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Volumn 105, Issue 33, 2008, Pages 12022-12027

The kinase domain of mitochondrial PINK1 faces the cytoplasm

Author keywords

Mitochondria; Parkin; Parkinson's disease; Topology

Indexed keywords

BIOLOGICAL MARKER; MITOCHONDRIAL PROTEIN; PHOSPHOTRANSFERASE; PINK1 ENZYME; PROTEIN KINASE; SMALL INTERFERING RNA;

EID: 50149121528     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0802814105     Document Type: Article
Times cited : (272)

References (40)
  • 1
    • 3142523288 scopus 로고    scopus 로고
    • Genetic clues to the pathogenesis of Parkinson's disease
    • Vila M, Przedborski S (2004) Genetic clues to the pathogenesis of Parkinson's disease. Nat Med 10 Suppl:S58-S62.
    • (2004) Nat Med , vol.10 , Issue.SUPPL.
    • Vila, M.1    Przedborski, S.2
  • 2
    • 34447307390 scopus 로고    scopus 로고
    • Impact of recent genetic findings in Parkinson's disease
    • Klein C, Lohmann-Hedrich K (2007) Impact of recent genetic findings in Parkinson's disease. Curr Opin Neurol 20:453-464.
    • (2007) Curr Opin Neurol , vol.20 , pp. 453-464
    • Klein, C.1    Lohmann-Hedrich, K.2
  • 3
    • 2442668926 scopus 로고    scopus 로고
    • Hereditary early-onset Parkinson's disease caused by mutations in PINK1
    • Valente EM, et al. (2004) Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 304:1158-1160.
    • (2004) Science , vol.304 , pp. 1158-1160
    • Valente, E.M.1
  • 4
    • 27144469287 scopus 로고    scopus 로고
    • Small interfering RNA targeting the PINK1 induces apoptosis in dopaminergic cells SH-SY5Y
    • Deng H, Jankovic J, Guo Y, Xie W, Le W (2005) Small interfering RNA targeting the PINK1 induces apoptosis in dopaminergic cells SH-SY5Y. Biochem Biophys ResCommun 337:1133-1138.
    • (2005) Biochem Biophys ResCommun , vol.337 , pp. 1133-1138
    • Deng, H.1    Jankovic, J.2    Guo, Y.3    Xie, W.4    Le, W.5
  • 5
    • 26644440926 scopus 로고    scopus 로고
    • Wild-type PINK1 prevents basal and induced neuronal apoptosis, a protective effect abrogated by Parkinson disease-related mutations
    • Petit A, et al. (2005) Wild-type PINK1 prevents basal and induced neuronal apoptosis, a protective effect abrogated by Parkinson disease-related mutations. J Biol Chem 280:34025-34032.
    • (2005) J Biol Chem , vol.280 , pp. 34025-34032
    • Petit, A.1
  • 6
    • 27944444154 scopus 로고    scopus 로고
    • Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism
    • Silvestri L, et al. (2005) Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism. Hum Mol Genet 14:3477-3492.
    • (2005) Hum Mol Genet , vol.14 , pp. 3477-3492
    • Silvestri, L.1
  • 7
    • 33745087689 scopus 로고    scopus 로고
    • PINK1 protein in normal human brain and Parkinson's disease
    • Gandhi S, et al. (2006) PINK1 protein in normal human brain and Parkinson's disease. Brain 129:1720-1731.
    • (2006) Brain , vol.129 , pp. 1720-1731
    • Gandhi, S.1
  • 8
    • 35748935851 scopus 로고    scopus 로고
    • The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1
    • Plun-Favreau H, et al. (2007) The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1. Nat Cell Biol 9:1243-1252.
    • (2007) Nat Cell Biol , vol.9 , pp. 1243-1252
    • Plun-Favreau, H.1
  • 9
    • 34547127902 scopus 로고    scopus 로고
    • PINK1 Protects against Oxidative Stress by Phosphorylating Mitochondrial Chaperone TRAP1
    • Pridgeon JW, Olzmann JA, Chin LS, Li L (2007) PINK1 Protects against Oxidative Stress by Phosphorylating Mitochondrial Chaperone TRAP1. PLoS Biol 5:e172.
    • (2007) PLoS Biol , vol.5
    • Pridgeon, J.W.1    Olzmann, J.A.2    Chin, L.S.3    Li, L.4
  • 10
    • 36049038504 scopus 로고    scopus 로고
    • Loss-of-function of human PINK1 results in mitochondrial pathology and can be rescued by parkin
    • Exner N, et al. (2007) Loss-of-function of human PINK1 results in mitochondrial pathology and can be rescued by parkin. J Neurosci 27:12413-12418.
    • (2007) J Neurosci , vol.27 , pp. 12413-12418
    • Exner, N.1
  • 11
    • 10044275502 scopus 로고    scopus 로고
    • Analysis of the PINK1 gene in a large cohort of cases with Parkinson disease
    • Rogaeva E, et al. (2004) Analysis of the PINK1 gene in a large cohort of cases with Parkinson disease. Arch Neurol 61:1898-1904.
    • (2004) Arch Neurol , vol.61 , pp. 1898-1904
    • Rogaeva, E.1
  • 12
    • 4444269012 scopus 로고    scopus 로고
    • Homozygous PINK1 C-terminus mutation causing early-onset parkinsonism
    • Rohe CF, et al. (2004) Homozygous PINK1 C-terminus mutation causing early-onset parkinsonism. Ann Neurol 56:427-431.
    • (2004) Ann Neurol , vol.56 , pp. 427-431
    • Rohe, C.F.1
  • 13
    • 0242321145 scopus 로고    scopus 로고
    • BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential
    • Nakajima A, Kataoka K, Hong M, Sakaguchi M, Huh NH (2003) BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential. Cancer Lett 201:195-201.
    • (2003) Cancer Lett , vol.201 , pp. 195-201
    • Nakajima, A.1    Kataoka, K.2    Hong, M.3    Sakaguchi, M.4    Huh, N.H.5
  • 14
    • 0035958558 scopus 로고    scopus 로고
    • Growth-suppressive effects of BPOZ and EGR2, two genes involved in the PTEN signaling pathway
    • Unoki M, Nakamura Y (2001) Growth-suppressive effects of BPOZ and EGR2, two genes involved in the PTEN signaling pathway. Oncogene 20:4457-4465.
    • (2001) Oncogene , vol.20 , pp. 4457-4465
    • Unoki, M.1    Nakamura, Y.2
  • 15
    • 33745589773 scopus 로고    scopus 로고
    • Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
    • Clark IE, et al. (2006) Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 441:1162-1166.
    • (2006) Nature , vol.441 , pp. 1162-1166
    • Clark, I.E.1
  • 16
    • 33745602748 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
    • Park J, et al. (2006) Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature 441:1157-1161.
    • (2006) Nature , vol.441 , pp. 1157-1161
    • Park, J.1
  • 17
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • Kitada T, et al. (1998) Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392:605-608.
    • (1998) Nature , vol.392 , pp. 605-608
    • Kitada, T.1
  • 18
    • 39449088321 scopus 로고    scopus 로고
    • The PINK1/Parkin pathway regulates mitochondrial morphology
    • Poole AC, et al. (2008) The PINK1/Parkin pathway regulates mitochondrial morphology. Proc Natl Acad Sci USA 105:1638-1643.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 1638-1643
    • Poole, A.C.1
  • 19
    • 0037338634 scopus 로고    scopus 로고
    • Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death
    • Darios F, et al. (2003) Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death. Hum Mol Genet 12:517-526.
    • (2003) Hum Mol Genet , vol.12 , pp. 517-526
    • Darios, F.1
  • 20
    • 33745068109 scopus 로고    scopus 로고
    • Altered cleavage and localization of PINK1 to aggresomes in the presence of proteasomal stress
    • Muqit MM, et al. (2006) Altered cleavage and localization of PINK1 to aggresomes in the presence of proteasomal stress. J Neurochem 98:156-169.
    • (2006) J Neurochem , vol.98 , pp. 156-169
    • Muqit, M.M.1
  • 21
    • 17644365438 scopus 로고    scopus 로고
    • Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability
    • Beilina A, et al. (2005) Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability. Proc Natl Acad Sci USA 102:5703-5708.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5703-5708
    • Beilina, A.1
  • 22
    • 39449098267 scopus 로고    scopus 로고
    • Cytoplasmic Pink1 activity protects neurons from dopaminergic neurotoxin MPTP
    • Haque ME, et al. (2008) Cytoplasmic Pink1 activity protects neurons from dopaminergic neurotoxin MPTP. Proc Natl Acad Sci USA 105:1716-1721.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 1716-1721
    • Haque, M.E.1
  • 23
    • 37549029702 scopus 로고    scopus 로고
    • Cytoplasmic localization and proteasomal degradation of N-terminally cleaved form of PINK1
    • Takatori S, Ito G, Iwatsubo T (2008) Cytoplasmic localization and proteasomal degradation of N-terminally cleaved form of PINK1. Neurosci Lett 430:13-17.
    • (2008) Neurosci Lett , vol.430 , pp. 13-17
    • Takatori, S.1    Ito, G.2    Iwatsubo, T.3
  • 24
    • 38849155699 scopus 로고    scopus 로고
    • Pink1 Parkinson mutations, the Cdc37/Hsp90 chaperones and Parkin all influence the maturation or subcellular distribution of Pink1
    • Weihofen A, Ostaszewski B, MinamiY, Selkoe DJ (2008) Pink1 Parkinson mutations, the Cdc37/Hsp90 chaperones and Parkin all influence the maturation or subcellular distribution of Pink1. Hum Mol Genet 17:602-616.
    • (2008) Hum Mol Genet , vol.17 , pp. 602-616
    • Weihofen, A.1    Ostaszewski, B.2    Minami, Y.3    Selkoe, D.J.4
  • 25
    • 0034633963 scopus 로고    scopus 로고
    • Immunoelectron microscopy provides evidence that tumor necrosis factor receptor-associated protein 1 (TRAP-1) is a mitochondrial protein which also localizes at specific extramitochondrial sites
    • Cechetto JD, Gupta RS (2000) Immunoelectron microscopy provides evidence that tumor necrosis factor receptor-associated protein 1 (TRAP-1) is a mitochondrial protein which also localizes at specific extramitochondrial sites. Exp Cell Res 260:30-39.
    • (2000) Exp Cell Res , vol.260 , pp. 30-39
    • Cechetto, J.D.1    Gupta, R.S.2
  • 26
    • 0034785591 scopus 로고    scopus 로고
    • A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death
    • Suzuki Y, et al. (2001) A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Mol Cell 8:613-621.
    • (2001) Mol Cell , vol.8 , pp. 613-621
    • Suzuki, Y.1
  • 27
    • 0035900732 scopus 로고    scopus 로고
    • Mitochondrial glycerol phosphate acyltransferase contains two transmembrane domains with the active site in the N-terminal domain facing the cytosol
    • ColemanRA
    • Gonzalez-Baro MR, Granger DA, ColemanRA(2001) Mitochondrial glycerol phosphate acyltransferase contains two transmembrane domains with the active site in the N-terminal domain facing the cytosol. J Biol Chem 276:43182-43188.
    • (2001) J Biol Chem , vol.276 , pp. 43182-43188
    • Gonzalez-Baro, M.R.1    Granger, D.A.2
  • 28
    • 0034640088 scopus 로고    scopus 로고
    • Tim23 links the inner and outer mitochondrial membranes
    • Donzeau M, et al. (2000) Tim23 links the inner and outer mitochondrial membranes. Cell 101:401-412.
    • (2000) Cell , vol.101 , pp. 401-412
    • Donzeau, M.1
  • 29
    • 2642587490 scopus 로고    scopus 로고
    • Tim50, a component of the mitochondrial translocator, regulates mitochondrial integrity and cell death
    • Guo Y, et al. (2004) Tim50, a component of the mitochondrial translocator, regulates mitochondrial integrity and cell death. J Biol Chem 279:24813-24825.
    • (2004) J Biol Chem , vol.279 , pp. 24813-24825
    • Guo, Y.1
  • 30
    • 33745917404 scopus 로고    scopus 로고
    • Distribution of PINK1 and LRRK2 in rat and mouse brain
    • Taymans JM, Van den HC, Baekelandt V (2006) Distribution of PINK1 and LRRK2 in rat and mouse brain. J Neurochem 98:951-961.
    • (2006) J Neurochem , vol.98 , pp. 951-961
    • Taymans1    JM, V.D.H.2    Baekelandt, V.3
  • 31
    • 36448932411 scopus 로고    scopus 로고
    • Expression of PINK1 mRNA in human and rodent brain and in Parkinson's disease
    • Blackinton JG, et al. (2007) Expression of PINK1 mRNA in human and rodent brain and in Parkinson's disease. Brain Res 1184:10-16.
    • (2007) Brain Res , vol.1184 , pp. 10-16
    • Blackinton, J.G.1
  • 33
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence NF, Sampat RM, Kopito RR (2001) Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292:1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 34
    • 0035344460 scopus 로고    scopus 로고
    • Versatility of the mitochondrial protein import machinery
    • GeisslerA
    • Pfanner N, GeisslerA(2001) Versatility of the mitochondrial protein import machinery. Nat Rev Mol Cell Biol 2:339-349.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 339-349
    • Pfanner, N.1
  • 35
    • 0016815025 scopus 로고
    • The distribution of anionic sites on the surfaces of mitochondrial membranes. Visual probing with polycationic ferritin
    • Hackenbrock CR, Miller KJ (1975) The distribution of anionic sites on the surfaces of mitochondrial membranes. Visual probing with polycationic ferritin. J Cell Biol 65:615-630.
    • (1975) J Cell Biol , vol.65 , pp. 615-630
    • Hackenbrock, C.R.1    Miller, K.J.2
  • 36
    • 1442337560 scopus 로고    scopus 로고
    • Mmm1p spans both the outer and inner mitochondrial membranes and contains distinct domains for targeting and foci formation
    • Kondo-Okamoto N, Shaw JM, Okamoto K (2003) Mmm1p spans both the outer and inner mitochondrial membranes and contains distinct domains for targeting and foci formation. J Biol Chem 278:48997-49005.
    • (2003) J Biol Chem , vol.278 , pp. 48997-49005
    • Kondo-Okamoto, N.1    Shaw, J.M.2    Okamoto, K.3
  • 37
    • 0028129071 scopus 로고
    • MMM1 encodes a mitochondrial outer membrane protein essential for establishing and maintaining the structure of yeast mitochondria
    • Burgess SM, Delannoy M, Jensen RE (1994) MMM1 encodes a mitochondrial outer membrane protein essential for establishing and maintaining the structure of yeast mitochondria. J Cell Biol 126:1375-1391.
    • (1994) J Cell Biol , vol.126 , pp. 1375-1391
    • Burgess, S.M.1    Delannoy, M.2    Jensen, R.E.3
  • 38
    • 0035931747 scopus 로고    scopus 로고
    • Mmm1p, a mitochondrial outer membrane protein, is connected to mitochondrial DNA (mtDNA) nucleoids and required for mtDNA stability
    • Hobbs AE, Srinivasan M, McCaffery JM, Jensen RE (2001) Mmm1p, a mitochondrial outer membrane protein, is connected to mitochondrial DNA (mtDNA) nucleoids and required for mtDNA stability. J Cell Biol 152:401-410.
    • (2001) J Cell Biol , vol.152 , pp. 401-410
    • Hobbs, A.E.1    Srinivasan, M.2    McCaffery, J.M.3    Jensen, R.E.4
  • 39
    • 33645798615 scopus 로고    scopus 로고
    • Spinal cord endoplasmic reticulum stress associated with a microsomal accumulation of mutant superoxide dismutase-1 in an ALS model
    • Kikuchi H, et al. (2006) Spinal cord endoplasmic reticulum stress associated with a microsomal accumulation of mutant superoxide dismutase-1 in an ALS model. Proc Natl Acad Sci USA 103:6025-6030.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 6025-6030
    • Kikuchi, H.1
  • 40
    • 34249947154 scopus 로고    scopus 로고
    • Two molecular pathways initiate mitochondria-dependent dopaminergic neurodegeneration in experimental Parkinson's disease
    • Perier C, et al. (2007) Two molecular pathways initiate mitochondria-dependent dopaminergic neurodegeneration in experimental Parkinson's disease. Proc Natl Acad Sci USA 104:8161-8166.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8161-8166
    • Perier, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.