메뉴 건너뛰기




Volumn 8, Issue SEP, 2014, Pages 1-11

Synaptic function is modulated by LRRK2 and glutamate release is increased in cortical neurons of G2019S LRRK2 knock-in mice

Author keywords

Cortical culture; Electrophysiology; G2019S; LRRK2; LRRK2 mutation; Parkinson disease; Transgenic mice

Indexed keywords

4 AMINOBUTYRIC ACID; GLUTAMIC ACID; LEUCINE RICH REPEAT KINASE 2; SYNAPSIN I;

EID: 84907573660     PISSN: 16625102     EISSN: None     Source Type: Journal    
DOI: 10.3389/fncel.2014.00301     Document Type: Article
Times cited : (87)

References (54)
  • 3
    • 84897401085 scopus 로고    scopus 로고
    • Palmitoylation of delta-catenin by DHHC5 mediates activity- induced synapse plasticity. Nat
    • Brigidi, G. S., Sun, Y., Beccano-Kelly, D., Pitman, K., Mobasser, M., Borgland, S. L., et al. (2014). Palmitoylation of delta-catenin by DHHC5 mediates activity- induced synapse plasticity. Nat. Neurosci. 17, 522-532. doi: 10.1038/nn.3657
    • (2014) Neurosci , vol.17 , pp. 522-532
    • Brigidi, G.S.1    Sun, Y.2    Beccano-Kelly, D.3    Pitman, K.4    Mobasser, M.5    Borgland, S.L.6
  • 4
    • 79955544006 scopus 로고    scopus 로고
    • Rac1 protein rescues neurite retraction caused by G2019S leucine-rich repeat kinase 2 (LRRK2)
    • Chan, D., Citro, A., Cordy, J. M., Shen, G. C., and Wolozin, B. (2011). Rac1 protein rescues neurite retraction caused by G2019S leucine-rich repeat kinase 2 (LRRK2). J. Biol. Chem. 286, 16140-16149. doi: 10.1074/jbc.M111.234005
    • (2011) J. Biol. Chem , vol.286 , pp. 16140-16149
    • Chan, D.1    Citro, A.2    Cordy, J.M.3    Shen, G.C.4    Wolozin, B.5
  • 5
    • 66549107350 scopus 로고    scopus 로고
    • Opposite changes in glutamatergic and GABAergic transmission underlie the diffuse hyperexcitability of synapsin I-deficient cortical networks
    • Chiappalone, M., Casagrande, S., Tedesco, M., Valtorta, F., Baldelli, P., Martinoia, S., et al. (2009). Opposite changes in glutamatergic and GABAergic transmission underlie the diffuse hyperexcitability of synapsin I-deficient cortical networks. Cereb. Cortex 19, 1422-1439. doi: 10.1093/cercor/bhn182
    • (2009) Cereb. Cortex , vol.19 , pp. 1422-1439
    • Chiappalone, M.1    Casagrande, S.2    Tedesco, M.3    Valtorta, F.4    Baldelli, P.5    Martinoia, S.6
  • 6
    • 84901669528 scopus 로고    scopus 로고
    • LRRK2 kinase activity regulates synaptic vesicle trafficking and neurotransmitter release through modulation of LRRK2 macro-molecular complex
    • Cirnaru, M. D., Marte, A., Belluzzi, E., Russo, I., Gabrielli, M., Longo, F., et al. LRRK2 kinase activity regulates synaptic vesicle trafficking and neurotransmitter release through modulation of LRRK2 macro-molecular complex. Front. Mol. Neurosci. 7:49. doi: 10.3389/fnmol.2014.00049
    • Front. Mol. Neurosci , vol.7 , pp. 49
    • Cirnaru, M.D.1    Marte, A.2    Belluzzi, E.3    Russo, I.4    Gabrielli, M.5    Longo, F.6
  • 7
    • 78649389313 scopus 로고    scopus 로고
    • The role of leucine-rich repeat kinase 2 (LRRK2) in Parkinson's disease
    • Cookson, M. R. (2010). The role of leucine-rich repeat kinase 2 (LRRK2) in Parkinson's disease. Nature Rev. 11, 791-797. doi: 10.1038/nrn2935
    • (2010) Nature Rev , vol.11 , pp. 791-797
    • Cookson, M.R.1
  • 9
    • 81555205691 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 (LRRK2) cellular biology: A review of recent advances in identifying physiological substrates and cellular functions
    • Drolet, R. E., Sanders, J. M., and Kern, J. T. (2011). Leucine-rich repeat kinase 2 (LRRK2) cellular biology: a review of recent advances in identifying physiological substrates and cellular functions. J. Neurogenet. 25, 140-151. doi: 10.3109/01677063.2011.627072
    • (2011) J. Neurogenet , vol.25 , pp. 140-151
    • Drolet, R.E.1    Sanders, J.M.2    Kern, J.T.3
  • 10
    • 35448956106 scopus 로고    scopus 로고
    • Vesicle pools and synapsins: New insights into old enigmas
    • Fdez, E., and Hilfiker, S. (2006). Vesicle pools and synapsins: new insights into old enigmas. Brain CellBiol. 35, 107-115. doi: 10.1007/s11068-007-9013-4
    • (2006) Brain CellBiol , vol.35 , pp. 107-115
    • Fdez, E.1    Hilfiker, S.2
  • 11
    • 80053968304 scopus 로고    scopus 로고
    • LRRK2 protein levels are determined by kinase function and are crucial for kidney and lung homeostasis in mice
    • Herzig, M. C., Kolly, C., Persohn, E., Theil, D., Schweizer, T., Hafner, T., et al. LRRK2 protein levels are determined by kinase function and are crucial for kidney and lung homeostasis in mice. Hum. Mol. Genet. 20, 4209-4223. doi: 10.1093/hmg/ddr348
    • Hum. Mol. Genet , vol.20 , pp. 4209-4223
    • Herzig, M.C.1    Kolly, C.2    Persohn, E.3    Theil, D.4    Schweizer, T.5    Hafner, T.6
  • 12
    • 0037389665 scopus 로고    scopus 로고
    • Essential function of alpha-calcium/calmodulin-dependent protein kinase II in neurotransmitter release at a glutamatergic central synapse
    • Hinds, H. L., Goussakov, I., Nakazawa, K., Tonegawa, S., and Bolshakov, V. Y. (2003). Essential function of alpha-calcium/calmodulin-dependent protein kinase II in neurotransmitter release at a glutamatergic central synapse. Proc. Natl. Acad. Sci. U.S.A. 100, 4275-4280. doi: 10.1073/pnas.0530202100
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 4275-4280
    • Hinds, H.L.1    Goussakov, I.2    Nakazawa, K.3    Tonegawa, S.4    Bolshakov, V.Y.5
  • 13
    • 84861552733 scopus 로고    scopus 로고
    • LRRK2 knockout mice have an intact dopaminergic system but display alterations in exploratory and motor co-ordination behaviors
    • Hinkle, K. M., Yue, M., Behrouz, B., Dachsel, J. C., Lincoln, S. J., Bowles, E. E., et al. (2012). LRRK2 knockout mice have an intact dopaminergic system but display alterations in exploratory and motor co-ordination behaviors. Mol. Neurodegener. 7:25. doi: 10.1186/1750-1326-7-25
    • (2012) Mol. Neurodegener , vol.7 , pp. 25
    • Hinkle, K.M.1    Yue, M.2    Behrouz, B.3    Dachsel, J.C.4    Lincoln, S.J.5    Bowles, E.E.6
  • 14
    • 34548314077 scopus 로고    scopus 로고
    • Kinase activity is not required for alphaCaMKII- dependent presynaptic plasticity at CA3-CA1 synapses
    • Hojjati, M. R., van Woerden, G. M., Tyler, W. J., Giese, K. P., Silva, A. J., Pozzo-Miller, L., et al. (2007). Kinase activity is not required for alphaCaMKII- dependent presynaptic plasticity at CA3-CA1 synapses. Nat. Neurosci. 10, 1125-1127. doi: 10.1038/nn1946
    • (2007) Nat. Neurosci , vol.10 , pp. 1125-1127
    • Hojjati, M.R.1    Van Woerden, G.M.2    Tyler, W.J.3    Giese, K.P.4    Silva, A.J.5    Pozzo-Miller, L.6
  • 15
    • 0033213603 scopus 로고    scopus 로고
    • A phospho-switch controls the dynamic association ofsynapsins with synaptic vesicles
    • Hosaka, M., Hammer, R. E., and Sudhof, T. C. (1999). A phospho-switch controls the dynamic association ofsynapsins with synaptic vesicles. Neuron 24, 377-387. doi: 10.1016/S0896-6273(00)80851-X
    • (1999) Neuron , vol.24 , pp. 377-387
    • Hosaka, M.1    Hammer, R.E.2    Sudhof, T.C.3
  • 16
    • 0035887768 scopus 로고    scopus 로고
    • Opposing changes in phosphorylation of specific sites in synapsin I during Ca2+-dependent glutamate release in isolated nerve terminals
    • Jovanovic, J. N., Sihra, T. S., Nairn, A. C., Hemmings, H. C. Jr., Greengard, P., and Czernik, A. J. (2001). Opposing changes in phosphorylation of specific sites in synapsin I during Ca2+-dependent glutamate release in isolated nerve terminals. J. Neurosci. 21, 7944-7953.
    • (2001) J. Neurosci , vol.21 , pp. 7944-7953
    • Jovanovic, J.N.1    Sihra, T.S.2    Nairn, A.C.3    Hemmings, H.C.4    Greengard, P.5    Czernik, A.J.6
  • 17
    • 84863337898 scopus 로고    scopus 로고
    • Opposing roles of synaptic and extrasynaptic NMDA receptor signaling in cocultured striatal and cortical neurons
    • Kaufman, A. M., Milnerwood, A. J., Sepers, M. D., Coquinco, A., She, K., Wang, L., et al. (2012). Opposing roles of synaptic and extrasynaptic NMDA receptor signaling in cocultured striatal and cortical neurons. J. Neurosci. 32, 3992-4003. doi: 10.1523/JNEUROSCI.4129-11.2012
    • (2012) J. Neurosci , vol.32 , pp. 3992-4003
    • Kaufman, A.M.1    Milnerwood, A.J.2    Sepers, M.D.3    Coquinco, A.4    She, K.5    Wang, L.6
  • 18
    • 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., et al. 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. doi: 10.1371/journal.pone.0030834
    • PLoS ONE , vol.7 , pp. 30834
    • Kawakami, F.1    Yabata, T.2    Ohta, E.3    Maekawa, T.4    Shimada, N.5    Suzuki, M.6
  • 19
    • 34248574535 scopus 로고    scopus 로고
    • Loss of LRRK2/PARK8 induces degeneration of dopaminergic neurons in Drosophila. Biochem
    • Lee, S. B., Kim, W., Lee, S., and Chung, J. (2007). Loss of LRRK2/PARK8 induces degeneration of dopaminergic neurons in Drosophila. Biochem. Biophys. Res. Commun. 358, 534-539. doi: 10.1016/j.bbrc.2007.04.156
    • (2007) Biophys. Res. Commun , vol.358 , pp. 534-539
    • Lee, S.B.1    Kim, W.2    Lee, S.3    Chung, J.4
  • 20
    • 84866646876 scopus 로고    scopus 로고
    • The synaptic function of LRRK2
    • Lee, S., Imai, Y., Gehrke, S., Liu, S., and Lu, B. (2012). The synaptic function of LRRK2. Biochem. Soc. Trans. 40, 1047-1051. doi: 10.1042/BST20120113
    • (2012) Biochem. Soc. Trans , vol.40 , pp. 1047-1051
    • Lee, S.1    Imai, Y.2    Gehrke, S.3    Liu, S.4    Lu, B.5
  • 21
    • 78650389179 scopus 로고    scopus 로고
    • LRRK2 kinase regulates synaptic morphology through distinct substrates at the presynaptic and postsy- naptic compartments of the Drosophila neuromuscular junction
    • Lee, S., Liu, H. P., Lin, W. Y., Guo, H., and Lu, B. (2010). LRRK2 kinase regulates synaptic morphology through distinct substrates at the presynaptic and postsy- naptic compartments of the Drosophila neuromuscular junction. J. Neurosci. 30, 16959-16969. doi: 10.1523/JNEUROSCI.1807-10.2010
    • (2010) J. Neurosci , vol.30 , pp. 16959-16969
    • Lee, S.1    Liu, H.P.2    Lin, W.Y.3    Guo, H.4    Lu, B.5
  • 22
    • 77957377567 scopus 로고    scopus 로고
    • LRRK2 G2019S mutation induces dendrite degeneration through mislocalization and phosphorylation of tau by recruiting autoactivated GSK3ss
    • 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 GSK3ss. J. Neurosci. 30, 13138-13149. doi: 10.1523/JNEUROSCI.1737-10.2010
    • (2010) J. Neurosci , vol.30 , pp. 13138-13149
    • Lin, C.H.1    Tsai, P.I.2    Wu, R.M.3    Chien, C.T.4
  • 23
    • 84893877488 scopus 로고    scopus 로고
    • Phosphoproteomic evaluation of pharmacological inhibition of leucine-rich repeat kinase 2 reveals significant off-target effects of LRRK-2-IN- 1
    • Luerman, G. C., Nguyen, C., Samaroo, H., Loos, P., Xi, H., Hurtado-Lorenzo, A., et al. (2014). Phosphoproteomic evaluation of pharmacological inhibition of leucine-rich repeat kinase 2 reveals significant off-target effects of LRRK-2-IN- 1. J. Neurochem. 128, 561-576. doi: 10.1111/jnc.12483
    • (2014) J. Neurochem , vol.128 , pp. 561-576
    • Luerman, G.C.1    Nguyen, C.2    Samaroo, H.3    Loos, P.4    Xi, H.5    Hurtado-Lorenzo, A.6
  • 24
    • 33751256567 scopus 로고    scopus 로고
    • The familial Parkinsonism gene LRRK2 regulates neurite process morphology
    • MacLeod, D., Dowman, J., Hammond, R., Leete, T., Inoue, K., and Abeliovich, (2006). The familial Parkinsonism gene LRRK2 regulates neurite process morphology. Neuron 52, 587-593. doi: 10.1016/j.neuron.2006. 10.008
    • (2006) Neuron , vol.52 , pp. 587-593
    • Macleod, D.1    Dowman, J.2    Hammond, R.3    Leete, T.4    Inoue, K.5    Abeliovich6
  • 25
    • 67650741663 scopus 로고    scopus 로고
    • Network homeostasis: A matter of coordination
    • Maffei, A., and Fontanini, A. (2009). Network homeostasis: a matter of coordination. Curr. Opin. Neurobiol. 19, 168-173. doi: 10.1016/j.conb.2009. 05.012
    • (2009) Curr. Opin. Neurobiol , vol.19 , pp. 168-173
    • Maffei, A.1    Fontanini, A.2
  • 26
    • 84866510734 scopus 로고    scopus 로고
    • LRRK2 controls an EndoA phosphorylation cycle in synaptic endocytosis
    • Matta, S., Van Kolen, K., da Cunha, R., van den Bogaart, G., Mandemakers, W., Miskiewicz, K., et al. (2012). LRRK2 controls an EndoA phosphorylation cycle in synaptic endocytosis. Neuron 75, 1008-1021. doi: 10.1016/j.neuron.2012.08.022
    • (2012) Neuron , vol.75 , pp. 1008-1021
    • Matta, S.1    Van Kolen, K.2    Da Cunha, R.3    Van Den Bogaart, G.4    Mandemakers, W.5    Miskiewicz, K.6
  • 27
    • 77957794336 scopus 로고    scopus 로고
    • Impaired dopaminergic neurotransmission and microtubule- associated protein tau alterations in human LRRK2 transgenic mice
    • Melrose, H. L., Dachsel, J. C., Behrouz, B., Lincoln, S. J., Yue, M., Hinkle, K. M., et al. (2010). Impaired dopaminergic neurotransmission and microtubule- associated protein tau alterations in human LRRK2 transgenic mice. Neurobiol. Dis. 40, 503-517. doi: 10.1016/j.nbd.2010.07.010
    • (2010) Neurobiol. Dis , vol.40 , pp. 503-517
    • Melrose, H.L.1    Dachsel, J.C.2    Behrouz, B.3    Lincoln, S.J.4    Yue, M.5    Hinkle, K.M.6
  • 28
    • 84863773618 scopus 로고    scopus 로고
    • Mitigation of augmented extrasynap- tic NMDAR signaling and apoptosis in cortico-striatal co-cultures from Huntington’s disease mice
    • Milnerwood, A. J., Kaufman, A. M., Sepers, M. D., Gladding, C. M., Zhang, L., Wang, L., et al. (2012). Mitigation of augmented extrasynap- tic NMDAR signaling and apoptosis in cortico-striatal co-cultures from Huntington’s disease mice. Neurobiol. Dis. 48, 40-51. doi: 10.1016/j.nbd.2012. 05.013
    • (2012) Neurobiol. Dis , vol.48 , pp. 40-51
    • Milnerwood, A.J.1    Kaufman, A.M.2    Sepers, M.D.3    Gladding, C.M.4    Zhang, L.5    Wang, L.6
  • 29
  • 30
    • 77956674229 scopus 로고    scopus 로고
    • 14-3-3 binding to LRRK2 is disrupted by multiple Parkinson’s disease-associated mutations and regulates cytoplasmic localization
    • Nichols, R. J., Dzamko, N., Morrice, N. A., Campbell, D. G., Deak, M., Ordureau, et al. (2010). 14-3-3 binding to LRRK2 is disrupted by multiple Parkinson’s disease-associated mutations and regulates cytoplasmic localization. Biochem. J. 430, 393-404. doi: 10.1042/BJ20100483
    • (2010) Biochem. J , vol.430 , pp. 393-404
    • Nichols, R.J.1    Dzamko, N.2    Morrice, N.A.3    Campbell, D.G.4    Deak, M.5    Ordureau6
  • 32
    • 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, H. J., Lin, X., Gu, X. L., Long, C. X., et al. (2009). Phosphorylation of ezrin/radixin/moesin proteins by LRRK2 promotes the rearrangement of actin cytoskeleton in neuronal morphogenesis. J. Neurosci. 29, 13971-13980. doi: 10.1523/JNEUROSCI.3799-09.2009
    • (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
  • 33
    • 84896736721 scopus 로고    scopus 로고
    • LRRK2 regulates synaptogenesis and dopamine receptor activation through modulation ofPKA activity
    • Parisiadou, L., Yu, J., Sgobio, C., Xie, C., Liu, G., Sun, L., et al. (2014). LRRK2 regulates synaptogenesis and dopamine receptor activation through modulation ofPKA activity. Nat. Neurosci. 17, 367-376. doi: 10.1038/nn.3636
    • (2014) Nat. Neurosci , vol.17 , pp. 367-376
    • Parisiadou, L.1    Yu, J.2    Sgobio, C.3    Xie, C.4    Liu, G.5    Sun, L.6
  • 34
    • 79951534656 scopus 로고    scopus 로고
    • LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool
    • Piccoli, G., Condliffe, S. B., Bauer, M., Giesert, F., Boldt, K., De Astis, S., et al. LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool. J. Neurosci. 31, 2225-2237. doi: 10.1523/JNEUROSCI.3730- 10.2011
    • J. Neurosci , vol.31 , pp. 2225-2237
    • Piccoli, G.1    Condliffe, S.B.2    Bauer, M.3    Giesert, F.4    Boldt, K.5    De Astis, S.6
  • 35
    • 84901320074 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 binds to neuronal vesicles through protein interactions mediated byits C-terminal WD40 domain
    • Piccoli, G., Onofri, F., Cirnaru, M. D., Kaiser, C. J., Jagtap, P., Kastenmuller, A., et al. (2014). Leucine-rich repeat kinase 2 binds to neuronal vesicles through protein interactions mediated byits C-terminal WD40 domain. Mol. Cell. Biol. 34, 2147-2161. doi: 10.1128/MCB.00914-13
    • (2014) Mol. Cell. Biol , vol.34 , pp. 2147-2161
    • Piccoli, G.1    Onofri, F.2    Cirnaru, M.D.3    Kaiser, C.J.4    Jagtap, P.5    Kastenmuller, A.6
  • 37
    • 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. doi: 10.1111/j.1471-4159.2008. 05217.x
    • (2008) J. Neurochem , vol.105 , pp. 1048-1056
    • Plowey, E.D.1    Cherra, S.J.2    Liu, Y.J.3    Chu, C.T.4
  • 38
    • 79953758383 scopus 로고    scopus 로고
    • Dopaminergic neuronal loss, reduced neurite complexity and autophagic abnormalities in transgenic mice expressing G2019S mutant LRRK2
    • Ramonet, D., Daher, J. P., Lin, B. M., Stafa, K., Kim, J., Banerjee, R., et al. (2011). Dopaminergic neuronal loss, reduced neurite complexity and autophagic abnormalities in transgenic mice expressing G2019S mutant LRRK2. PLoS ONE 6:e18568. doi: 10.1371/journal.pone.0018568
    • (2011) PLoS ONE , vol.6 , pp. 18568
    • Ramonet, D.1    Daher, J.P.2    Lin, B.M.3    Stafa, K.4    Kim, J.5    Banerjee, R.6
  • 39
    • 77956704554 scopus 로고    scopus 로고
    • 14-3-3 proteins are promising LRRK2 interactors
    • Rudenko, I. N., and Cookson, M. R. (2010). 14-3-3 proteins are promising LRRK2 interactors. Biochem. J. 430, e5-e6. doi: 10.1042/BJ20101200
    • (2010) Biochem. J , vol.430 , pp. e5-e6
    • Rudenko, I.N.1    Cookson, M.R.2
  • 40
    • 73649120624 scopus 로고    scopus 로고
    • Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization
    • Sen, S., Webber, P. J., and West, A. B. (2009). Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization. J. Biol. Chem. 284, 36346-36356. doi: 10.1074/jbc.M109.025437
    • (2009) J. Biol. Chem , vol.284 , pp. 36346-36356
    • Sen, S.1    Webber, P.J.2    West, A.B.3
  • 41
    • 84876981927 scopus 로고    scopus 로고
    • Short- andlong- term effects of LRRK2 on axon and dendrite growth
    • Sepulveda, B., Mesias, R., Li, X., Yue, Z., and Benson, D. L. (2013). Short- andlong- term effects of LRRK2 on axon and dendrite growth. PLoS ONE 8:e61986. doi: 10.1371/journal.pone.0061986
    • (2013) PLoS ONE , vol.8 , pp. 61986
    • Sepulveda, B.1    Mesias, R.2    Li, X.3    Yue, Z.4    Benson, D.L.5
  • 42
    • 33750503402 scopus 로고    scopus 로고
    • Arc/Arg3.1 mediates homeostatic synaptic scaling of AMPA receptors
    • Shepherd, J. D., Rumbaugh, G., Wu, J., Chowdhury, S., Plath, N., Kuhl, D., et al. (2006). Arc/Arg3.1 mediates homeostatic synaptic scaling of AMPA receptors. Neuron 52, 475-484. doi: 10.1016/j.neuron.2006.08.034
    • (2006) Neuron , vol.52 , pp. 475-484
    • Shepherd, J.D.1    Rumbaugh, G.2    Wu, J.3    Chowdhury, S.4    Plath, N.5    Kuhl, D.6
  • 43
    • 0026637195 scopus 로고
    • Deficient hippocampal long-term potentiation in alpha-calcium-calmodulin kinase II mutant mice
    • Silva, A. J., Stevens, C. F., Tonegawa, S., and Wang, Y. (1992). Deficient hippocampal long-term potentiation in alpha-calcium-calmodulin kinase II mutant mice. Science 257, 201-206. doi: 10.1126/science.1378648
    • (1992) Science , vol.257 , pp. 201-206
    • Silva, A.J.1    Stevens, C.F.2    Tonegawa, S.3    Wang, Y.4
  • 44
    • 84897586124 scopus 로고    scopus 로고
    • Functional interaction of Parkinson’s disease-associated LRRK2 with members of the dynamin GTPase superfamily
    • Stafa, K., Tsika, E., Moser, R., Musso, A., Glauser, L., Jones, A., et al. (2014). Functional interaction of Parkinson’s disease-associated LRRK2 with members of the dynamin GTPase superfamily. Hum. Mol. Genet. 23, 2055-2077. doi: 10.1093/hmg/ddt600
    • (2014) Hum. Mol. Genet , vol.23 , pp. 2055-2077
    • Stafa, K.1    Tsika, E.2    Moser, R.3    Musso, A.4    Glauser, L.5    Jones, A.6
  • 45
    • 2942556680 scopus 로고    scopus 로고
    • The synaptic vesicle cycle
    • Sudhof, T. C. (2004). The synaptic vesicle cycle. Annu. Rev. Neurosci. 27, 509-547. doi: 10.1146/annurev.neuro.26.041002.131412
    • (2004) Annu. Rev. Neurosci , vol.27 , pp. 509-547
    • Sudhof, T.C.1
  • 46
    • 79961232361 scopus 로고    scopus 로고
    • Progranulin deficiency decreases gross neural connectivitybutenhances transmission at individual synapses
    • Tapia, L., Milnerwood, A., Guo, A., Mills, F., Yoshida, E., Vasuta, C., et al. Progranulin deficiency decreases gross neural connectivitybutenhances transmission at individual synapses. J. Neurosci. 31, 11126-11132. doi: 10.1523/JNEUROSCI.6244-10.2011
    • J. Neurosci , vol.31 , pp. 11126-11132
    • Tapia, L.1    Milnerwood, A.2    Guo, A.3    Mills, F.4    Yoshida, E.5    Vasuta, C.6
  • 47
    • 0025098982 scopus 로고
    • Redistribution of synaptophysin and synapsin I during alpha- latrotoxin-induced release of neurotransmitter at the neuromuscular junction
    • Torri-Tarelli, F., Villa, A., Valtorta, F., De Camilli, P., Greengard, P., and Ceccarelli, (1990). Redistribution of synaptophysin and synapsin I during alpha- latrotoxin-induced release of neurotransmitter at the neuromuscular junction. J. CellBiol. 110, 449-459. doi: 10.1083/jcb.110.2.449
    • (1990) J. CellBiol , vol.110 , pp. 449-459
    • Torri-Tarelli, F.1    Villa, A.2    Valtorta, F.3    De Camilli, P.4    Greengard, P.5    Ceccarelli6
  • 48
    • 84867649477 scopus 로고    scopus 로고
    • Phosphorylation of 4E-BP1 in the mammalian brain is not altered by LRRK2 expression or pathogenic mutations
    • Trancikova, A., Mamais, A., Webber, P. J., Stafa, K., Tsika, E., Glauser, L., et al. Phosphorylation of 4E-BP1 in the mammalian brain is not altered by LRRK2 expression or pathogenic mutations. PLoS ONE 7:e47784. doi: 10.1371/journal.pone.0047784
    • PLoS ONE , vol.7 , pp. 47784
    • Trancikova, A.1    Mamais, A.2    Webber, P.J.3    Stafa, K.4    Tsika, E.5    Glauser, L.6
  • 49
    • 84860123187 scopus 로고    scopus 로고
    • Site-specific synapsin I phosphorylation participates in the expression of post-tetanic potentiation and its enhancement by BDNF
    • Valente, P., Casagrande, S., Nieus, T., Verstegen, A. M., Valtorta, F., Benfenati, F., et al. (2012). Site-specific synapsin I phosphorylation participates in the expression of post-tetanic potentiation and its enhancement by BDNF. J. Neurosci. 32, 5868-5879. doi: 10.1523/JNEUROSCI.5275-11.2012
    • (2012) J. Neurosci , vol.32 , pp. 5868-5879
    • Valente, P.1    Casagrande, S.2    Nieus, T.3    Verstegen, A.M.4    Valtorta, F.5    Benfenati, F.6
  • 50
    • 84901019188 scopus 로고    scopus 로고
    • Phosphorylation of synapsin I by cyclin-dependent kinase-5 sets the ratio between the resting and recycling pools of synaptic vesicles at hippocampal synapses
    • Verstegen, A. M., Tagliatti, E., Lignani, G., Marte, A., Stolero, T., Atias, M., et al. (2014). Phosphorylation of synapsin I by cyclin-dependent kinase-5 sets the ratio between the resting and recycling pools of synaptic vesicles at hippocampal synapses. J. Neurosci. 34, 7266-7280. doi: 10.1523/JNEUROSCI.3973- 13.2014
    • (2014) J. Neurosci , vol.34 , pp. 7266-7280
    • Verstegen, A.M.1    Tagliatti, E.2    Lignani, G.3    Marte, A.4    Stolero, T.5    Atias, M.6
  • 51
    • 84892706803 scopus 로고    scopus 로고
    • Inhibitoryplasticitydictates the sign ofplasticityat excitatory synapses
    • Wang, L., and Maffei, A. (2014). Inhibitoryplasticitydictates the sign ofplasticityat excitatory synapses. J. Neurosci. 34, 1083-1093. doi: 10.1523/JNEUROSCI.4711- 13.2014
    • (2014) J. Neurosci , vol.34 , pp. 1083-1093
    • Wang, L.1    Maffei, A.2
  • 52
    • 84860389765 scopus 로고    scopus 로고
    • Autophosphorylation in the leucine-rich repeat kinase 2 (LRRK2) GTPase domain modifies kinase and GTP-binding activities
    • Webber, P. J., Smith, A. D., Sen, S., Renfrow, M. B., Mobley, J. A., and West, A. (2011). Autophosphorylation in the leucine-rich repeat kinase 2 (LRRK2) GTPase domain modifies kinase and GTP-binding activities. J. Mol. Biol. 412, 94-110. doi: 10.1016/j.jmb.2011.07.033
    • (2011) J. Mol. Biol , vol.412 , pp. 94-110
    • Webber, P.J.1    Smith, A.D.2    Sen, S.3    Renfrow, M.B.4    Mobley, J.A.5    West, A.6
  • 53
    • 28044460070 scopus 로고    scopus 로고
    • Parkinson’s disease-associated mutations in leucine-rich repeat kinase augment kinase activity
    • West, A. B., Moore, D. J., Biskup, S., Bugayenko, A., Smith, W. W., Ross, C. A., et al. (2005). Parkinson’s disease-associated mutations in leucine-rich repeat kinase augment kinase activity. Proc. Natl. Acad. Sci. U.S.A. 102, 16842-16847. doi: 10.1073/pnas.0507360102
    • (2005) Proc. Natl. Acad. Sci. U.S.A , 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
  • 54
    • 79151473945 scopus 로고    scopus 로고
    • Adult neurogenesis and neurite outgrowth are impaired in LRRK2 G2019S mice
    • Winner, B., Melrose, H. L., Zhao, C., Hinkle, K. M., Yue, M., Kent, C., et al. (2011). Adult neurogenesis and neurite outgrowth are impaired in LRRK2 G2019S mice. Neurobiol. Dis. 41, 706-716. doi: 10.1016/j.nbd.2010.12.008
    • (2011) Neurobiol. Dis , vol.41 , pp. 706-716
    • Winner, B.1    Melrose, H.L.2    Zhao, C.3    Hinkle, K.M.4    Yue, M.5    Kent, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.