C., Leroy E., Ide S.E., Dehejia A., Dutra A., et al. Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science 1997, 276(5321):2045-2047.
72. Riparbelli M.G., Callaini G. The Drosophila parkin homologue is required for normal mitochondrial dynamics during spermiogenesis. Developmental Biology 2007, 303(1):108-120.
73. Sandebring A., Thomas K.J., Beilina A., van der Brug M., Cleland M.M., Ahmad R., et al. Mitochondrial alterations in PINK1 deficient cells are influenced by calcineurin-dependent dephosphorylation of dynamin-related protein 1. PLoS One 2009, 4(5):e5701.
74. Satake W., Nakabayashi Y., Mizuta I., Hirota Y., Ito C., Kubo M., et al. Genome-wide association study identifies common variants at four loci as genetic risk factors for Parkinson's disease. Nature Genetics 2009, 41(12):1303-1307.
75. Sen S., Webber P.J., West A.B. Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization. The Journal of Biological Chemistry 2009, 284(52):36346-36356.
76. Sha D., Chin L.S., Li L. Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF-kappaB signaling. Human Molecular Genetics 2010, 19(2):352-363.
77. Simon-Sanchez J., Singleton A.B. Sequencing analysis of OMI/HTRA2 shows previously reported pathogenic mutations in neurologically normal controls. Human Molecular Genetics 2008, 17(13):1988-1993.
78. Simon-Sanchez J., Schulte C., Bras J.M., Sharma M., Gibbs J.R., Berg D., et al. Genome-wide association study reveals genetic risk underlying Parkinson's disease. Nature Genetics 2009, 41(12):1308-1312.
79. Singleton A.B., Farrer M., Johnson J., Singleton A., Hague S., Kachergus J., et al. alpha-Synuclein locus triplication causes Parkinson's disease. Science 2003, 302(5646):841.
80. Smith W.W., Pei Z., Jiang H., Dawson V.L., Dawson T.M., Ross C.A. Kinase activity of mutant LRRK2 mediates neuronal toxicity. Nature Neuroscience 2006, 9(10):1231-1233.
81. Smith W.W., Pei Z., Jiang H., Moore D.J., Liang Y., West A.B., et al. Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration. Proceedings of the National Academy of Sciences of the United States of America 2005, 102(51):18676-18681.
82. Spillantini M.G., Schmidt M.L., Lee V.M., Trojanowski J.Q., Jakes R., Goedert M. Alpha-synuclein in Lewy bodies. Nature 1997, 388(6645):839-840.
83. Stefansson H., Helgason A., Thorleifsson G., Steinthorsdottir V., Masson G., Barnard J., et al. A common inversion under selection in Europeans. Nature Genetics 2005, 37(2):129-137.
84. Strauss K.M., Martins L.M., Plun-Favreau H., Marx F.P., Kautzmann S., Berg D., et al. Loss of function mutations in the gene encoding Omi/HtrA2 in Parkinson's disease. Human Molecular Genetics 2005, 14(15):2099-2111.
85. Tan E.K. The role of common genetic risk variants in Parkinson disease. Clinical Genetics 2007, 72(5):387-393.
86. Taymans J.M., Cookson M.R. Mechanisms in dominant parkinsonism: The toxic triangle of LRRK2, alpha-synuclein, and tau. BioEssays 2010, 32(3):227-235.
87. Valente E.M., Abou-Sleiman P.M., Caputo V., Muqit M.M., Harvey K., Gispert S., et al. Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 2004, 304(5674):1158-1160.
88. Ved R., Saha S., Westlund B., Perier C., Burnam L., Sluder A., et al. Similar patterns of mitochondrial vulnerability and rescue induced by genetic modification of alpha-synuclein, parkin, and DJ-1 in Caenorhabditis elegans. The Journal of Biological Chemistry 2005, 280(52):42655-42668.
89. Vives-Bauza C., Zhou C., Huang Y., Cui M., de Vries R.L., Kim J., et al. PINK1-dependent recruitment of Parkin to mitochondria in mitophagy. Proceedings of the National Academy of Sciences of the United States of America 2010, 107(1):378-383.
90. Wood S.J., Wypych J., Steavenson S., Louis J.C., Citron M., Biere A.L. alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease. The Journal of Biological Chemistry 1999, 274(28):19509-19512.
91. Xu J., Kao S.Y., Lee F.J., Song W., Jin L.W., Yankner B.A. Dopamine-dependent neurotoxicity of alpha-synuclein: A mechanism for selective neurodegeneration in Parkinson disease. Nature Medicine 2002, 8(6):600-606.
92. Zarranz J.J., Alegre J., Gomez-Esteban J.C., Lezcano E., Ros R., Ampuero I., et al. The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia. Annals of Neurology 2004, 55(2):164-173.
93. Zhang L., Shimoji M., Thomas B., Moore D.J., Yu S.W., Marupudi N.I., et al. Mitochondrial localization of the Parkinson's disease related protein DJ-1: Implications for pathogenesis. Human Molecular Genetics 2005, 14(14):2063-2073.
94. Zhou C., Huang Y., Shao Y., May J., Prou D., Perier C., et al. The kinase domain of mitochondrial PINK1 faces the cytoplasm. Proceedings of the National Academy of Sciences of the United States of America 2008, 105(33):12022-12027.
95. Zimprich A., Biskup S., Leitner P., Lichtner P., Farrer M., Lincoln S., et al. Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology. Neuron 2004, 44(4):601-607.