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Volumn 24, Issue 17, 2015, Pages 4879-4900

I2020T mutant LRRK2 iPSC-derived neurons in the Sagamihara family exhibit increased Tau phosphorylation through the AKT/GSK-3ß signaling pathway

(19)  Ohta, Etsuro a,b   Nihira, Tomoko a,b   Uchino, Akiko a,c   Imaizumi, Yoichi b   Okada, Yohei b,d   Akamatsu, Wado b,e   Takahashi, Kayoko f   Hayakawa, Hideki a   Nagai, Makiko g   Ohyama, Manabu b   Ryo, Masafuchi g   Ogino, Mieko g   Murayama, Shigeo c   Takashima, Akihiko h   Nishiyama, Kazutoshi a,g   Mizuno, Yoshikuni a   Mochizuki, Hideki i   Obata, Fumiya a   Okano, Hideyuki b  


Author keywords

[No Author keywords available]

Indexed keywords

DOPAMINE; GLYCOGEN SYNTHASE KINASE 3BETA; LEUCINE RICH REPEAT KINASE 2; PROTEIN KINASE B; TAU PROTEIN; CASPASE 3; GLYCOGEN SYNTHASE KINASE 3; GLYCOGEN SYNTHASE KINASE 3 BETA; LRRK2 PROTEIN, HUMAN; PROTEIN SERINE THREONINE KINASE;

EID: 84941886639     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddv212     Document Type: Article
Times cited : (54)

References (62)
  • 4
    • 68649110032 scopus 로고    scopus 로고
    • Mendelian forms of Parkinson's disease
    • Gasser, T. (2009) Mendelian forms of Parkinson's disease. Biochim Biophys Acta., 1792, 587-596.
    • (2009) Biochim Biophys Acta. , vol.1792 , pp. 587-596
    • Gasser, T.1
  • 5
    • 80054787664 scopus 로고    scopus 로고
    • What genetics tells us about the causes and mechanisms of Parkinson's disease
    • Corti, O., Lesage, S. and Brice, A. (2011) What genetics tells us about the causes and mechanisms of Parkinson's disease. Physiol. Rev., 91, 1161-1218.
    • (2011) Physiol. Rev. , vol.91 , pp. 1161-1218
    • Corti, O.1    Lesage, S.2    Brice, A.3
  • 6
    • 79960210306 scopus 로고    scopus 로고
    • Genetic characteristics of leucine-rich repeat kinase 2 (LRRK2) associated Parkinson's disease
    • Bardien, S., Lesage, S., Brice, A. and Carr, J. (2011) Genetic characteristics of leucine-rich repeat kinase 2 (LRRK2) associated Parkinson's disease. Parkinsonism Relat. Disord., 17, 501-508.
    • (2011) Parkinsonism Relat. Disord. , vol.17 , pp. 501-508
    • Bardien, S.1    Lesage, S.2    Brice, A.3    Carr, J.4
  • 7
    • 14744299357 scopus 로고    scopus 로고
    • The RIP kinases: crucial integrators of cellular stress
    • Meylan, E. and Tschopp, J. (2005) The RIP kinases: crucial integrators of cellular stress. Trends Biochem. Sci., 30, 151-159.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 151-159
    • Meylan, E.1    Tschopp, J.2
  • 9
    • 51949090816 scopus 로고    scopus 로고
    • Phosphorylation of 4E-BP by LRRK2 affects the maintenance of dopaminergic neurons in Drosophila
    • Imai, Y., Gehrke, S.,Wang, H.Q., Takahashi, R., Hasegawa, K., Oota, E. and Lu, B. (2008) Phosphorylation of 4E-BP by LRRK2 affects the maintenance of dopaminergic neurons in Drosophila. EMBO J., 27, 2432-2443.
    • (2008) EMBO J. , vol.27 , pp. 2432-2443
    • Imai, Y.1    Gehrke, S.2    Wang, H.Q.3    Takahashi, R.4    Hasegawa, K.5    Oota, E.6    Lu, B.7
  • 10
    • 34447118788 scopus 로고    scopus 로고
    • LRRK2 phosphorylates moesin at threonine-558: characterization of howParkinson's disease mutants affect kinase activity
    • Jaleel, M., Nichols, R.J., Deak, M., Campbell, D.G., Gillardon, F., Knebel, A. and Alessi, D.R. (2007) LRRK2 phosphorylates moesin at threonine-558: characterization of howParkinson's disease mutants affect kinase activity. Biochem. J., 405, 307-317.
    • (2007) Biochem. J. , vol.405 , pp. 307-317
    • Jaleel, M.1    Nichols, R.J.2    Deak, M.3    Campbell, D.G.4    Gillardon, F.5    Knebel, A.6    Alessi, D.R.7
  • 11
    • 84856404449 scopus 로고    scopus 로고
    • LRRK2 phosphorylates tubulin-associated tau but not the free molecule: LRRK2-mediated regulation of the tau-tubulin association and neurite outgrowth
    • Kawakami, F., Yabata, T., Ohta, E., Maekawa, T., Shimada, N., Suzuki, M., Maruyama, H., Ichikawa, T. and Obata, F. (2012) LRRK2 phosphorylates tubulin-associated tau but not the free molecule: LRRK2-mediated regulation of the tau-tubulin association and neurite outgrowth. PLoS One, 7, e30834.
    • (2012) PLoS One , vol.7
    • Kawakami, F.1    Yabata, T.2    Ohta, E.3    Maekawa, T.4    Shimada, N.5    Suzuki, M.6    Maruyama, H.7    Ichikawa, T.8    Obata, F.9
  • 16
    • 34548432121 scopus 로고    scopus 로고
    • Mechanistic insight into the dominant mode of the Parkinson's disease-associated G2019S LRRK2 mutation
    • Luzon-Toro, B., de la Torre, E.R., Delgado, A., Perez-Tur, J. and Hilfiker, S. (2007) Mechanistic insight into the dominant mode of the Parkinson's disease-associated G2019S LRRK2 mutation. Hum. Mol. Genet., 16, 2031-2039.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 2031-2039
    • Luzon-Toro, B.1    de la Torre, E.R.2    Delgado, A.3    Perez-Tur, J.4    Hilfiker, S.5
  • 18
    • 77953395313 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 mutations and Parkinson's disease: three questions
    • Greggio, E. and Cookson, M.R. (2009) Leucine-rich repeat kinase 2 mutations and Parkinson's disease: three questions. ASN Neuro, 1, e00002.
    • (2009) ASN Neuro , vol.1
    • Greggio, E.1    Cookson, M.R.2
  • 19
    • 79960346073 scopus 로고    scopus 로고
    • LRRK2 directly phosphorylates Akt1 as a possible physiological substrate: impairment of the kinase activity by Parkinson's disease-associated mutations
    • Ohta, E., Kawakami, F., Kubo, M. and Obata, F. (2011) LRRK2 directly phosphorylates Akt1 as a possible physiological substrate: impairment of the kinase activity by Parkinson's disease-associated mutations. FEBS Lett., 585, 2165-2170.
    • (2011) FEBS Lett. , vol.585 , pp. 2165-2170
    • Ohta, E.1    Kawakami, F.2    Kubo, M.3    Obata, F.4
  • 20
    • 84872320159 scopus 로고    scopus 로고
    • Dominant-negative effects of LRRK2 heterodimers: a possible mechanism of neurodegeneration in Parkinson's disease caused by LRRK2 I2020T mutation
    • Ohta, E., Kawakami, F., Kubo, M. and Obata, F. (2013) Dominant-negative effects of LRRK2 heterodimers: a possible mechanism of neurodegeneration in Parkinson's disease caused by LRRK2 I2020T mutation. Biochem. Biophys. Res. Commun., 430, 560-566.
    • (2013) Biochem. Biophys. Res. Commun. , vol.430 , pp. 560-566
    • Ohta, E.1    Kawakami, F.2    Kubo, M.3    Obata, F.4
  • 21
    • 39549117093 scopus 로고    scopus 로고
    • Role of autophagy in G2019S-LRRK2-associated neurite shortening in differentiated SH-SY5Y cells
    • Plowey, E.D., Cherra, S.J. 3rd, Liu, Y.J. and Chu, C.T. (2008) Role of autophagy in G2019S-LRRK2-associated neurite shortening in differentiated SH-SY5Y cells. J. Neurochem., 105, 1048-1056.
    • (2008) J. Neurochem. , vol.105 , pp. 1048-1056
    • Plowey, E.D.1    Cherra 3rd, S.J.2    Liu, Y.J.3    Chu, C.T.4
  • 28
    • 84867031150 scopus 로고    scopus 로고
    • Mitochondrial dysfunction associated with increased oxidative stress and a-synuclein accumulation in PARK2 iPSC-derived neurons and postmortem brain tissue
    • Imaizumi, Y., Okada, Y., Akamatsu,W., Koike, M., Kuzumaki, N., Hayakawa, H., Nihira, T., Kobayashi, T., Ohyama, M., Sato, S. et al. (2012) Mitochondrial dysfunction associated with increased oxidative stress and a-synuclein accumulation in PARK2 iPSC-derived neurons and postmortem brain tissue. Mol. Brain, 5, 35.
    • (2012) Mol. Brain , vol.5 , pp. 35
    • Imaizumi, Y.1    Okada, Y.2    Akamatsu, W.3    Koike, M.4    Kuzumaki, N.5    Hayakawa, H.6    Nihira, T.7    Kobayashi, T.8    Ohyama, M.9    Sato, S.10
  • 29
    • 36248966518 scopus 로고    scopus 로고
    • Induction of pluripotent stem cells from adult human fibroblasts by defined factors
    • Takahashi, K., Tanabe, K., Ohnuki, M., Narita, M., Ichisaka, T., Tomoda, K. and Yamanaka, S. (2007) Induction of pluripotent stem cells from adult human fibroblasts by defined factors. Cell, 131, 861-872.
    • (2007) Cell , vol.131 , pp. 861-872
    • Takahashi, K.1    Tanabe, K.2    Ohnuki, M.3    Narita, M.4    Ichisaka, T.5    Tomoda, K.6    Yamanaka, S.7
  • 31
    • 64249149785 scopus 로고    scopus 로고
    • Familial parkinsonism: study of original Sagamihara PARK8 (I2020T) kindred with variable clinicopathologic outcomes
    • Hasegawa, K., Stoessl, A.J., Yokoyama, T., Kowa, H., Wszolek, Z.K. and Yagishita, S. (2009) Familial parkinsonism: study of original Sagamihara PARK8 (I2020T) kindred with variable clinicopathologic outcomes. Parkinsonism Relat. Disord., 15, 300-306.
    • (2009) Parkinsonism Relat. Disord. , vol.15 , pp. 300-306
    • Hasegawa, K.1    Stoessl, A.J.2    Yokoyama, T.3    Kowa, H.4    Wszolek, Z.K.5    Yagishita, S.6
  • 32
    • 84864384240 scopus 로고    scopus 로고
    • The relationship between subcortical tau pathology and Alzheimer's disease
    • Attems, J., Thal, D.R. and Jellinger, K.A. (2012) The relationship between subcortical tau pathology and Alzheimer's disease. Biochem. Soc. Trans., 40, 711-715.
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 711-715
    • Attems, J.1    Thal, D.R.2    Jellinger, K.A.3
  • 33
    • 70449732111 scopus 로고    scopus 로고
    • I2020T leucine-rich repeat kinase 2, the causative mutant molecule of familial Parkinson's disease, has a higher intracellular degradation rate than the wild-type molecule
    • Ohta, E., Katayama, Y., Kawakami, F., Yamamoto, M., Tajima, K., Maekawa, T., Iida, N., Hattori, S. and Obata, F. (2009) I2020T leucine-rich repeat kinase 2, the causative mutant molecule of familial Parkinson's disease, has a higher intracellular degradation rate than the wild-type molecule. Biochem. Biophys. Res. Commun., 390, 710-715.
    • (2009) Biochem. Biophys. Res. Commun. , vol.390 , pp. 710-715
    • Ohta, E.1    Katayama, Y.2    Kawakami, F.3    Yamamoto, M.4    Tajima, K.5    Maekawa, T.6    Iida, N.7    Hattori, S.8    Obata, F.9
  • 34
    • 72949106466 scopus 로고    scopus 로고
    • Prevention of intracellular degradation of I2020T mutant LRRK2 restores its protectivity against apoptosis
    • Ohta, E., Kubo, M. and Obata, F. (2010) Prevention of intracellular degradation of I2020T mutant LRRK2 restores its protectivity against apoptosis. Biochem. Biophys. Res. Commun., 391, 242-247.
    • (2010) Biochem. Biophys. Res. Commun. , vol.391 , pp. 242-247
    • Ohta, E.1    Kubo, M.2    Obata, F.3
  • 35
    • 84895065892 scopus 로고    scopus 로고
    • Evidence that the LRRK2 ROC domain Parkinson's disease-associated mutants A1442P and R1441C exhibit increased intracellular degradation
    • Greene, I.D., Mastaglia, F., Meloni, B.P., West, K.A., Chieng, J., Mitchell, C.J., Gai,W.P. and Boulos, S. (2014) Evidence that the LRRK2 ROC domain Parkinson's disease-associated mutants A1442P and R1441C exhibit increased intracellular degradation. J. Neurosci. Res., 92, 506-516.
    • (2014) J. Neurosci. Res. , vol.92 , pp. 506-516
    • Greene, I.D.1    Mastaglia, F.2    Meloni, B.P.3    West, K.A.4    Chieng, J.5    Mitchell, C.J.6    Gai, W.P.7    Boulos, S.8
  • 37
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: navigating downstream
    • Manning, B.D. and Cantley, L.C. (2007) AKT/PKB signaling: navigating downstream. Cell, 129, 1261-1274.
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 38
    • 68249104469 scopus 로고    scopus 로고
    • Emerging role of LRRK2 in human neural progenitor cell cycle progression, survival and differentiation
    • Milosevic, J., Schwarz, S.C., Ogunlade, V., Meyer, A.K., Storch, A. and Schwarz, J. (2009) Emerging role of LRRK2 in human neural progenitor cell cycle progression, survival and differentiation. Mol. Neurodegener., 4, 25.
    • (2009) Mol. Neurodegener. , vol.4 , pp. 25
    • Milosevic, J.1    Schwarz, S.C.2    Ogunlade, V.3    Meyer, A.K.4    Storch, A.5    Schwarz, J.6
  • 41
    • 84866721819 scopus 로고    scopus 로고
    • Presynaptic dysfunction in Parkinson's disease: a focus on LRRK2
    • Belluzzi, E., Greggio, E. and Piccoli, G. (2012) Presynaptic dysfunction in Parkinson's disease: a focus on LRRK2. Biochem. Soc. Trans., 40, 1111-1116.
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 1111-1116
    • Belluzzi, E.1    Greggio, E.2    Piccoli, G.3
  • 44
    • 59649100571 scopus 로고    scopus 로고
    • Snapin facilitates the synchronization of synaptic vesicle fusion
    • Pan, P.Y., Tian, J.H. and Sheng, Z.H. (2009) Snapin facilitates the synchronization of synaptic vesicle fusion. Neuron, 61, 412-424.
    • (2009) Neuron , vol.61 , pp. 412-424
    • Pan, P.Y.1    Tian, J.H.2    Sheng, Z.H.3
  • 45
    • 84861853310 scopus 로고    scopus 로고
    • APPL1 potentiates insulin secretion in pancreatic ß cells by enhancing protein kinase Aktdependent expression of SNARE proteins in mice
    • Cheng, K.K., Lam, K.S., Wu, D.,Wang, Y., Sweeney, G., Hoo, R. L., Zhang, J. and Xu, A. (2012) APPL1 potentiates insulin secretion in pancreatic ß cells by enhancing protein kinase Aktdependent expression of SNARE proteins in mice. Proc. Natl. Acad. Sci. USA, 109, 8919-8924.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 8919-8924
    • Cheng, K.K.1    Lam, K.S.2    Wu, D.3    Wang, Y.4    Sweeney, G.5    Hoo, R.L.6    Zhang, J.7    Xu, A.8
  • 47
    • 79959222357 scopus 로고    scopus 로고
    • Deconstructing GSK-3: The Fine Regulation of Its Activity
    • Medina, M. and Wandosell, F. (2011) Deconstructing GSK-3: The Fine Regulation of Its Activity. Int. J. Alzheimers Dis., 2011, 479249.
    • (2011) Int. J. Alzheimers Dis. , vol.2011 , pp. 479249
    • Medina, M.1    Wandosell, F.2
  • 49
    • 77957377567 scopus 로고    scopus 로고
    • LRRK2 G2019S mutation induces dendrite degeneration through mislocalization and phosphorylation of tau by recruiting autoactivated GSK-3ß
    • Lin, C.H., Tsai, P.I., Wu, R.M. and Chien, C.T. (2010) LRRK2 G2019S mutation induces dendrite degeneration through mislocalization and phosphorylation of tau by recruiting autoactivated GSK-3ß. J. Neurosci., 30, 13138-13149.
    • (2010) J. Neurosci. , vol.30 , pp. 13138-13149
    • Lin, C.H.1    Tsai, P.I.2    Wu, R.M.3    Chien, C.T.4
  • 50
    • 84891832231 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 regulates tau phosphorylation through direct activation of glycogen synthase kinase-3ß
    • Kawakami, F., Shimada, N., Ohta, E., Kagiya, G., Kawashima, R., Maekawa, T., Maruyama, H. and Ichikawa, T. (2014) Leucine-rich repeat kinase 2 regulates tau phosphorylation through direct activation of glycogen synthase kinase-3ß. FEBS J., 281, 3-13.
    • (2014) FEBS J. , vol.281 , pp. 3-13
    • Kawakami, F.1    Shimada, N.2    Ohta, E.3    Kagiya, G.4    Kawashima, R.5    Maekawa, T.6    Maruyama, H.7    Ichikawa, T.8
  • 52
    • 0037378026 scopus 로고    scopus 로고
    • Oxidative Stress in Parkinson's disease
    • Jenner, P. (2003) Oxidative Stress in Parkinson's disease. Ann. Neurol., 53, S26-S38.
    • (2003) Ann. Neurol. , vol.53 , pp. S26-S38
    • Jenner, P.1
  • 55
    • 58049206540 scopus 로고    scopus 로고
    • Spatiotemporal recapitulation of central nervous system development by murine embryonic stem cell-derived neural stem/ progenitor cells
    • Okada, Y., Matsumoto, A., Shimazaki, T., Enoki, R., Koizumi, A., Ishii, S., Itoyama, Y., Sobue, G. and Okano, H. (2008) Spatiotemporal recapitulation of central nervous system development by murine embryonic stem cell-derived neural stem/ progenitor cells. Stem Cells, 26, 3086-3098.
    • (2008) Stem Cells , vol.26 , pp. 3086-3098
    • Okada, Y.1    Matsumoto, A.2    Shimazaki, T.3    Enoki, R.4    Koizumi, A.5    Ishii, S.6    Itoyama, Y.7    Sobue, G.8    Okano, H.9
  • 58
    • 34047133699 scopus 로고    scopus 로고
    • Independent occurrence of I2020T mutation in the kinase domain of the leucine rich repeat kinase 2 gene in Japanese and German Parkinson's disease families
    • Ohta, E., Hasegawa, K., Gasser, T. and Obata, F. (2007) Independent occurrence of I2020T mutation in the kinase domain of the leucine rich repeat kinase 2 gene in Japanese and German Parkinson's disease families. Neurosci. Lett., 417, 21-23.
    • (2007) Neurosci. Lett. , vol.417 , pp. 21-23
    • Ohta, E.1    Hasegawa, K.2    Gasser, T.3    Obata, F.4
  • 62
    • 0031561429 scopus 로고    scopus 로고
    • Comparison of exocytotic mechanisms between acetylcholine- and catecholaminecontaining vesicles in rat pheochromocytoma cells
    • Nishiki, T., Shoji-Kasai, Y., Sekiguchi, M., Iwasaki, S., Kumakura, K. and Takahashi, M. (1997) Comparison of exocytotic mechanisms between acetylcholine- and catecholaminecontaining vesicles in rat pheochromocytoma cells. Biochem. Biophys. Res. Commun., 239, 57-62.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 57-62
    • Nishiki, T.1    Shoji-Kasai, Y.2    Sekiguchi, M.3    Iwasaki, S.4    Kumakura, K.5    Takahashi, M.6


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