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Volumn 2013, Issue 2, 2013, Pages

APP interacts with LRP4 and agrin to coordinate the development of the neuromuscular junction in mice

Author keywords

[No Author keywords available]

Indexed keywords

AGRIN; AMYLOID PRECURSOR PROTEIN; CHOLINERGIC RECEPTOR; HYBRID PROTEIN; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN 4; MALTOSE BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 84882685865     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.00220.001     Document Type: Article
Times cited : (50)

References (71)
  • 1
    • 0034103961 scopus 로고    scopus 로고
    • Developmental regulation of amyloid precursor protein at the neuromuscular junction in mouse skeletal muscle
    • doi: 10.1006/mcne.2000.0834
    • Akaaboune M, Allinquant B, Farza H, Roy K, Magoul R, Fiszman M, et al. 2000. Developmental regulation of amyloid precursor protein at the neuromuscular junction in mouse skeletal muscle. Mol Cell Neurosci 15:355-67. doi: 10.1006/mcne.2000.0834.
    • (2000) Mol Cell Neurosci , vol.15 , pp. 355-367
    • Akaaboune, M.1    Allinquant, B.2    Farza, H.3    Roy, K.4    Magoul, R.5    Fiszman, M.6
  • 2
    • 26444607532 scopus 로고    scopus 로고
    • Neuronal sorting protein-related receptor sorLA/LR11 regulates processing of the amyloid precursor protein
    • doi: 10.1073/pnas.0503689102
    • Andersen OM, Reiche J, Schmidt V, Gotthardt M, Spoelgen R, Behlke J, et al. 2005. Neuronal sorting protein-related receptor sorLA/LR11 regulates processing of the amyloid precursor protein. Proc Natl Acad Sci USA 102:13461-6. doi: 10.1073/pnas.0503689102.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13461-13466
    • Andersen, O.M.1    Reiche, J.2    Schmidt, V.3    Gotthardt, M.4    Spoelgen, R.5    Behlke, J.6
  • 3
    • 23744516021 scopus 로고    scopus 로고
    • Modulation of synaptic plasticity and memory by Reelin involves differential splicing of the lipoprotein receptor Apoer2
    • doi: 10.1016/j.neuron.2005.07.007
    • Beffert U, Weeber EJ, Durudas A, Qiu S, Masiulis I, Sweatt JD, et al. 2005. Modulation of synaptic plasticity and memory by Reelin involves differential splicing of the lipoprotein receptor Apoer2. Neuron 47:567-79. doi: 10.1016/j.neuron.2005.07.007.
    • (2005) Neuron , vol.47 , pp. 567-579
    • Beffert, U.1    Weeber, E.J.2    Durudas, A.3    Qiu, S.4    Masiulis, I.5    Sweatt, J.D.6
  • 4
    • 81255209222 scopus 로고    scopus 로고
    • A valid mouse model of AGRIN-associated congenital myasthenic syndrome
    • doi: 10.1093/hmg/ddr396
    • Bogdanik LP, Burgess RW. 2011. A valid mouse model of AGRIN-associated congenital myasthenic syndrome. Hum Mol Genet 20:4617-33. doi: 10.1093/hmg/ddr396.
    • (2011) Hum Mol Genet , vol.20 , pp. 4617-4633
    • Bogdanik, L.P.1    Burgess, R.W.2
  • 5
    • 1842451733 scopus 로고    scopus 로고
    • Kinase-and rapsyn-independent activities of the muscle-specific kinase (MuSK)
    • doi: 10.1016/j.neuroscience.2003.12.031
    • Bromann PA, Zhou H, Sanes JR. 2004. Kinase-and rapsyn-independent activities of the muscle-specific kinase (MuSK). Neuroscience 125:417-26. doi: 10.1016/j.neuroscience.2003.12.031.
    • (2004) Neuroscience , vol.125 , pp. 417-426
    • Bromann, P.A.1    Zhou, H.2    Sanes, J.R.3
  • 6
    • 0034597091 scopus 로고    scopus 로고
    • Agrin isoforms with distinct amino termini: Differential expression, localization, and function
    • doi: 10.1083/jcb.151.1.41
    • Burgess RW, Skarnes WC, Sanes JR. 2000. Agrin isoforms with distinct amino termini: differential expression, localization, and function. J Cell Biol 151:41-52. doi: 10.1083/jcb.151.1.41.
    • (2000) J Cell Biol , vol.151 , pp. 41-52
    • Burgess, R.W.1    Skarnes, W.C.2    Sanes, J.R.3
  • 7
    • 79955398495 scopus 로고    scopus 로고
    • Neuromuscular synaptic patterning requires the function of skeletal muscle dihydropyridine receptors
    • doi: 10.1038/nn.2792
    • Chen F, Liu Y, Sugiura Y, Allen PD, Gregg RG, Lin W. 2011. Neuromuscular synaptic patterning requires the function of skeletal muscle dihydropyridine receptors. Nat Neurosci 14:570-7. doi: 10.1038/nn.2792.
    • (2011) Nat Neurosci , vol.14 , pp. 570-577
    • Chen, F.1    Liu, Y.2    Sugiura, Y.3    Allen, P.D.4    Gregg, R.G.5    Lin, W.6
  • 8
    • 76549084350 scopus 로고    scopus 로고
    • Ubiquitin carboxyl-terminal hydrolase L1 is required for maintaining the structure and function of the neuromuscular junction
    • doi: 10.1073/pnas.0911516107
    • Chen F, Sugiura Y, Myers KG, Liu Y, Lin W. 2010a. Ubiquitin carboxyl-terminal hydrolase L1 is required for maintaining the structure and function of the neuromuscular junction. Proc Natl Acad Sci USA 107:1636-41. doi: 10.1073/pnas.0911516107.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 1636-1641
    • Chen, F.1    Sugiura, Y.2    Myers, K.G.3    Liu, Y.4    Lin, W.5
  • 9
    • 77955350021 scopus 로고    scopus 로고
    • ApoE4 reduces glutamate receptor function and synaptic plasticity by selectively impairing ApoE receptor recycling
    • doi: 10.1073/pnas.0914984107
    • Chen Y, Durakoglugil MS, Xian X, Herz J. 2010b. ApoE4 reduces glutamate receptor function and synaptic plasticity by selectively impairing ApoE receptor recycling. Proc Natl Acad Sci USA 107:12011-6. doi: 10.1073/pnas.0914984107.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 12011-12016
    • Chen, Y.1    Durakoglugil, M.S.2    Xian, X.3    Herz, J.4
  • 11
    • 57449084208 scopus 로고    scopus 로고
    • apoE isoform-specific disruption of amyloid β peptide clearance from mouse brain
    • doi: 10.1172/JCI36663
    • Deane R, Sagare A, Hamm K, Parisi M, Lane S, Finn MB, et al. 2008. apoE isoform-specific disruption of amyloid β peptide clearance from mouse brain. J Clin Invest 118:4002-13. doi: 10.1172/JCI36663.
    • (2008) J Clin Invest , vol.118 , pp. 4002-4013
    • Deane, R.1    Sagare, A.2    Hamm, K.3    Parisi, M.4    Lane, S.5    Finn, M.B.6
  • 12
    • 15844417385 scopus 로고    scopus 로고
    • The receptor tyrosine kinase MuSK is required for neuromuscular junction formation in vivo
    • doi: 10.1016/ S0092-8674(00)81251-9
    • DeChiara TM, Bowen DC, Valenzuela DM, Simmons MV, Poueymirou WT, Thomas S, et al. 1996. The receptor tyrosine kinase MuSK is required for neuromuscular junction formation in vivo. Cell 85:501-12. doi: 10.1016/ S0092-8674(00)81251-9.
    • (1996) Cell , vol.85 , pp. 501-512
    • Dechiara, T.M.1    Bowen, D.C.2    Valenzuela, D.M.3    Simmons, M.V.4    Poueymirou, W.T.5    Thomas, S.6
  • 13
    • 78649348989 scopus 로고    scopus 로고
    • Lipoprotein receptors-an evolutionarily ancient multifunctional receptor family
    • doi: 10.1515/BC.2010.129
    • Dieckmann M, Dietrich MF, Herz J. 2010. Lipoprotein receptors-an evolutionarily ancient multifunctional receptor family. Biol Chem 391:1341-63. doi: 10.1515/BC.2010.129.
    • (2010) Biol Chem , vol.391 , pp. 1341-1363
    • Dieckmann, M.1    Dietrich, M.F.2    Herz, J.3
  • 14
    • 77956309791 scopus 로고    scopus 로고
    • Ectodomains of the LDL receptor-related proteins LRP1b and LRP4 have anchorage independent functions in vivo
    • doi: 10.1371/journal.pone.0009960
    • Dietrich MF, van der Weyden L, Prosser HM, Bradley A, Herz J, Adams DJ. 2010. Ectodomains of the LDL receptor-related proteins LRP1b and LRP4 have anchorage independent functions in vivo. PLOS ONE 5:e9960. doi: 10.1371/journal.pone.0009960.
    • (2010) PLOS ONE , vol.5
    • Dietrich, M.F.1    van der Weyden, L.2    Prosser, H.M.3    Bradley, A.4    Herz, J.5    Adams, D.J.6
  • 16
    • 0026652948 scopus 로고
    • RNA splicing regulates agrin-mediated acetylcholine receptor clustering activity on cultured myotubes
    • doi: 10.1016/0896-6273(92)90129-2
    • Ferns M, Hoch W, Campanelli JT, Rupp F, Hall ZW, Scheller RH. 1992. RNA splicing regulates agrin-mediated acetylcholine receptor clustering activity on cultured myotubes. Neuron 8:1079-86. doi: 10.1016/0896-6273(92)90129-2.
    • (1992) Neuron , vol.8 , pp. 1079-1086
    • Ferns, M.1    Hoch, W.2    Campanelli, J.T.3    Rupp, F.4    Hall, Z.W.5    Scheller, R.H.6
  • 17
    • 0027517961 scopus 로고
    • The ability of agrin to cluster AChRs depends on alternative splicing and on cell surface proteoglycans
    • doi: 10.1016/0896-6273(93)90153-I
    • Ferns MJ, Campanelli JT, Hoch W, Scheller RH, Hall Z. 1993. The ability of agrin to cluster AChRs depends on alternative splicing and on cell surface proteoglycans. Neuron 11:491-502. doi: 10.1016/0896-6273(93)90153-I.
    • (1993) Neuron , vol.11 , pp. 491-502
    • Ferns, M.J.1    Campanelli, J.T.2    Hoch, W.3    Scheller, R.H.4    Hall, Z.5
  • 18
    • 33646046808 scopus 로고    scopus 로고
    • Structure of an LDLR-RAP complex reveals a general mode for ligand recognition by lipoprotein receptors
    • doi: 10.1016/j.molcel.2006.02.021
    • Fisher C, Beglova N, Blacklow SC. 2006. Structure of an LDLR-RAP complex reveals a general mode for ligand recognition by lipoprotein receptors. Mol Cell 22:277-83. doi: 10.1016/j.molcel.2006.02.021.
    • (2006) Mol Cell , vol.22 , pp. 277-283
    • Fisher, C.1    Beglova, N.2    Blacklow, S.C.3
  • 19
    • 33747080004 scopus 로고    scopus 로고
    • MuSK expressed in the brain mediates cholinergic responses, synaptic plasticity, and memory formation
    • doi: 10.1523/JNEUROSCI.1674-06.2006
    • Garcia-Osta A, Tsokas P, Pollonini G, Landau EM, Blitzer R, Alberini CM. 2006. MuSK expressed in the brain mediates cholinergic responses, synaptic plasticity, and memory formation. J Neurosci 26:7919-32. doi: 10.1523/JNEUROSCI.1674-06.2006.
    • (2006) J Neurosci , vol.26 , pp. 7919-7932
    • Garcia-Osta, A.1    Tsokas, P.2    Pollonini, G.3    Landau, E.M.4    Blitzer, R.5    Alberini, C.M.6
  • 20
    • 0029893117 scopus 로고    scopus 로고
    • Defective neuromuscular synaptogenesis in agrin-deficient mutant mice
    • doi: 10.1016/S0092-8674(00)81253-2
    • Gautam M, Noakes PG, Moscoso L, Rupp F, Scheller RH, Merlie JP, et al. 1996. Defective neuromuscular synaptogenesis in agrin-deficient mutant mice. Cell 85:525-35. doi: 10.1016/S0092-8674(00)81253-2.
    • (1996) Cell , vol.85 , pp. 525-535
    • Gautam, M.1    Noakes, P.G.2    Moscoso, L.3    Rupp, F.4    Scheller, R.H.5    Merlie, J.P.6
  • 21
    • 0026088977 scopus 로고
    • Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
    • doi: 10.1038/349704a0
    • Goate A, Chartier-Harlin MC, Mullan M, Brown J, Crawford F, Fidani L, et al. 1991. Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature 349:704-6. doi: 10.1038/349704a0.
    • (1991) Nature , vol.349 , pp. 704-706
    • Goate, A.1    Chartier-Harlin, M.C.2    Mullan, M.3    Brown, J.4    Crawford, F.5    Fidani, L.6
  • 22
    • 80855144111 scopus 로고    scopus 로고
    • The extracellular region of Lrp4 is sufficient to mediate neuromuscular synapse formation
    • doi: 10.1002/dvdy.22772
    • Gomez AM, Burden SJ. 2011. The extracellular region of Lrp4 is sufficient to mediate neuromuscular synapse formation. Dev Dyn 240:2626-33. doi: 10.1002/dvdy.22772.
    • (2011) Dev Dyn , vol.240 , pp. 2626-2633
    • Gomez, A.M.1    Burden, S.J.2
  • 23
    • 0034682827 scopus 로고    scopus 로고
    • Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction
    • doi: 10.1074/jbc.M000955200
    • Gotthardt M, Trommsdorff M, Nevitt MF, Shelton J, Richardson JA, Stockinger W, et al. 2000. Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction. J Biol Chem 275:25616-24. doi: 10.1074/jbc.M000955200.
    • (2000) J Biol Chem , vol.275 , pp. 25616-25624
    • Gotthardt, M.1    Trommsdorff, M.2    Nevitt, M.F.3    Shelton, J.4    Richardson, J.A.5    Stockinger, W.6
  • 24
    • 0032864614 scopus 로고    scopus 로고
    • Agrin-independent activation of the agrin signal transduction pathway
    • doi: 10.1002/(SICI)1097-4695(19990905)40:3<356::AID-NEU7>3.0.CO;2-F
    • Grow WA, Ferns M, Gordon H. 1999a. Agrin-independent activation of the agrin signal transduction pathway. J Neurobiol 40:356-65. doi: 10.1002/(SICI)1097-4695(19990905)40:3<356::AID-NEU7>3.0.CO;2-F.
    • (1999) J Neurobiol , vol.40 , pp. 356-365
    • Grow, W.A.1    Ferns, M.2    Gordon, H.3
  • 25
    • 0041382568 scopus 로고    scopus 로고
    • A mechanism for acetylcholine receptor clustering distinct from agrin signaling
    • doi: 10.1159/000017411
    • Grow WA, Ferns M, Gordon H. 1999b. A mechanism for acetylcholine receptor clustering distinct from agrin signaling. Dev Neurosci 21:436-43. doi: 10.1159/000017411.
    • (1999) Dev Neurosci , vol.21 , pp. 436-443
    • Grow, W.A.1    Ferns, M.2    Gordon, H.3
  • 26
    • 0027354449 scopus 로고
    • Synaptic structure and development: The neuromuscular junction
    • Hall ZW, Sanes JR. 1993. Synaptic structure and development: the neuromuscular junction. Cell 72:99-121.
    • (1993) Cell , vol.72 , pp. 99-121
    • Hall, Z.W.1    Sanes, J.R.2
  • 27
    • 0034305790 scopus 로고    scopus 로고
    • Apolipoprotein E receptors: Linking brain development and Alzheimer's disease
    • doi: 10.1038/35036221
    • Herz J, Beffert U. 2000. Apolipoprotein E receptors: linking brain development and Alzheimer's disease. Nat Rev Neurosci 1:51-8. doi: 10.1038/35036221.
    • (2000) Nat Rev Neurosci , vol.1 , pp. 51-58
    • Herz, J.1    Beffert, U.2
  • 28
    • 33750333569 scopus 로고    scopus 로고
    • Reelin, lipoprotein receptors and synaptic plasticity
    • doi: 10.1038/nrn2009
    • Herz J, Chen Y. 2006. Reelin, lipoprotein receptors and synaptic plasticity. Nat Rev Neurosci 7:850-9. doi: 10.1038/nrn2009.
    • (2006) Nat Rev Neurosci , vol.7 , pp. 850-859
    • Herz, J.1    Chen, Y.2
  • 29
    • 0025786502 scopus 로고
    • 39-kDa protein modulates binding of ligands to low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor
    • Herz J, Goldstein JL, Strickland DK, Ho YK, Brown MS. 1991. 39-kDa protein modulates binding of ligands to low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor. J Biol Chem 266:21232-8.
    • (1991) J Biol Chem , vol.266 , pp. 21232-21238
    • Herz, J.1    Goldstein, J.L.2    Strickland, D.K.3    Ho, Y.K.4    Brown, M.S.5
  • 30
    • 33644844430 scopus 로고    scopus 로고
    • Synapse disassembly and formation of new synapses in postnatal muscle upon conditional inactivation of MuSK
    • doi: 10.1016/j.mcn.2005.10.020
    • Hesser BA, Henschel O, Witzemann V. 2006. Synapse disassembly and formation of new synapses in postnatal muscle upon conditional inactivation of MuSK. Mol Cell Neurosci 31:470-80. doi: 10.1016/j.mcn.2005.10.020.
    • (2006) Mol Cell Neurosci , vol.31 , pp. 470-480
    • Hesser, B.A.1    Henschel, O.2    Witzemann, V.3
  • 31
    • 27144504391 scopus 로고    scopus 로고
    • F-spondin interaction with the apolipoprotein E receptor ApoEr2 affects processing of amyloid precursor protein
    • doi: 10.1128/MCB.25.21.9259-9268.2005
    • Hoe HS, Wessner D, Beffert U, Becker AG, Matsuoka Y, Rebeck GW. 2005. F-spondin interaction with the apolipoprotein E receptor ApoEr2 affects processing of amyloid precursor protein. Mol Cell Biol 25:9259-68. doi: 10.1128/MCB.25.21.9259-9268.2005.
    • (2005) Mol Cell Biol , vol.25 , pp. 9259-9268
    • Hoe, H.S.1    Wessner, D.2    Beffert, U.3    Becker, A.G.4    Matsuoka, Y.5    Rebeck, G.W.6
  • 32
    • 27944471018 scopus 로고    scopus 로고
    • Abnormal development of the apical ectodermal ridge and polysyndactyly in Megf7-deficient mice
    • doi: 10.1093/hmg/ddi381
    • Johnson EB, Hammer RE, Herz J. 2005. Abnormal development of the apical ectodermal ridge and polysyndactyly in Megf7-deficient mice. Hum Mol Genet 14:3523-38. doi: 10.1093/hmg/ddi381.
    • (2005) Hum Mol Genet , vol.14 , pp. 3523-3538
    • Johnson, E.B.1    Hammer, R.E.2    Herz, J.3
  • 33
    • 33749431699 scopus 로고    scopus 로고
    • Defective splicing of Megf7/Lrp4, a regulator of distal limb development, in autosomal recessive mulefoot disease
    • doi: 10.1016/j.ygeno.2006.08.005
    • Johnson EB, Steffen DJ, Lynch KW, Herz J. 2006. Defective splicing of Megf7/Lrp4, a regulator of distal limb development, in autosomal recessive mulefoot disease. Genomics 88:600-9. doi: 10.1016/j.ygeno.2006.08.005.
    • (2006) Genomics , vol.88 , pp. 600-609
    • Johnson, E.B.1    Steffen, D.J.2    Lynch, K.W.3    Herz, J.4
  • 34
    • 77956414899 scopus 로고    scopus 로고
    • Lrp4 regulates initiation of ureteric budding and is crucial for kidney formation-a mouse model for Cenani-Lenz syndrome
    • doi: 10.1371/journal.pone.0010418
    • Karner CM, Dietrich MF, Johnson EB, Kappesser N, Tennert C, Percin F, et al. 2010. Lrp4 regulates initiation of ureteric budding and is crucial for kidney formation-a mouse model for Cenani-Lenz syndrome. PLOS ONE 5:e10418. doi: 10.1371/journal.pone.0010418.
    • (2010) PLOS ONE , vol.5
    • Karner, C.M.1    Dietrich, M.F.2    Johnson, E.B.3    Kappesser, N.4    Tennert, C.5    Percin, F.6
  • 35
    • 53649090611 scopus 로고    scopus 로고
    • O-fucosylation of muscle agrin determines its ability to cluster acetylcholine receptors
    • doi: 10.1016/j. mcn.2008.07.026
    • Kim ML, Chandrasekharan K, Glass M, Shi S, Stahl MC, Kaspar B, et al. 2008a. O-fucosylation of muscle agrin determines its ability to cluster acetylcholine receptors. Mol Cell Neurosci 39:452-64. doi: 10.1016/j. mcn.2008.07.026.
    • (2008) Mol Cell Neurosci , vol.39 , pp. 452-464
    • Kim, M.L.1    Chandrasekharan, K.2    Glass, M.3    Shi, S.4    Stahl, M.C.5    Kaspar, B.6
  • 36
    • 55049092996 scopus 로고    scopus 로고
    • Lrp4 is a receptor for agrin and forms a complex with MuSK
    • doi: 10.1016/j.cell.2008.10.002
    • Kim N, Stiegler AL, Cameron TO, Hallock PT, Gomez AM, Huang JH, et al. 2008b. Lrp4 is a receptor for agrin and forms a complex with MuSK. Cell 135:334-42. doi: 10.1016/j.cell.2008.10.002.
    • (2008) Cell , vol.135 , pp. 334-342
    • Kim, N.1    Stiegler, A.L.2    Cameron, T.O.3    Hallock, P.T.4    Gomez, A.M.5    Huang, J.H.6
  • 37
    • 0029128232 scopus 로고
    • LDL receptor-related protein, a multifunctional ApoE receptor, binds secreted beta-amyloid precursor protein and mediates its degradation
    • doi: 10.1016/0092-8674(95)90320-8
    • Kounnas MZ, Moir RD, Rebeck GW, Bush AI, Argraves WS, Tanzi RE, et al. 1995. LDL receptor-related protein, a multifunctional ApoE receptor, binds secreted beta-amyloid precursor protein and mediates its degradation. Cell 82:331-40. doi: 10.1016/0092-8674(95)90320-8.
    • (1995) Cell , vol.82 , pp. 331-340
    • Kounnas, M.Z.1    Moir, R.D.2    Rebeck, G.W.3    Bush, A.I.4    Argraves, W.S.5    Tanzi, R.E.6
  • 38
    • 34447132889 scopus 로고    scopus 로고
    • Synapse loss in cortex of agrin-deficient mice after genetic rescue of perinatal death
    • doi: 10.1523/ JNEUROSCI.1609-07.2007
    • Ksiazek I, Burkhardt C, Lin S, Seddik R, Maj M, Bezakova G, et al. 2007. Synapse loss in cortex of agrin-deficient mice after genetic rescue of perinatal death. J Neurosci 27:7183-95. doi: 10.1523/ JNEUROSCI.1609-07.2007.
    • (2007) J Neurosci , vol.27 , pp. 7183-7195
    • Ksiazek, I.1    Burkhardt, C.2    Lin, S.3    Seddik, R.4    Maj, M.5    Bezakova, G.6
  • 39
    • 77957254613 scopus 로고    scopus 로고
    • Genetic dissection of the amyloid precursor protein in developmental function and amyloid pathogenesis
    • doi: 10.1074/jbc. M110.137729
    • Li H, Wang Z, Wang B, Guo Q, Dolios G, Tabuchi K, et al. 2010. Genetic dissection of the amyloid precursor protein in developmental function and amyloid pathogenesis. J Biol Chem 285:30598-605. doi: 10.1074/jbc. M110.137729.
    • (2010) J Biol Chem , vol.285 , pp. 30598-30605
    • Li, H.1    Wang, Z.2    Wang, B.3    Guo, Q.4    Dolios, G.5    Tabuchi, K.6
  • 40
    • 0035953645 scopus 로고    scopus 로고
    • Distinct roles of nerve and muscle in postsynaptic differentiation of the neuromuscular synapse
    • doi: 10.1038/35074025
    • Lin W, Burgess RW, Dominguez B, Pfaff SL, Sanes JR, Lee KF. 2001. Distinct roles of nerve and muscle in postsynaptic differentiation of the neuromuscular synapse. Nature 410:1057-64. doi: 10.1038/35074025.
    • (2001) Nature , vol.410 , pp. 1057-1064
    • Lin, W.1    Burgess, R.W.2    Dominguez, B.3    Pfaff, S.L.4    Sanes, J.R.5    Lee, K.F.6
  • 41
    • 67349270258 scopus 로고    scopus 로고
    • Abnormal development of the neuromuscular junction in Nedd4-deficient mice
    • doi: 10.1016/j.ydbio.2009.03.023
    • Liu Y, Oppenheim RW, Sugiura Y, Lin W. 2009. Abnormal development of the neuromuscular junction in Nedd4-deficient mice. Dev Biol 330:153-66. doi: 10.1016/j.ydbio.2009.03.023.
    • (2009) Dev Biol , vol.330 , pp. 153-166
    • Liu, Y.1    Oppenheim, R.W.2    Sugiura, Y.3    Lin, W.4
  • 42
    • 46749156985 scopus 로고    scopus 로고
    • Essential roles of the acetylcholine receptor γ-subunit in neuromuscular synaptic patterning
    • doi: 10.1242/dev.018119
    • Liu Y, Padgett D, Takahashi M, Li H, Sayeed A, Teichert RW, et al. 2008. Essential roles of the acetylcholine receptor γ-subunit in neuromuscular synaptic patterning. Development 135:1957-67. doi: 10.1242/dev.018119.
    • (2008) Development , vol.135 , pp. 1957-1967
    • Liu, Y.1    Padgett, D.2    Takahashi, M.3    Li, H.4    Sayeed, A.5    Teichert, R.W.6
  • 43
    • 0028935085 scopus 로고
    • Role for a synapse-specific carbohydrate in agrin-induced clustering of acetylcholine receptors
    • doi: 10.1016/0896-6273(95)90218-X
    • Martin PT, Sanes JR. 1995. Role for a synapse-specific carbohydrate in agrin-induced clustering of acetylcholine receptors. Neuron 14:743-54. doi: 10.1016/0896-6273(95)90218-X.
    • (1995) Neuron , vol.14 , pp. 743-754
    • Martin, P.T.1    Sanes, J.R.2
  • 44
    • 63949084694 scopus 로고    scopus 로고
    • Lipoprotein receptors and cholesterol in APP trafficking and proteolytic processing, implications for Alzheimer's disease
    • doi: 10.1016/j.semcdb.2008.10.005
    • Marzolo MP, Bu G. 2009. Lipoprotein receptors and cholesterol in APP trafficking and proteolytic processing, implications for Alzheimer's disease. Semin Cell Dev Biol 20:191-200. doi: 10.1016/j.semcdb.2008.10.005.
    • (2009) Semin Cell Dev Biol , vol.20 , pp. 191-200
    • Marzolo, M.P.1    Bu, G.2
  • 45
    • 68349146507 scopus 로고    scopus 로고
    • Transmembrane agrin regulates dendritic filopodia and synapse formation in mature hippocampal neuron cultures
    • doi: 10.1016/j. neuroscience.2009.06.012
    • McCroskery S, Bailey A, Lin L, Daniels MP. 2009. Transmembrane agrin regulates dendritic filopodia and synapse formation in mature hippocampal neuron cultures. Neuroscience 163:168-79. doi: 10.1016/j. neuroscience.2009.06.012.
    • (2009) Neuroscience , vol.163 , pp. 168-179
    • McCroskery, S.1    Bailey, A.2    Lin, L.3    Daniels, M.P.4
  • 47
    • 0028344867 scopus 로고
    • Localization and alternative splicing of agrin mRNA in adult rat brain: Transcripts encoding isoforms that aggregate acetylcholine receptors are not restricted to cholinergic regions
    • O'Connor LT, Lauterborn JC, Gall CM, Smith MA. 1994. Localization and alternative splicing of agrin mRNA in adult rat brain: transcripts encoding isoforms that aggregate acetylcholine receptors are not restricted to cholinergic regions. J Neurosci 14:1141-52.
    • (1994) J Neurosci , vol.14 , pp. 1141-1152
    • O'Connor, L.T.1    Lauterborn, J.C.2    Gall, C.M.3    Smith, M.A.4
  • 48
    • 58149330442 scopus 로고    scopus 로고
    • Lrp4 modulates extracellular integration of cell signaling pathways in development
    • doi: 10.1371/journal.pone.0004092
    • Ohazama A, Johnson EB, Ota MS, Choi HY, Porntaveetus T, Oommen S, et al. 2008. Lrp4 modulates extracellular integration of cell signaling pathways in development. PLOS ONE 3:e4092. doi: 10.1371/journal.pone.0004092.
    • (2008) PLOS ONE , vol.3
    • Ohazama, A.1    Johnson, E.B.2    Ota, M.S.3    Choi, H.Y.4    Porntaveetus, T.5    Oommen, S.6
  • 49
    • 0036846405 scopus 로고    scopus 로고
    • The cytoplasmic domain of the LDL receptor-related protein regulates multiple steps in APP processing
    • doi: 10.1093/emboj/cdf568
    • Pietrzik CU, Busse T, Merriam DE, Weggen S, Koo EH. 2002. The cytoplasmic domain of the LDL receptor-related protein regulates multiple steps in APP processing. EMBO J 21:5691-700. doi: 10.1093/emboj/cdf568.
    • (2002) EMBO J , vol.21 , pp. 5691-5700
    • Pietrzik, C.U.1    Busse, T.2    Merriam, D.E.3    Weggen, S.4    Koo, E.H.5
  • 50
    • 42149122012 scopus 로고    scopus 로고
    • Functional role of lipoprotein receptors in Alzheimer's disease
    • doi: 10.2174/156720508783884675
    • Pietrzik CU, Jaeger S. 2008. Functional role of lipoprotein receptors in Alzheimer's disease. Curr Alzheimer Res 5:15-25. doi: 10.2174/156720508783884675.
    • (2008) Curr Alzheimer Res , vol.5 , pp. 15-25
    • Pietrzik, C.U.1    Jaeger, S.2
  • 51
    • 0032936983 scopus 로고    scopus 로고
    • Development of the vertebrate neuromuscular junction
    • doi: 10.1146/annurev.neuro.22.1.389
    • Sanes JR, Lichtman JW. 1999. Development of the vertebrate neuromuscular junction. Annu Rev Neurosci 22:389-442. doi: 10.1146/annurev.neuro.22.1.389.
    • (1999) Annu Rev Neurosci , vol.22 , pp. 389-442
    • Sanes, J.R.1    Lichtman, J.W.2
  • 52
    • 0035511932 scopus 로고    scopus 로고
    • Induction, assembly, maturation and maintenance of a postsynaptic apparatus
    • doi: 10.1038/35097557
    • Sanes JR, Lichtman JW. 2001. Induction, assembly, maturation and maintenance of a postsynaptic apparatus. Nat Rev Neurosci 2:791-805. doi: 10.1038/35097557.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 791-805
    • Sanes, J.R.1    Lichtman, J.W.2
  • 53
    • 0027365822 scopus 로고
    • Increased amyloid beta-peptide deposition in cerebral cortex as a consequence of apolipoprotein E genotype in late-onset Alzheimer disease
    • doi: 10.1073/pnas.90.20.9649
    • Schmechel DE, Saunders AM, Strittmatter WJ, Crain BJ, Hulette CM, Joo SH, et al. 1993. Increased amyloid beta-peptide deposition in cerebral cortex as a consequence of apolipoprotein E genotype in late-onset Alzheimer disease. Proc Natl Acad Sci USA 90:9649-53. doi: 10.1073/pnas.90.20.9649.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9649-9653
    • Schmechel, D.E.1    Saunders, A.M.2    Strittmatter, W.J.3    Crain, B.J.4    Hulette, C.M.5    Joo, S.H.6
  • 54
    • 27144547977 scopus 로고    scopus 로고
    • Homo-and heterodimerization of APP family members promotes intercellular adhesion
    • doi: 10.1038/sj.emboj.7600824
    • Soba P, Eggert S, Wagner K, Zentgraf H, Siehl K, Kreger S, et al. 2005. Homo-and heterodimerization of APP family members promotes intercellular adhesion. EMBO J 24:3624-34. doi: 10.1038/sj.emboj.7600824.
    • (2005) EMBO J , vol.24 , pp. 3624-3634
    • Soba, P.1    Eggert, S.2    Wagner, K.3    Zentgraf, H.4    Siehl, K.5    Kreger, S.6
  • 55
    • 0028823323 scopus 로고
    • Tissue-and age-specific expression patterns of alternatively spliced agrin mRNA transcripts in embryonic rat suggest novel developmental roles
    • Stone DM, Nikolics K. 1995. Tissue-and age-specific expression patterns of alternatively spliced agrin mRNA transcripts in embryonic rat suggest novel developmental roles. J Neurosci 15:6767-78.
    • (1995) J Neurosci , vol.15 , pp. 6767-6778
    • Stone, D.M.1    Nikolics, K.2
  • 56
    • 0033568874 scopus 로고    scopus 로고
    • The Drosophila beta-amyloid precursor protein homolog promotes synapse differentiation at the neuromuscular junction
    • Torroja L, Packard M, Gorczyca M, White K, Budnik V. 1999. The Drosophila beta-amyloid precursor protein homolog promotes synapse differentiation at the neuromuscular junction. J Neurosci 19:7793-803.
    • (1999) J Neurosci , vol.19 , pp. 7793-7803
    • Torroja, L.1    Packard, M.2    Gorczyca, M.3    White, K.4    Budnik, V.5
  • 58
    • 0033003134 scopus 로고    scopus 로고
    • Reeler/Disabled-like disruption of neuronal migration in knockout mice lacking the VLDL receptor and ApoE receptor 2
    • doi: 10.1016/S0092-8674(00)80782-5
    • Trommsdorff M, Gotthardt M, Hiesberger T, Shelton J, Stockinger W, Nimpf J, et al. 1999. Reeler/Disabled-like disruption of neuronal migration in knockout mice lacking the VLDL receptor and ApoE receptor 2. Cell 97:689-701. doi: 10.1016/S0092-8674(00)80782-5.
    • (1999) Cell , vol.97 , pp. 689-701
    • Trommsdorff, M.1    Gotthardt, M.2    Hiesberger, T.3    Shelton, J.4    Stockinger, W.5    Nimpf, J.6
  • 59
    • 0034629292 scopus 로고    scopus 로고
    • Modulation of ß-amyloid precursor protein processing by the low density lipoprotein receptor-related protein (LRP). Evidence that LRP contributes to the pathogenesis of Alzheimer's disease
    • doi: 10.1074/jbc.275.10.7410
    • Ulery PG, Beers J, Mikhailenko I, Tanzi RE, Rebeck GW, Hyman BT, et al. 2000. Modulation of ß-amyloid precursor protein processing by the low density lipoprotein receptor-related protein (LRP). Evidence that LRP contributes to the pathogenesis of Alzheimer's disease. J Biol Chem 275:7410-5. doi: 10.1074/jbc.275.10.7410.
    • (2000) J Biol Chem , vol.275 , pp. 7410-7415
    • Ulery, P.G.1    Beers, J.2    Mikhailenko, I.3    Tanzi, R.E.4    Rebeck, G.W.5    Hyman, B.T.6
  • 61
    • 69749115919 scopus 로고    scopus 로고
    • Presynaptic and postsynaptic interaction of the amyloid precursor protein promotes peripheral and central synaptogenesis
    • doi: 10.1523/JNEUROSCI.2132-09.2009
    • Wang Z, Wang B, Yang L, Guo Q, Aithmitti N, Songyang Z, et al. 2009. Presynaptic and postsynaptic interaction of the amyloid precursor protein promotes peripheral and central synaptogenesis. J Neurosci 29:10788-801. doi: 10.1523/JNEUROSCI.2132-09.2009.
    • (2009) J Neurosci , vol.29 , pp. 10788-10801
    • Wang, Z.1    Wang, B.2    Yang, L.3    Guo, Q.4    Aithmitti, N.5    Songyang, Z.6
  • 62
    • 33846155569 scopus 로고    scopus 로고
    • LDL-receptor-related protein 4 is crucial for formation of the neuromuscular junction
    • doi: 10.1242/dev.02696
    • Weatherbee SD, Anderson KV, Niswander LA. 2006. LDL-receptor-related protein 4 is crucial for formation of the neuromuscular junction. Development 133:4993-5000. doi: 10.1242/dev.02696.
    • (2006) Development , vol.133 , pp. 4993-5000
    • Weatherbee, S.D.1    Anderson, K.V.2    Niswander, L.A.3
  • 63
    • 0037131401 scopus 로고    scopus 로고
    • Reelin and ApoE receptors cooperate to enhance hippocampal synaptic plasticity and learning
    • doi: 10.1074/ jbc.M205147200
    • Weeber EJ, Beffert U, Jones C, Christian JM, Forster E, Sweatt JD, et al. 2002. Reelin and ApoE receptors cooperate to enhance hippocampal synaptic plasticity and learning. J Biol Chem 277:39944-52. doi: 10.1074/ jbc.M205147200.
    • (2002) J Biol Chem , vol.277 , pp. 39944-39952
    • Weeber, E.J.1    Beffert, U.2    Jones, C.3    Christian, J.M.4    Forster, E.5    Sweatt, J.D.6
  • 64
    • 79957909084 scopus 로고    scopus 로고
    • APP and APLP2 are essential at PNS and CNS synapses for transmission, spatial learning and LTP
    • doi: 10.1038/ emboj.2011.119
    • Weyer SW, Klevanski M, Delekate A, Voikar V, Aydin D, Hick M, et al. 2011. APP and APLP2 are essential at PNS and CNS synapses for transmission, spatial learning and LTP. EMBO J 30:2266-80. doi: 10.1038/ emboj.2011.119.
    • (2011) EMBO J , vol.30 , pp. 2266-2280
    • Weyer, S.W.1    Klevanski, M.2    Delekate, A.3    Voikar, V.4    Aydin, D.5    Hick, M.6
  • 65
    • 84865963074 scopus 로고    scopus 로고
    • Distinct roles of muscle and motoneuron LRP4 in neuromuscular junction formation
    • doi: 10.1016/j.neuron.2012.04.033
    • Wu H, Lu Y, Shen C, Patel N, Gan L, Xiong WC, et al. 2012. Distinct roles of muscle and motoneuron LRP4 in neuromuscular junction formation. Neuron 75:94-107. doi: 10.1016/j.neuron.2012.04.033.
    • (2012) Neuron , vol.75 , pp. 94-107
    • Wu, H.1    Lu, Y.2    Shen, C.3    Patel, N.4    Gan, L.5    Xiong, W.C.6
  • 66
    • 77950462859 scopus 로고    scopus 로고
    • To build a synapse: Signaling pathways in neuromuscular junction assembly
    • doi: 10.1242/dev.038711
    • Wu H, Xiong WC, Mei L. 2010. To build a synapse: signaling pathways in neuromuscular junction assembly. Development 137:1017-33. doi: 10.1242/dev.038711.
    • (2010) Development , vol.137 , pp. 1017-1033
    • Wu, H.1    Xiong, W.C.2    Mei, L.3
  • 67
    • 0034983538 scopus 로고    scopus 로고
    • Patterning of muscle acetylcholine receptor gene expression in the absence of motor innervation
    • doi: 10.1016/ S0896-6273(01)00287-2
    • Yang X, Arber S, William C, Li L, Tanabe Y, Jessell TM, et al. 2001. Patterning of muscle acetylcholine receptor gene expression in the absence of motor innervation. Neuron 30:399-410. doi: 10.1016/ S0896-6273(01)00287-2.
    • (2001) Neuron , vol.30 , pp. 399-410
    • Yang, X.1    Arber, S.2    William, C.3    Li, L.4    Tanabe, Y.5    Jessell, T.M.6
  • 68
    • 84866480273 scopus 로고    scopus 로고
    • Lrp4 is a retrograde signal for presynaptic differentiation at neuromuscular synapses
    • doi: 10.1038/nature11348
    • Yumoto N, Kim N, Burden SJ. 2012. Lrp4 is a retrograde signal for presynaptic differentiation at neuromuscular synapses. Nature 489:438-42. doi: 10.1038/nature11348.
    • (2012) Nature , vol.489 , pp. 438-442
    • Yumoto, N.1    Kim, N.2    Burden, S.J.3
  • 69
    • 53849093434 scopus 로고    scopus 로고
    • LRP4 serves as a coreceptor of agrin
    • doi: 10.1016/j.neuron.2008.10.006
    • Zhang B, Luo S, Wang Q, Suzuki T, Xiong WC, Mei L. 2008. LRP4 serves as a coreceptor of agrin. Neuron 60:285-97. doi: 10.1016/j.neuron.2008.10.006.
    • (2008) Neuron , vol.60 , pp. 285-297
    • Zhang, B.1    Luo, S.2    Wang, Q.3    Suzuki, T.4    Xiong, W.C.5    Mei, L.6
  • 70
    • 0028988801 scopus 로고
    • ß-Amyloid precursor protein-deficient mice show reactive gliosis and decreased locomotor activity
    • doi: 10.1016/0092-8674(95)90073-X
    • Zheng H, Jiang M, Trumbauer ME, Sirinathsinghji DJ, Hopkins R, Smith DW, et al. 1995. ß-Amyloid precursor protein-deficient mice show reactive gliosis and decreased locomotor activity. Cell 81:525-31. doi: 10.1016/0092-8674(95)90073-X.
    • (1995) Cell , vol.81 , pp. 525-531
    • Zheng, H.1    Jiang, M.2    Trumbauer, M.E.3    Sirinathsinghji, D.J.4    Hopkins, R.5    Smith, D.W.6
  • 71
    • 84863011431 scopus 로고    scopus 로고
    • Structural basis of agrin-LRP4-MuSK signaling
    • doi: 10.1101/gad.180885.111
    • Zong Y, Zhang B, Gu S, Lee K, Zhou J, Yao G, et al. 2012. Structural basis of agrin-LRP4-MuSK signaling. Genes Dev 26:247-58. doi: 10.1101/gad.180885.111.
    • (2012) Genes Dev , vol.26 , pp. 247-258
    • Zong, Y.1    Zhang, B.2    Gu, S.3    Lee, K.4    Zhou, J.5    Yao, G.6


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