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Volumn 45, Issue 8, 2013, Pages

LRRK2 phosphorylates Snapin and inhibits interaction of Snapin with SNAP-25

Author keywords

Kinase; LRRK2; SNAP 25; Snapin; SNARE vesicle; Synaptotagmin

Indexed keywords

BINDING PROTEIN; GLUTATHIONE TRANSFERASE; LEUCINE RICH REPEAT KINASE 2; RAS PROTEIN; SNAPIN PROTEIN; SNARE PROTEIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNAPTOTAGMIN; THREONINE; UNCLASSIFIED DRUG; LRRK2 PROTEIN, MOUSE; MUTANT PROTEIN; PHOSPHOTHREONINE; PROTEIN SERINE THREONINE KINASE; SNAPIN PROTEIN, HUMAN; SYNAPTOBREVIN 2; SYNTAXIN; VESICULAR TRANSPORT PROTEIN;

EID: 84883034462     PISSN: 12263613     EISSN: 20926413     Source Type: Journal    
DOI: 10.1038/emm.2013.68     Document Type: Article
Times cited : (47)

References (67)
  • 1
    • 8844233579 scopus 로고    scopus 로고
    • Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology
    • 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;44:601-607.
    • (2004) Neuron , vol.44 , pp. 601-607
    • Zimprich, A.1    Biskup, S.2    Leitner, P.3    Lichtner, P.4    Farrer, M.5    Lincoln, S.6
  • 2
    • 8844266996 scopus 로고    scopus 로고
    • Cloning of the gene containing mutations that cause PARK8-linked Parkinson's disease
    • Paisan-Ruiz C, Jain S, Evans EW, Gilks WP, Simon J, Van Der Brug M et al. Cloning of the gene containing mutations that cause PARK8-linked Parkinson's disease. Neuron 2004;44:595-600.
    • (2004) Neuron , vol.44 , pp. 595-600
    • Paisan-Ruiz, C.1    Jain, S.2    Evans, E.W.3    Gilks, W.P.4    Simon, J.5    Van Der Brug, M.6
  • 3
    • 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;102:16842-16847.
    • (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
  • 4
    • 77953530143 scopus 로고    scopus 로고
    • Biochemical and molecular features of LRRK2 and its pathophysiological roles in Parkinson's disease
    • Seol W. Biochemical and molecular features of LRRK2 and its pathophysiological roles in Parkinson's disease. BMB Rep 2010;43:233-244.
    • (2010) BMB Rep , vol.43 , pp. 233-244
    • Seol, W.1
  • 6
    • 29444437871 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration
    • Smith WW, Pei Z, Jiang H, Moore DJ, Liang Y, West AB et al. Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration. Proc Natl Acad Sci USA 2005;102:18676-18681.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 18676-18681
    • Smith, W.W.1    Pei, Z.2    Jiang, H.3    Moore, D.J.4    Liang, Y.5    West, A.B.6
  • 7
    • 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;313:3658-3670.
    • (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
  • 9
    • 39549117093 scopus 로고    scopus 로고
    • Role of autophagy in G2019SLRRK2-associated neurite shortening in differentiated SH-SY5Y cells
    • Plowey ED, Cherra SJ 3rd, Liu YJ, Chu CT. Role of autophagy in G2019SLRRK2-associated neurite shortening in differentiated SH-SY5Y cells. J Neurochem 2008;105:1048-1056.
    • (2008) J Neurochem , vol.105 , pp. 1048-1056
    • Plowey, E.D.1    Cherra III, S.J.2    Liu, Y.J.3    Chu, C.T.4
  • 10
    • 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;52:587-593.
    • (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
  • 11
    • 33846562487 scopus 로고    scopus 로고
    • Parkinson's disease-associated mutations in LRRK2 link enhanced GTP-binding and kinase activities to neuronal toxicity
    • West AB, Moore DJ, Choi C, Andrabi SA, Li X, Dikeman D et al. Parkinson's disease-associated mutations in LRRK2 link enhanced GTP-binding and kinase activities to neuronal toxicity. Hum Mol Genet 2007;16:223-232.
    • (2007) Hum Mol Genet , vol.16 , pp. 223-232
    • West, A.B.1    Moore, D.J.2    Choi, C.3    Andrabi, S.A.4    Li, X.5    Dikeman, D.6
  • 12
    • 51349166968 scopus 로고    scopus 로고
    • Wild-type LRRK2 but not its mutant attenuates stress-induced cell death via ERK pathway
    • Liou AK, Leak RK, Li L, Zigmond MJ. Wild-type LRRK2 but not its mutant attenuates stress-induced cell death via ERK pathway. Neurobiol Dis 2008;32:116-124.
    • (2008) Neurobiol Dis , vol.32 , pp. 116-124
    • Liou, A.K.1    Leak, R.K.2    Li, L.3    Zigmond, M.J.4
  • 13
    • 77449141215 scopus 로고    scopus 로고
    • LRRK2 enhances oxidative stress-induced neurotoxicity via its kinase activity
    • Heo HY, Park JM, Kim CH, Han BS, Kim KS, Seol W. LRRK2 enhances oxidative stress-induced neurotoxicity via its kinase activity. Exp Cell Res 2010;316:649-656.
    • (2010) Exp Cell Res , vol.316 , pp. 649-656
    • Heo, H.Y.1    Park, J.M.2    Kim, C.H.3    Han, B.S.4    Kim, K.S.5    Seol, W.6
  • 15
    • 34447118788 scopus 로고    scopus 로고
    • LRRK2 phosphorylates moesin at threonine-558: Characterization of how Parkinson's disease mutants affect kinase activity
    • Jaleel M, Nichols RJ, Deak M, Campbell DG, Gillardon F, Knebel A et al. LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity. Biochem J 2007;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
  • 16
    • 34548432121 scopus 로고    scopus 로고
    • Mechanistic insight into the dominant mode of the Parkinson's disease-associated G2019S LRRK2 mutation
    • Luzon-Toro B, Rubio De La Torre E, Delgado A, Perez-Tur J, Hilfiker S. Mechanistic insight into the dominant mode of the Parkinson's disease-associated G2019S LRRK2 mutation. Hum Mol Genet 2007;16:2031-2039.
    • (2007) Hum Mol Genet , vol.16 , pp. 2031-2039
    • Luzon-Toro, B.1    Rubio De La Torre, E.2    Delgado, A.3    Perez-Tur, J.4    Hilfiker, S.5
  • 19
    • 41549144503 scopus 로고    scopus 로고
    • The chaperone activity of heat shock protein 90 is critical for maintaining the stability of leucine-rich repeat kinase 2
    • Wang L, Xie C, Greggio E, Parisiadou L, Shim H, Sun L et al. The chaperone activity of heat shock protein 90 is critical for maintaining the stability of leucine-rich repeat kinase 2. J Neurosci 2008;28:3384-3391.
    • (2008) J Neurosci , vol.28 , pp. 3384-3391
    • Wang, L.1    Xie, C.2    Greggio, E.3    Parisiadou, L.4    Shim, H.5    Sun, L.6
  • 20
    • 69249211037 scopus 로고    scopus 로고
    • Interaction of elongation factor 1-alpha with leucine-rich repeat kinase 2 impairs kinase activity and microtubule bundling in vitro
    • Gillardon F. Interaction of elongation factor 1-alpha with leucine-rich repeat kinase 2 impairs kinase activity and microtubule bundling in vitro. Neuroscience 2009;163:533-539.
    • (2009) Neuroscience , vol.163 , pp. 533-539
    • Gillardon, F.1
  • 21
    • 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;110:1514-1522.
    • (2009) J Neurochem , vol.110 , pp. 1514-1522
    • Gillardon, F.1
  • 22
    • 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;86:1711-1720.
    • (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
  • 23
    • 70349576902 scopus 로고    scopus 로고
    • Mutations in the LRRK2 Roc-COR tandem domain link Parkinson's disease to Wnt signalling pathways
    • Sancho RM, Law BM, Harvey K. Mutations in the LRRK2 Roc-COR tandem domain link Parkinson's disease to Wnt signalling pathways. Hum Mol Genet 2009;18:3955-3968.
    • (2009) Hum Mol Genet , vol.18 , pp. 3955-3968
    • Sancho, R.M.1    Law, B.M.2    Harvey, K.3
  • 24
    • 65649142038 scopus 로고    scopus 로고
    • The Parkinson disease-associated protein kinase LRRK2 exhibits MAPKKK activity and phosphorylates MKK3/6 and MKK4/7, in vitro
    • Gloeckner CJ, Schumacher A, Boldt K, Ueffing M. The Parkinson disease-associated protein kinase LRRK2 exhibits MAPKKK activity and phosphorylates MKK3/6 and MKK4/7, in vitro. J Neurochem 2009;109:959-968.
    • (2009) J Neurochem , vol.109 , pp. 959-968
    • Gloeckner, C.J.1    Schumacher, A.2    Boldt, K.3    Ueffing, M.4
  • 25
    • 51949090816 scopus 로고    scopus 로고
    • Phosphorylation of 4E-BP by LRRK2 affects the maintenance of dopaminergic neurons in Drosophila
    • Imai Y, Gehrke S, Wang HQ, Takahashi R, Hasegawa K, Oota E et al. Phosphorylation of 4E-BP by LRRK2 affects the maintenance of dopaminergic neurons in Drosophila. Embo J 2008;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
  • 26
    • 78650389179 scopus 로고    scopus 로고
    • LRRK2 kinase regulates synaptic morphology through distinct substrates at the presynaptic and postsynaptic compartments of the Drosophila neuromuscular junction
    • Lee S, Liu HP, Lin WY, Guo H, Lu B. LRRK2 kinase regulates synaptic morphology through distinct substrates at the presynaptic and postsynaptic compartments of the Drosophila neuromuscular junction. J Neurosci 2010;30:16959-16969.
    • (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
  • 27
    • 78149446290 scopus 로고    scopus 로고
    • ARHGEF7 (Beta-PIX) acts as guanine nucleotide exchange factor for leucine-rich repeat kinase 2
    • Haebig K, Gloeckner CJ, Miralles MG, Gillardon F, Schulte C, Riess O et al. ARHGEF7 (Beta-PIX) acts as guanine nucleotide exchange factor for leucine-rich repeat kinase 2. PLoS One 2010;5:e13762.
    • (2010) PLoS One , vol.5
    • Haebig, K.1    Gloeckner, C.J.2    Miralles, M.G.3    Gillardon, F.4    Schulte, C.5    Riess, O.6
  • 28
    • 0033366466 scopus 로고    scopus 로고
    • Snapin: A SNARE-associated protein implicated in synaptic transmission
    • Ilardi JM, Mochida S, Sheng ZH. Snapin: a SNARE-associated protein implicated in synaptic transmission. Nat Neurosci 1999;2:119-124.
    • (1999) Nat Neurosci , vol.2 , pp. 119-124
    • Ilardi, J.M.1    Mochida, S.2    Sheng, Z.H.3
  • 29
    • 27744502972 scopus 로고    scopus 로고
    • The role of Snapin in neurosecretion: Snapin knock-out mice exhibit impaired calcium-dependent exocytosis of large dense-core vesicles in chromaffin cells
    • Tian JH, Wu ZX, Unzicker M, Lu L, Cai Q, Li C et al. The role of Snapin in neurosecretion: snapin knock-out mice exhibit impaired calcium-dependent exocytosis of large dense-core vesicles in chromaffin cells. J Neurosci 2005;25:10546-10555.
    • (2005) J Neurosci , vol.25 , pp. 10546-10555
    • Tian, J.H.1    Wu, Z.X.2    Unzicker, M.3    Lu, L.4    Cai, Q.5    Li, C.6
  • 30
    • 67651177960 scopus 로고    scopus 로고
    • Snapin associates with late endocytic compartments and interacts with late endosomal SNAREs
    • Lu L, Cai Q, Tian JH, Sheng ZH. Snapin associates with late endocytic compartments and interacts with late endosomal SNAREs. Biosci Rep 2009;29:261-269.
    • (2009) Biosci Rep , vol.29 , pp. 261-269
    • Lu, L.1    Cai, Q.2    Tian, J.H.3    Sheng, Z.H.4
  • 31
    • 59649100571 scopus 로고    scopus 로고
    • Snapin facilitates the synchronization of synaptic vesicle fusion
    • Pan PY, Tian JH, Sheng ZH. Snapin facilitates the synchronization of synaptic vesicle fusion. Neuron 2009;61:412-424.
    • (2009) Neuron , vol.61 , pp. 412-424
    • Pan, P.Y.1    Tian, J.H.2    Sheng, Z.H.3
  • 33
    • 77957325618 scopus 로고    scopus 로고
    • Snapin-regulated late endosomal transport is critical for efficient autophagy-lysosomal function in neurons
    • Cai Q, Lu L, Tian JH, Zhu YB, Qiao H, Sheng ZH. Snapin-regulated late endosomal transport is critical for efficient autophagy-lysosomal function in neurons. Neuron 2010;68:73-86.
    • (2010) Neuron , vol.68 , pp. 73-86
    • Cai, Q.1    Lu, L.2    Tian, J.H.3    Zhu, Y.B.4    Qiao, H.5    Sheng, Z.H.6
  • 34
    • 3242747322 scopus 로고    scopus 로고
    • Effects of PKA-mediated phosphorylation of Snapin on synaptic transmission in cultured hippocampal neurons
    • Thakur P, Stevens DR, Sheng ZH, Rettig J. Effects of PKA-mediated phosphorylation of Snapin on synaptic transmission in cultured hippocampal neurons. J Neurosci 2004;24:6476-6481.
    • (2004) J Neurosci , vol.24 , pp. 6476-6481
    • Thakur, P.1    Stevens, D.R.2    Sheng, Z.H.3    Rettig, J.4
  • 35
    • 83255185773 scopus 로고    scopus 로고
    • Type VI adenylyl cyclase (AC6) regulates neurite extension by binding to Snapin and Snap25
    • Wu CS, Lin JT, Chien CL, Chang WC, Lai HL, Chang CP et al. Type VI adenylyl cyclase (AC6) regulates neurite extension by binding to Snapin and Snap25. Mol Cell Biol 2011;31:4874-4886.
    • (2011) Mol Cell Biol , vol.31 , pp. 4874-4886
    • Wu, C.S.1    Lin, J.T.2    Chien, C.L.3    Chang, W.C.4    Lai, H.L.5    Chang, C.P.6
  • 36
    • 70350653779 scopus 로고    scopus 로고
    • Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinson's disease
    • Nichols RJ, Dzamko N, Hutti JE, Cantley LC, Deak M, Moran J et al. Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinson's disease. Biochem J 2009;424:47-60.
    • (2009) Biochem J , vol.424 , pp. 47-60
    • Nichols, R.J.1    Dzamko, N.2    Hutti, J.E.3    Cantley, L.C.4    Deak, M.5    Moran, J.6
  • 37
    • 77951240010 scopus 로고    scopus 로고
    • SH-SY5Y human neuroblastoma cell line: In vitro cell model of dopaminergic neurons in Parkinson's disease
    • Xie HR, Hu LS, Li GY. SH-SY5Y human neuroblastoma cell line: in vitro cell model of dopaminergic neurons in Parkinson's disease. Chin Med J (Engl) 2010;123:1086-1092.
    • (2010) Chin Med J (Engl) , vol.123 , pp. 1086-1092
    • Xie, H.R.1    Hu, L.S.2    Li, G.Y.3
  • 38
    • 65949110134 scopus 로고    scopus 로고
    • Langerhans cell protein 1 (LCP1) binds to PNUTS in the nucleus: Implications for this complex in transcriptional regulation
    • Lee SJ, Lee JK, Maeng YS, Kim YM, Kwon YG. Langerhans cell protein 1 (LCP1) binds to PNUTS in the nucleus: implications for this complex in transcriptional regulation. Exp Mol Med 2009;41:189-200.
    • (2009) Exp Mol Med , vol.41 , pp. 189-200
    • Lee, S.J.1    Lee, J.K.2    Maeng, Y.S.3    Kim, Y.M.4    Kwon, Y.G.5
  • 39
    • 33745847751 scopus 로고    scopus 로고
    • Pleckstrin homology domain of phospholipase C-gamma1 directly binds to 68-kDa neurofilament light chain
    • Kim SK, Choi JH, Suh PG, Chang JS. Pleckstrin homology domain of phospholipase C-gamma1 directly binds to 68-kDa neurofilament light chain. Exp Mol Med 2006;38:265-272.
    • (2006) Exp Mol Med , vol.38 , pp. 265-272
    • Kim, S.K.1    Choi, J.H.2    Suh, P.G.3    Chang, J.S.4
  • 40
    • 0035071322 scopus 로고    scopus 로고
    • Phosphorylation of Snapin by PKA modulates its interaction with the SNARE complex
    • Chheda MG, Ashery U, Thakur P, Rettig J, Sheng ZH. Phosphorylation of Snapin by PKA modulates its interaction with the SNARE complex. Nat Cell Biol 2001;3:331-338.
    • (2001) Nat Cell Biol , vol.3 , pp. 331-338
    • Chheda, M.G.1    Ashery, U.2    Thakur, P.3    Rettig, J.4    Sheng, Z.H.5
  • 41
    • 35648970630 scopus 로고    scopus 로고
    • The UT-A1 urea transporter interacts with snapin, a SNARE-associated protein
    • Mistry AC, Mallick R, Frohlich O, Klein JD, Rehm A, Chen G et al. The UT-A1 urea transporter interacts with snapin, a SNARE-associated protein. J Biol Chem 2007;282:30097-30106.
    • (2007) J Biol Chem , vol.282 , pp. 30097-30106
    • Mistry, A.C.1    Mallick, R.2    Frohlich, O.3    Klein, J.D.4    Rehm, A.5    Chen, G.6
  • 42
    • 0034934782 scopus 로고    scopus 로고
    • Glutamate regulates actin-based motility in axonal filopodia
    • Chang S, De Camilli P. Glutamate regulates actin-based motility in axonal filopodia. Nat Neurosci 2001;4:787-793.
    • (2001) Nat Neurosci , vol.4 , pp. 787-793
    • Chang, S.1    De Camilli, P.2
  • 43
    • 33745494172 scopus 로고    scopus 로고
    • Distinct endocytic pathways control the rate and extent of synaptic vesicle protein recycling
    • Voglmaier SM, Kam K, Yang H, Fortin DL, Hua Z, Nicoll RA et al. Distinct endocytic pathways control the rate and extent of synaptic vesicle protein recycling. Neuron 2006;51:71-84.
    • (2006) Neuron , vol.51 , pp. 71-84
    • Voglmaier, S.M.1    Kam, K.2    Yang, H.3    Fortin, D.L.4    Hua, Z.5    Nicoll, R.A.6
  • 44
    • 34548860902 scopus 로고    scopus 로고
    • Studying vesicle cycling in presynaptic terminals using the genetically encoded probe synaptopHluorin
    • Burrone J, Li Z, Murthy VN. Studying vesicle cycling in presynaptic terminals using the genetically encoded probe synaptopHluorin. Nat Protoc 2006;1:2970-2978.
    • (2006) Nat Protoc , vol.1 , pp. 2970-2978
    • Burrone, J.1    Li, Z.2    Murthy, V.N.3
  • 46
    • 78149435654 scopus 로고    scopus 로고
    • Identification and characterization of a leucine-rich repeat kinase 2 (LRRK2) consensus phosphorylation motif
    • Pungaliya PP, Bai Y, Lipinski K, Anand VS, Sen S, Brown EL et al. Identification and characterization of a leucine-rich repeat kinase 2 (LRRK2) consensus phosphorylation motif. PLoS One 2010;5:e13672.
    • (2010) PLoS One , vol.5
    • Pungaliya, P.P.1    Bai, Y.2    Lipinski, K.3    Anand, V.S.4    Sen, S.5    Brown, E.L.6
  • 47
    • 14844320520 scopus 로고    scopus 로고
    • EBAG9 adds a new layer of control on large dense-core vesicle exocytosis via interaction with Snapin
    • Ruder C, Reimer T, Delgado-Martinez I, Hermosilla R, Engelsberg A, Nehring R et al. EBAG9 adds a new layer of control on large dense-core vesicle exocytosis via interaction with Snapin. Mol Biol Cell 2005;16:1245-1257.
    • (2005) Mol Biol Cell , vol.16 , pp. 1245-1257
    • Ruder, C.1    Reimer, T.2    Delgado-Martinez, I.3    Hermosilla, R.4    Engelsberg, A.5    Nehring, R.6
  • 48
    • 8544278211 scopus 로고    scopus 로고
    • Regulation of type VI adenylyl cyclase by Snapin, a SNAP25-binding protein
    • Chou JL, Huang CL, Lai HL, Hung AC, Chien CL, Kao YY et al. Regulation of type VI adenylyl cyclase by Snapin, a SNAP25-binding protein. J Biol Chem 2004;279:46271-46279.
    • (2004) J Biol Chem , vol.279 , pp. 46271-46279
    • Chou, J.L.1    Huang, C.L.2    Lai, H.L.3    Hung, A.C.4    Chien, C.L.5    Kao, Y.Y.6
  • 49
    • 38049136729 scopus 로고    scopus 로고
    • Snapin interacts with the Exo70 subunit of the exocyst and modulates GLUT4 trafficking
    • Bao Y, Lopez JA, James DE, Hunziker W. Snapin interacts with the Exo70 subunit of the exocyst and modulates GLUT4 trafficking. J Biol Chem 2008;283:324-331.
    • (2008) J Biol Chem , vol.283 , pp. 324-331
    • Bao, Y.1    Lopez, J.A.2    James, D.E.3    Hunziker, W.4
  • 50
    • 33750978419 scopus 로고    scopus 로고
    • Casein kinase 1 delta (CK1delta) interacts with the SNARE associated protein snapin
    • Wolff S, Stoter M, Giamas G, Piesche M, Henne-Bruns D, Banting G et al. Casein kinase 1 delta (CK1delta) interacts with the SNARE associated protein snapin. FEBS Lett 2006;580:6477-6484.
    • (2006) FEBS Lett , vol.580 , pp. 6477-6484
    • Wolff, S.1    Stoter, M.2    Giamas, G.3    Piesche, M.4    Henne-Bruns, D.5    Banting, G.6
  • 51
    • 35748941237 scopus 로고    scopus 로고
    • Snapin, a new regulator of receptor signaling, augments alpha1A-adrenoceptor-operated calcium influx through TRPC6
    • Suzuki F, Morishima S, Tanaka T, Muramatsu I. Snapin, a new regulator of receptor signaling, augments alpha1A-adrenoceptor-operated calcium influx through TRPC6. J Biol Chem 2007;282:29563-29573.
    • (2007) J Biol Chem , vol.282 , pp. 29563-29573
    • Suzuki, F.1    Morishima, S.2    Tanaka, T.3    Muramatsu, I.4
  • 52
    • 2942750191 scopus 로고    scopus 로고
    • Reinvestigation of the role of snapin in neurotransmitter release
    • Vites O, Rhee JS, Schwarz M, Rosenmund C, Jahn R. Reinvestigation of the role of snapin in neurotransmitter release. J Biol Chem 2004;279:26251-26256.
    • (2004) J Biol Chem , vol.279 , pp. 26251-26256
    • Vites, O.1    Rhee, J.S.2    Schwarz, M.3    Rosenmund, C.4    Jahn, R.5
  • 53
    • 77956314453 scopus 로고    scopus 로고
    • CDK5 serves as a major control point in neurotransmitter release
    • Kim SH, Ryan TA. CDK5 serves as a major control point in neurotransmitter release. Neuron 2010;67:797-809.
    • (2010) Neuron , vol.67 , pp. 797-809
    • Kim, S.H.1    Ryan, T.A.2
  • 55
    • 77957951520 scopus 로고    scopus 로고
    • EHD1 is a synaptic protein that modulates exocytosis through binding to snapin
    • Wei S, Xu Y, Shi H, Wong SH, Han W, Talbot K et al. EHD1 is a synaptic protein that modulates exocytosis through binding to snapin. Mol Cell Neurosci 2011;45:418-429.
    • (2011) Mol Cell Neurosci , vol.45 , pp. 418-429
    • Wei, S.1    Xu, Y.2    Shi, H.3    Wong, S.H.4    Han, W.5    Talbot, K.6
  • 56
    • 33749563041 scopus 로고    scopus 로고
    • Dysbindin-1 is a synaptic and microtubular protein that binds brain snapin
    • Talbot K, Cho DS, Ong WY, Benson MA, Han LY, Kazi HA et al. Dysbindin-1 is a synaptic and microtubular protein that binds brain snapin. Hum Mol Genet 2006;15:3041-3054.
    • (2006) Hum Mol Genet , vol.15 , pp. 3041-3054
    • Talbot, K.1    Cho, D.S.2    Ong, W.Y.3    Benson, M.A.4    Han, L.Y.5    Kazi, H.A.6
  • 57
    • 33745480157 scopus 로고    scopus 로고
    • Ryanodine receptor interaction with the SNARE-associated protein snapin
    • Zissimopoulos S, West DJ, Williams AJ, Lai FA. Ryanodine receptor interaction with the SNARE-associated protein snapin. J Cell Sci 2006;119:2386-2397.
    • (2006) J Cell Sci , vol.119 , pp. 2386-2397
    • Zissimopoulos, S.1    West, D.J.2    Williams, A.J.3    Lai, F.A.4
  • 58
    • 84860389765 scopus 로고    scopus 로고
    • Autophosphorylation in the leucine-rich repeat kinase 2 (LRRK2) GTPase domain modifies kinase and GTP-binding activities
    • Webber PJ, Smith AD, Sen S, Renfrow MB, Mobley JA, West AB. Autophosphorylation in the leucine-rich repeat kinase 2 (LRRK2) GTPase domain modifies kinase and GTP-binding activities. J Mol Biol 2011;412:94-110.
    • (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.B.6
  • 59
    • 84858050446 scopus 로고    scopus 로고
    • ArfGAP1 is a GTPase activating protein for LRRK2: Reciprocal regulation of ArfGAP1 by LRRK2
    • Xiong Y, Yuan C, Chen R, Dawson TM, Dawson VL. ArfGAP1 is a GTPase activating protein for LRRK2: reciprocal regulation of ArfGAP1 by LRRK2. J Neurosci 2012;32:3877-3886.
    • (2012) J Neurosci , vol.32 , pp. 3877-3886
    • Xiong, Y.1    Yuan, C.2    Chen, R.3    Dawson, T.M.4    Dawson, V.L.5
  • 60
    • 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, Obata F. LRRK2 directly phosphorylates Akt1 as a possible physiological substrate: impairment of the kinase activity by Parkinson's disease-associated mutations. FEBS Lett 2011;585:2165-2170.
    • (2011) FEBS Lett , vol.585 , pp. 2165-2170
    • Ohta, E.1    Kawakami, F.2    Kubo, M.3    Obata, F.4
  • 61
    • 79951534656 scopus 로고    scopus 로고
    • LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool
    • Piccoli G, Condliffe SB, Bauer M, Giesert F, Boldt K, De Astis S et al. LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool. J Neurosci 2011;31:2225-2237.
    • (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
  • 62
    • 0027306854 scopus 로고
    • Inhibition of axonal growth by SNAP-25 antisense oligonucleotides in vitro and in vivo
    • Osen-Sand A, Catsicas M, Staple JK, Jones KA, Ayala G, Knowles J et al. Inhibition of axonal growth by SNAP-25 antisense oligonucleotides in vitro and in vivo. Nature 1993;364:445-448.
    • (1993) Nature , vol.364 , pp. 445-448
    • Osen-Sand, A.1    Catsicas, M.2    Staple, J.K.3    Jones, K.A.4    Ayala, G.5    Knowles, J.6
  • 63
    • 83255185773 scopus 로고    scopus 로고
    • Type VI adenylyl cyclase regulates neurite extension by binding to Snapin and Snap25
    • Wu CS, Lin JT, Chien CL, Chang WC, Lai HL, Chang CP et al. Type VI adenylyl cyclase regulates neurite extension by binding to Snapin and Snap25. Mol Cell Biol 2011;31:4874-4886.
    • (2011) Mol Cell Biol , vol.31 , pp. 4874-4886
    • Wu, C.S.1    Lin, J.T.2    Chien, C.L.3    Chang, W.C.4    Lai, H.L.5    Chang, C.P.6
  • 64
    • 84863241584 scopus 로고    scopus 로고
    • Roles of the Drosophila LRRK2 homolog in Rab7-dependent lysosomal positioning
    • Dodson MW, Zhang T, Jiang C, Chen S, Guo M. Roles of the Drosophila LRRK2 homolog in Rab7-dependent lysosomal positioning. Hum Mol Genet 2012;21:1350-1363.
    • (2012) Hum Mol Genet , vol.21 , pp. 1350-1363
    • Dodson, M.W.1    Zhang, T.2    Jiang, C.3    Chen, S.4    Guo, M.5
  • 65
    • 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 2010;65:66-79.
    • (2010) 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
  • 67
    • 58149456661 scopus 로고    scopus 로고
    • Prevention of interferon-stimulated gene expression using microRNAdesigned hairpins
    • Bauer M, Kinkl N, Meixner A, Kremmer E, Riemenschneider M, Forstl H et al. Prevention of interferon-stimulated gene expression using microRNAdesigned hairpins. Gene Ther 2009;16:142-147.
    • (2009) Gene Ther , vol.16 , pp. 142-147
    • Bauer, M.1    Kinkl, N.2    Meixner, A.3    Kremmer, E.4    Riemenschneider, M.5    Forstl, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.