메뉴 건너뛰기




Volumn 3, Issue 5, 2010, Pages 396-400

LRRK2 function on actin and microtubule dynamics in Parkinson disease

Author keywords

ERM; Filamentous actin; G2019S; Golgi apparatus; LRRK2; Microtubule; Neuronal morphogenesis; Parkinson disease; Phosphorylation; Tubulin

Indexed keywords


EID: 77958093993     PISSN: None     EISSN: 19420889     Source Type: Journal    
DOI: 10.4161/cib.3.5.12286     Document Type: Article
Times cited : (41)

References (56)
  • 1
    • 56249113020 scopus 로고    scopus 로고
    • The role of the cytoskeleton during neuronal polarization
    • Witte H, Bradke F. The role of the cytoskeleton during neuronal polarization. Curr Opin Neurobiol 2008; 18:479-87.
    • (2008) Curr Opin Neurobiol , vol.18 , pp. 479-487
    • Witte, H.1    Bradke, F.2
  • 2
    • 0033748308 scopus 로고    scopus 로고
    • Establishment of neuronal polarity: lessons from cultured hippocampal neurons
    • Bradke F, Dotti CG. Establishment of neuronal polarity: lessons from cultured hippocampal neurons. Curr Opin Neurobiol 2000; 10:574-81.
    • (2000) Curr Opin Neurobiol , vol.10 , pp. 574-581
    • Bradke, F.1    Dotti, C.G.2
  • 3
    • 0033770166 scopus 로고    scopus 로고
    • Neurodegeneration: diseases of the cytoskeleton?
    • McMurray CT. Neurodegeneration: diseases of the cytoskeleton? Cell Death Differ 2000; 7:861-5.
    • (2000) Cell Death Differ , vol.7 , pp. 861-865
    • McMurray, C.T.1
  • 4
    • 7944236911 scopus 로고    scopus 로고
    • The cytoskeleton in neurodegenerative diseases
    • Cairns NJ, Lee VM, Trojanowski JQ. The cytoskeleton in neurodegenerative diseases. J Pathol 2004; 204:438-49.
    • (2004) J Pathol , vol.204 , pp. 438-449
    • Cairns, N.J.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 5
    • 0026563548 scopus 로고
    • Filaments of Lewy bodies contain insoluble cytoskeletal elements
    • Galloway PG, Mulvihill P, Perry G. Filaments of Lewy bodies contain insoluble cytoskeletal elements. Am J Pathol 1992; 140:809-22.
    • (1992) Am J Pathol , vol.140 , pp. 809-822
    • Galloway, P.G.1    Mulvihill, P.2    Perry, G.3
  • 6
    • 67049159505 scopus 로고    scopus 로고
    • Is Alzheimer's disease a result of presynaptic failure? Synaptic dysfunctions induced by oligomeric beta-amyloid
    • Nimmrich V, Ebert U. Is Alzheimer's disease a result of presynaptic failure? Synaptic dysfunctions induced by oligomeric beta-amyloid. Rev Neurosci 2009; 20:1-12.
    • (2009) Rev Neurosci , vol.20 , pp. 1-12
    • Nimmrich, V.1    Ebert, U.2
  • 7
    • 73549085595 scopus 로고    scopus 로고
    • Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis
    • Nemani VM, Lu W, Berge V, Nakamura K, Onoa B, Lee MK, et al. Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis. Neuron 65:66-79.
    • Neuron , vol.65 , pp. 66-79
    • Nemani, V.M.1    Lu, W.2    Berge, V.3    Nakamura, K.4    Onoa, B.5    Lee, M.K.6
  • 8
    • 0022919318 scopus 로고
    • Beyond self-assembly: from microtubules to morphogenesis
    • Kirschner M, Mitchison T. Beyond self-assembly: from microtubules to morphogenesis. Cell 1986; 45:329-42.
    • (1986) Cell , vol.45 , pp. 329-342
    • Kirschner, M.1    Mitchison, T.2
  • 9
    • 0028787230 scopus 로고
    • Force generation by microtubule assembly/disassembly in mitosis and related movements
    • Inoue S, Salmon ED. Force generation by microtubule assembly/disassembly in mitosis and related movements. Mol Biol Cell 1995; 6:1619-40.
    • (1995) Mol Biol Cell , vol.6 , pp. 1619-1640
    • Inoue, S.1    Salmon, E.D.2
  • 10
    • 33745991140 scopus 로고    scopus 로고
    • Microtubule dynamic instability
    • Burbank KS, Mitchison TJ. Microtubule dynamic instability. Curr Biol 2006; 16:516-7.
    • (2006) Curr Biol , vol.16 , pp. 516-517
    • Burbank, K.S.1    Mitchison, T.J.2
  • 11
    • 65249107203 scopus 로고    scopus 로고
    • Microtubule assembly, organization and dynamics in axons and dendrites
    • Conde C, Caceres A. Microtubule assembly, organization and dynamics in axons and dendrites. Nature Rev Neurosci 2009; 10:319-32.
    • (2009) Nature Rev Neurosci , vol.10 , pp. 319-332
    • Conde, C.1    Caceres, A.2
  • 12
    • 33750466222 scopus 로고    scopus 로고
    • Microtubule: a common target for parkin and Parkinson's disease toxins
    • Feng J. Microtubule: a common target for parkin and Parkinson's disease toxins. Neuroscientist 2006; 12:469-76.
    • (2006) Neuroscientist , vol.12 , pp. 469-476
    • Feng, J.1
  • 13
    • 26644464601 scopus 로고    scopus 로고
    • Selective vulnerability of dopaminergic neurons to microtubule depolymerization
    • Ren Y, Liu W, Jiang H, Jiang Q, Feng J. Selective vulnerability of dopaminergic neurons to microtubule depolymerization. J Biol Chem 2005; 280:34105-12.
    • (2005) J Biol Chem , vol.280 , pp. 34105-34112
    • Ren, Y.1    Liu, W.2    Jiang, H.3    Jiang, Q.4    Feng, J.5
  • 14
    • 63649093151 scopus 로고    scopus 로고
    • Parkin protects dopaminergic neurons against microtubuledepolymerizing toxins by attenuating microtubuleassociated protein kinase activation
    • Ren Y, Jiang H, Yang F, Nakaso K, Feng J. Parkin protects dopaminergic neurons against microtubuledepolymerizing toxins by attenuating microtubuleassociated protein kinase activation. J Biol Chem 2009; 284:4009-17.
    • (2009) J Biol Chem , vol.284 , pp. 4009-4017
    • Ren, Y.1    Jiang, H.2    Yang, F.3    Nakaso, K.4    Feng, J.5
  • 16
    • 20444451210 scopus 로고    scopus 로고
    • Parkin stabilizes microtubules through strong binding mediated by three independent domains
    • Yang F, Jiang Q, Zhao J, Ren Y, Sutton MD, Feng J. Parkin stabilizes microtubules through strong binding mediated by three independent domains. J Biol Chem 2005; 280:17154-62.
    • (2005) J Biol Chem , vol.280 , pp. 17154-17162
    • Yang, F.1    Jiang, Q.2    Zhao, J.3    Ren, Y.4    Sutton, M.D.5    Feng, J.6
  • 17
    • 33845656077 scopus 로고    scopus 로고
    • Impairment of microtubule-dependent trafficking by overexpression of alpha-synuclein
    • Lee HJ, Khoshaghideh F, Lee S, Lee SJ. Impairment of microtubule-dependent trafficking by overexpression of alpha-synuclein. Eur J Neurosci 2006; 24:3153-62.
    • (2006) Eur J Neurosci , vol.24 , pp. 3153-3162
    • Lee, H.J.1    Khoshaghideh, F.2    Lee, S.3    Lee, S.J.4
  • 19
    • 34248595601 scopus 로고    scopus 로고
    • alpha-Synuclein and its disease-related mutants interact differentially with the microtubule protein tau and associate with the actin cytoskeleton
    • Esposito A, Dohm CP, Kermer P, Bahr M, Wouters FS. alpha-Synuclein and its disease-related mutants interact differentially with the microtubule protein tau and associate with the actin cytoskeleton. Neurobiol Disease 2007; 26:521-31.
    • (2007) Neurobiol Disease , vol.26 , pp. 521-531
    • Esposito, A.1    Dohm, C.P.2    Kermer, P.3    Bahr, M.4    Wouters, F.S.5
  • 20
    • 72549088299 scopus 로고    scopus 로고
    • PINK1 gene knockdown leads to increased binding of parkin with actin filament
    • Kim KH, Son JH. PINK1 gene knockdown leads to increased binding of parkin with actin filament. Neurosci Lett 2010; 468:272-6.
    • (2010) Neurosci Lett , vol.468 , pp. 272-276
    • Kim, K.H.1    Son, J.H.2
  • 21
    • 34547189670 scopus 로고    scopus 로고
    • Parkin interacts with LIM Kinase 1 and reduces its cofilin-phosphorylation activity via ubiquitination
    • Lim MK, Kawamura T, Ohsawa Y, Ohtsubo M, Asakawa S, Takayanagi A, et al. Parkin interacts with LIM Kinase 1 and reduces its cofilin-phosphorylation activity via ubiquitination. Exp Cell Res 2007; 313:2858-74.
    • (2007) Exp Cell Res , vol.313 , pp. 2858-2874
    • Lim, M.K.1    Kawamura, T.2    Ohsawa, Y.3    Ohtsubo, M.4    Asakawa, S.5    Takayanagi, A.6
  • 22
    • 70449377127 scopus 로고    scopus 로고
    • Phosphorylation of ezrin/radixin/moesin proteins by LRRK2 promotes the rearrangement of actin cytoskeleton in neuronal morphogenesis
    • Parisiadou L, Xie C, Cho HJ, Lin X, Gu XL, Long CX, et al. Phosphorylation of ezrin/radixin/moesin proteins by LRRK2 promotes the rearrangement of actin cytoskeleton in neuronal morphogenesis. J Neurosci 2009; 29:13971-80.
    • (2009) J Neurosci , vol.29 , pp. 13971-13980
    • Parisiadou, L.1    Xie, C.2    Cho, H.J.3    Lin, X.4    Gu, X.L.5    Long, C.X.6
  • 23
    • 0033583284 scopus 로고    scopus 로고
    • The role of local actin instability in axon formation
    • Bradke F, Dotti CG. The role of local actin instability in axon formation. Science 1999; 283:1931-4.
    • (1999) Science , vol.283 , pp. 1931-1934
    • Bradke, F.1    Dotti, C.G.2
  • 24
    • 70350417339 scopus 로고    scopus 로고
    • Cytoskeletal dynamics in growth-cone steering
    • Geraldo S, Gordon-Weeks PR. Cytoskeletal dynamics in growth-cone steering. J Cell Sci 2009; 122:3595-604.
    • (2009) J Cell Sci , vol.122 , pp. 3595-3604
    • Geraldo, S.1    Gordon-Weeks, P.R.2
  • 25
    • 4644291645 scopus 로고    scopus 로고
    • Analysis of alpha-synuclein-associated proteins by quantitative proteomics
    • Zhou Y, Gu G, Goodlett DR, Zhang T, Pan C, Montine TJ, et al. Analysis of alpha-synuclein-associated proteins by quantitative proteomics. J Biol Chem 2004; 279:39155-64.
    • (2004) J Biol Chem , vol.279 , pp. 39155-39164
    • Zhou, Y.1    Gu, G.2    Goodlett, D.R.3    Zhang, T.4    Pan, C.5    Montine, T.J.6
  • 26
    • 69149089036 scopus 로고    scopus 로고
    • Molecular pathogenesis of Parkinson disease: insights from genetic studies
    • Gasser T. Molecular pathogenesis of Parkinson disease: insights from genetic studies. Expert Rev Mol Med 2009; 11:22.
    • (2009) Expert Rev Mol Med , vol.11 , pp. 22
    • Gasser, T.1
  • 28
    • 70350450693 scopus 로고    scopus 로고
    • LRRK2 in Parkinson's disease: function in cells and neurodegeneration
    • Webber PJ, West AB. LRRK2 in Parkinson's disease: function in cells and neurodegeneration. FEBS J 2009; 276:6436-44.
    • (2009) FEBS J , vol.276 , pp. 6436-6444
    • Webber, P.J.1    West, A.B.2
  • 29
    • 34548604567 scopus 로고    scopus 로고
    • The Parkinson's disease-associated protein, leucine-rich repeat kinase 2 (LRRK2), is an authentic GTPase that stimulates kinase activity
    • Guo L, Gandhi PN, Wang W, Petersen RB, Wilson-Delfosse AL, Chen SG. The Parkinson's disease-associated protein, leucine-rich repeat kinase 2 (LRRK2), is an authentic GTPase that stimulates kinase activity. Exp Cell Res 2007; 313:3658-70.
    • (2007) Exp Cell Res , vol.313 , pp. 3658-3670
    • Guo, L.1    Gandhi, P.N.2    Wang, W.3    Petersen, R.B.4    Wilson-Delfosse, A.L.5    Chen, S.G.6
  • 30
    • 61349137536 scopus 로고    scopus 로고
    • LRRK2 and neurodegeneration
    • Santpere G, Ferrer I. LRRK2 and neurodegeneration. Acta Neuropathol 2009; 117:227-46.
    • (2009) Acta Neuropathol , vol.117 , pp. 227-246
    • Santpere, G.1    Ferrer, I.2
  • 31
    • 48749095219 scopus 로고    scopus 로고
    • Expression of the LRRK2 gene in the midbrain dopaminergic neurons of the substantia nigra
    • Han BS, Iacovitti L, Katano T, Hattori N, Seol W, Kim KS. Expression of the LRRK2 gene in the midbrain dopaminergic neurons of the substantia nigra. Neuroscience Lett 2008; 442:190-4.
    • (2008) Neuroscience Lett , vol.442 , pp. 190-194
    • Han, B.S.1    Iacovitti, L.2    Katano, T.3    Hattori, N.4    Seol, W.5    Kim, K.S.6
  • 33
  • 34
    • 68949125734 scopus 로고    scopus 로고
    • Zeroing in on LRRK2-linked pathogenic mechanisms in Parkinson's disease
    • Biskup S, West AB. Zeroing in on LRRK2-linked pathogenic mechanisms in Parkinson's disease. Biochim Biophys Acta 2009; 1792:625-33.
    • (2009) Biochim Biophys Acta , vol.1792 , pp. 625-633
    • Biskup, S.1    West, A.B.2
  • 36
    • 28044460070 scopus 로고    scopus 로고
    • Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity
    • West AB, Moore DJ, Biskup S, Bugayenko A, Smith WW, Ross CA, et al. Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity. Proc Natl Acad Sci USA 2005; 102:16842-7.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16842-16847
    • West, A.B.1    Moore, D.J.2    Biskup, S.3    Bugayenko, A.4    Smith, W.W.5    Ross, C.A.6
  • 37
    • 33751256567 scopus 로고    scopus 로고
    • The familial Parkinsonism gene LRRK2 regulates neurite process morphology
    • MacLeod D, Dowman J, Hammond R, Leete T, Inoue K, Abeliovich A. The familial Parkinsonism gene LRRK2 regulates neurite process morphology. Neuron 2006; 52:587-93.
    • (2006) Neuron , vol.52 , pp. 587-593
    • MacLeod, D.1    Dowman, J.2    Hammond, R.3    Leete, T.4    Inoue, K.5    Abeliovich, A.6
  • 38
    • 0032940071 scopus 로고    scopus 로고
    • ERM proteins in cell adhesion and membrane dynamics
    • Mangeat P, Roy C, Martin M. ERM proteins in cell adhesion and membrane dynamics. Trends Cell Biol 1999; 9:187-92.
    • (1999) Trends Cell Biol , vol.9 , pp. 187-192
    • Mangeat, P.1    Roy, C.2    Martin, M.3
  • 39
    • 0036346708 scopus 로고    scopus 로고
    • ERM proteins and merlin: integrators at the cell cortex
    • Bretscher A, Edwards K, Fehon RG. ERM proteins and merlin: integrators at the cell cortex. Nat Rev Mol Cell Biol 2002; 3:586-99.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 586-599
    • Bretscher, A.1    Edwards, K.2    Fehon, R.G.3
  • 40
    • 0027933858 scopus 로고
    • Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family
    • Turunen O, Wahlstrom T, Vaheri A. Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family. J Cell Biol 1994; 126:1445-53.
    • (1994) J Cell Biol , vol.126 , pp. 1445-1453
    • Turunen, O.1    Wahlstrom, T.2    Vaheri, A.3
  • 41
    • 0032547839 scopus 로고    scopus 로고
    • Suppression of radixin and moesin alters growth cone morphology, motility and process formation in primary cultured neurons
    • Paglini G, Kunda P, Quiroga S, Kosik K, Caceres A. Suppression of radixin and moesin alters growth cone morphology, motility and process formation in primary cultured neurons. J Cell Biol 1998; 143:443-55.
    • (1998) J Cell Biol , vol.143 , pp. 443-455
    • Paglini, G.1    Kunda, P.2    Quiroga, S.3    Kosik, K.4    Caceres, A.5
  • 42
    • 0028229539 scopus 로고
    • ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons
    • Tsukita S, Oishi K, Sato N, Sagara J, Kawai A, Tsukita S. ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons. J Cell Biol 1994; 126:391-401.
    • (1994) J Cell Biol , vol.126 , pp. 391-401
    • Tsukita, S.1    Oishi, K.2    Sato, N.3    Sagara, J.4    Kawai, A.5    Tsukita, S.6
  • 43
    • 0037730396 scopus 로고    scopus 로고
    • cAMP-induced AQP2 translocation is associated with RhoA inhibition through RhoA phosphorylation and interaction with RhoGDI
    • Tamma G, Klussmann E, Procino G, Svelto M, Rosenthal W, Valenti G. cAMP-induced AQP2 translocation is associated with RhoA inhibition through RhoA phosphorylation and interaction with RhoGDI. J Cell Sci 2003; 116:1519-25.
    • (2003) J Cell Sci , vol.116 , pp. 1519-1525
    • Tamma, G.1    Klussmann, E.2    Procino, G.3    Svelto, M.4    Rosenthal, W.5    Valenti, G.6
  • 44
    • 33846161917 scopus 로고    scopus 로고
    • Rho kinase activates ezrin-radixin-moesin (ERM) proteins and mediates their function in cortical neuron growth, morphology and motility in vitro
    • Haas MA, Vickers JC, Dickson TC. Rho kinase activates ezrin-radixin-moesin (ERM) proteins and mediates their function in cortical neuron growth, morphology and motility in vitro. J Neurosci Res 2007; 85:34-46.
    • (2007) J Neurosci Res , vol.85 , pp. 34-46
    • Haas, M.A.1    Vickers, J.C.2    Dickson, T.C.3
  • 46
    • 31144443248 scopus 로고    scopus 로고
    • The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity
    • Gloeckner CJ, Kinkl N, Schumacher A, Braun RJ, O'Neill E, Meitinger T, et al. The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity. Hum Mol Genet 2006; 15:223-32.
    • (2006) Hum Mol Genet , vol.15 , pp. 223-232
    • Gloeckner, C.J.1    Kinkl, N.2    Schumacher, A.3    Braun, R.J.4    O'Neill, E.5    Meitinger, T.6
  • 47
    • 45549085874 scopus 로고    scopus 로고
    • The Roc domain of leucine-rich repeat kinase 2 is sufficient for interaction with microtubules
    • Gandhi PN, Wang X, Zhu X, Chen SG, Wilson-Delfosse AL. The Roc domain of leucine-rich repeat kinase 2 is sufficient for interaction with microtubules. J Neurosci Res 2008; 86:1711-20.
    • (2008) J Neurosci Res , vol.86 , pp. 1711-1720
    • Gandhi, P.N.1    Wang, X.2    Zhu, X.3    Chen, S.G.4    Wilson-Delfosse, A.L.5
  • 48
    • 72149087091 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 regulates the progression of neuropathology induced by Parkinson'sdisease-related mutant alpha-synuclein
    • Lin X, Parisiadou L, Gu XL, Wang L, Shim H, Sun L, et al. Leucine-rich repeat kinase 2 regulates the progression of neuropathology induced by Parkinson'sdisease-related mutant alpha-synuclein. Neuron 2009; 64:807-27.
    • (2009) Neuron , vol.64 , pp. 807-827
    • Lin, X.1    Parisiadou, L.2    Gu, X.L.3    Wang, L.4    Shim, H.5    Sun, L.6
  • 49
    • 0031039519 scopus 로고    scopus 로고
    • Tubulin post-translational modifications-enzymes and their mechanisms of action
    • MacRae TH. Tubulin post-translational modifications-enzymes and their mechanisms of action. Eur J Biochem 1997; 244:265-78.
    • (1997) Eur J Biochem , vol.244 , pp. 265-278
    • MacRae, T.H.1
  • 50
    • 68949218403 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 phosphorylates brain tubulin-beta isoforms and modulates microtubule stability-a point of convergence in parkinsonian neurodegeneration?
    • Gillardon F. Leucine-rich repeat kinase 2 phosphorylates brain tubulin-beta isoforms and modulates microtubule stability-a point of convergence in parkinsonian neurodegeneration? J Neurochem 2009; 110:1514-22.
    • (2009) J Neurochem , vol.110 , pp. 1514-1522
    • Gillardon, F.1
  • 52
    • 0028950267 scopus 로고
    • Organization of organelles and membrane traffic by microtubules
    • Cole NB, Lippincott-Schwartz J. Organization of organelles and membrane traffic by microtubules. Curr Opinion Cell Biol 1995; 7:55-64.
    • (1995) Curr Opinion Cell Biol , vol.7 , pp. 55-64
    • Cole, N.B.1    Lippincott-Schwartz, J.2
  • 53
    • 0032578031 scopus 로고    scopus 로고
    • Microtubule-based membrane movement
    • Lane J, Allan V. Microtubule-based membrane movement. Biochim Biophys Acta 1998; 1376:27-55.
    • (1998) Biochim Biophys Acta , vol.1376 , pp. 27-55
    • Lane, J.1    Allan, V.2
  • 54
    • 0022412716 scopus 로고
    • Microtubules and the organization of the Golgi complex
    • Thyberg J, Moskalewski S. Microtubules and the organization of the Golgi complex. Exp Cell Res 1985; 159:1-16.
    • (1985) Exp Cell Res , vol.159 , pp. 1-16
    • Thyberg, J.1    Moskalewski, S.2
  • 55
    • 0033080404 scopus 로고    scopus 로고
    • Role of microtubules in the organization of the Golgi complex
    • Thyberg J, Moskalewski S. Role of microtubules in the organization of the Golgi complex. Exp Cell Res 1999; 246:263-79.
    • (1999) Exp Cell Res , vol.246 , pp. 263-279
    • Thyberg, J.1    Moskalewski, S.2
  • 56
    • 0006327768 scopus 로고
    • Role of microtubules in the distribution of the Golgi apparatus: effect of taxol and microinjected anti-alpha-tubulin antibodies
    • Wehland J, Henkart M, Klausner R, Sandoval IV. Role of microtubules in the distribution of the Golgi apparatus: effect of taxol and microinjected anti-alpha-tubulin antibodies. Proc Natl Acad Sci USA 1983; 80:4286-90.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 4286-4290
    • Wehland, J.1    Henkart, M.2    Klausner, R.3    Sandoval, I.V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.