메뉴 건너뛰기




Volumn 8, Issue , 2007, Pages

Tyrosine phosphatases such as SHP-2 act in a balance with Src-family kinases in stabilization of postsynaptic clusters of acetylcholine receptors

Author keywords

[No Author keywords available]

Indexed keywords

AGRIN; CHOLINERGIC RECEPTOR; PERVANADATE; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE INHIBITOR; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE INHIBITOR; PROTEIN TYROSINE PHOSPHATASE SHP 2; ACETYLCHOLINE; ENZYME INHIBITOR; MUSK PROTEIN, MOUSE; PROTEIN TYROSINE PHOSPHATASE, NON RECEPTOR TYPE 11; PROTEIN TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 11; SIGNAL PEPTIDE; UNCLASSIFIED DRUG;

EID: 34447639963     PISSN: None     EISSN: 14712202     Source Type: Journal    
DOI: 10.1186/1471-2202-8-46     Document Type: Article
Times cited : (9)

References (58)
  • 1
    • 0035511932 scopus 로고    scopus 로고
    • Induction, assembly, maturation and maintenance of a postsynaptic apparatus
    • 10.1038/35097557 11715056
    • Sanes JR Lichtman JW Induction, assembly, maturation and maintenance of a postsynaptic apparatus Nat Rev Neurosci 2001 2 11 791-805 10.1038/ 35097557 11715056
    • (2001) Nat Rev Neurosci , vol.2 , Issue.11 , pp. 791-805
    • Sanes, J.R.1    Lichtman, J.W.2
  • 2
    • 0033764559 scopus 로고    scopus 로고
    • Synapse elimination and indelible memory
    • 10.1016/S0896-6273(00)80893-4 10719884
    • Lichtman JW Colman H Synapse elimination and indelible memory Neuron 2000 25 2 269-278 10.1016/S0896-6273(00)80893-4 10719884
    • (2000) Neuron , vol.25 , Issue.2 , pp. 269-278
    • Lichtman, J.W.1    Colman, H.2
  • 3
    • 33748935769 scopus 로고    scopus 로고
    • Development of the neuromuscular junction
    • 10.1007/s00441-006-0237-x 16819627
    • Witzemann V Development of the neuromuscular junction Cell Tissue Res 2006 326 2 263-271 10.1007/s00441-006-0237-x 16819627
    • (2006) Cell Tissue Res , vol.326 , Issue.2 , pp. 263-271
    • Witzemann, V.1
  • 4
    • 30444439534 scopus 로고    scopus 로고
    • The synaptic muscle-specific kinase (MuSK) complex: New partners, new functions
    • 10.1002/bies.20305 16237673
    • Strochlic L Cartaud A Cartaud J The synaptic muscle-specific kinase (MuSK) complex: New partners, new functions Bioessays 2005 27 11 1129-1135 10.1002/bies.20305 16237673
    • (2005) Bioessays , vol.27 , Issue.11 , pp. 1129-1135
    • Strochlic, L.1    Cartaud, A.2    Cartaud, J.3
  • 6
    • 34447645593 scopus 로고    scopus 로고
    • Assembly of the postsynaptic membrane at the neuromuscular junction: Paradigm lost
    • 16386415
    • Kummer TT Misgeld T Sanes JR Assembly of the postsynaptic membrane at the neuromuscular junction: Paradigm lost Curr Opin Neurobiol 2005 16386415
    • (2005) Curr Opin Neurobiol
    • Kummer, T.T.1    Misgeld, T.2    Sanes, J.R.3
  • 7
    • 4444334503 scopus 로고    scopus 로고
    • A single pulse of agrin triggers a pathway that acts to cluster acetylcholine receptors
    • 515067 15340048 10.1128/MCB.24.18.7841-7854.2004
    • Mittaud P Camilleri AA Willmann R Erb-Vogtli S Burden SJ Fuhrer C A single pulse of agrin triggers a pathway that acts to cluster acetylcholine receptors Mol Cell Biol 2004 24 18 7841-7854 515067 15340048 10.1128/MCB.24.18.7841-7854.2004
    • (2004) Mol Cell Biol , vol.24 , Issue.18 , pp. 7841-7854
    • Mittaud, P.1    Camilleri, A.A.2    Willmann, R.3    Erb-Vogtli, S.4    Burden, S.J.5    Fuhrer, C.6
  • 8
    • 1642487117 scopus 로고    scopus 로고
    • Inhibition of synapse assembly in mammalian muscle in vivo by RNA interference
    • 1298976 14749715 10.1038/sj.embor.7400065
    • Kong XC Barzaghi P Ruegg MA Inhibition of synapse assembly in mammalian muscle in vivo by RNA interference EMBO Rep 2004 5 2 183-188 1298976 14749715 10.1038/sj.embor.7400065
    • (2004) EMBO Rep , vol.5 , Issue.2 , pp. 183-188
    • Kong, X.C.1    Barzaghi, P.2    Ruegg, M.A.3
  • 9
    • 0036176468 scopus 로고    scopus 로고
    • Clustering of nicotinic acetylcholine receptors: From the neuromuscular junction to interneuronal synapses
    • 10.1385/MN:25:1:079 11890459
    • Huh KH Fuhrer C Clustering of nicotinic acetylcholine receptors: From the neuromuscular junction to interneuronal synapses Mol Neurobiol 2002 25 1 79-112 10.1385/MN:25:1:079 11890459
    • (2002) Mol Neurobiol , vol.25 , Issue.1 , pp. 79-112
    • Huh, K.H.1    Fuhrer, C.2
  • 10
    • 0036693564 scopus 로고    scopus 로고
    • Neuromuscular synaptogenesis: Clustering of acetylcholine receptors revisited
    • 10.1007/s00018-002-8509-4 12363034
    • Willmann R Fuhrer C Neuromuscular synaptogenesis: Clustering of acetylcholine receptors revisited Cell Mol Life Sci 2002 59 8 1296-1316 10.1007/s00018-002-8509-4 12363034
    • (2002) Cell Mol Life Sci , vol.59 , Issue.8 , pp. 1296-1316
    • Willmann, R.1    Fuhrer, C.2
  • 11
    • 27744607526 scopus 로고    scopus 로고
    • Src-family kinases stabilize the neuromuscular synapse in vivo via protein interactions, phosphorylation, and cytoskeletal linkage of acetylcholine receptors
    • 10.1523/JNEUROSCI.2103-05.2005 16280586
    • Sadasivam G Willmann R Lin S Erb-Vogtli S Kong XC Ruegg MA Fuhrer C Src-family kinases stabilize the neuromuscular synapse in vivo via protein interactions, phosphorylation, and cytoskeletal linkage of acetylcholine receptors J Neurosci 2005 25 45 10479-10493 10.1523/ JNEUROSCI.2103-05.2005 16280586
    • (2005) J Neurosci , vol.25 , Issue.45 , pp. 10479-10493
    • Sadasivam, G.1    Willmann, R.2    Lin, S.3    Erb-Vogtli, S.4    Kong, X.C.5    Ruegg, M.A.6    Fuhrer, C.7
  • 12
    • 0037182593 scopus 로고    scopus 로고
    • Laminin-1 redistributes postsynaptic proteins and requires rapsyn, tyrosine phosphorylation, and Src and Fyn to stably cluster acetylcholine receptors
    • 10.1083/jcb.200202110 12034776
    • Marangi PA Wieland ST Fuhrer C Laminin-1 redistributes postsynaptic proteins and requires rapsyn, tyrosine phosphorylation, and Src and Fyn to stably cluster acetylcholine receptors J Cell Biol 2002 157 5 883-895 10.1083/jcb.200202110 12034776
    • (2002) J Cell Biol , vol.157 , Issue.5 , pp. 883-895
    • Marangi, P.A.1    Wieland, S.T.2    Fuhrer, C.3
  • 13
    • 33845504867 scopus 로고    scopus 로고
    • Regulation of nicotinic acetylcholine receptors by tyrosine kinases in the peripheral and central nervous system: Same players, different roles
    • 10.1007/s00018-006-6081-z 17086381
    • Wiesner A Fuhrer C Regulation of nicotinic acetylcholine receptors by tyrosine kinases in the peripheral and central nervous system: Same players, different roles Cell Mol Life Sci 2006 63 23 2818-2828 10.1007/ s00018-006-6081-z 17086381
    • (2006) Cell Mol Life Sci , vol.63 , Issue.23 , pp. 2818-2828
    • Wiesner, A.1    Fuhrer, C.2
  • 14
    • 0035341457 scopus 로고    scopus 로고
    • Src, Fyn, and Yes are not required for neuromuscular synapse formation but are necessary for stabilization of agrin-induced clusters of acetylcholine receptors
    • 11312300
    • Smith CL Mittaud P Prescott ED Fuhrer C Burden SJ Src, Fyn, and Yes are not required for neuromuscular synapse formation but are necessary for stabilization of agrin-induced clusters of acetylcholine receptors J Neurosci 2001 21 9 3151-3160 11312300
    • (2001) J Neurosci , vol.21 , Issue.9 , pp. 3151-3160
    • Smith, C.L.1    Mittaud, P.2    Prescott, E.D.3    Fuhrer, C.4    Burden, S.J.5
  • 15
    • 0033757623 scopus 로고    scopus 로고
    • Maturation and maintenance of the neuromuscular synapse: Genetic evidence for roles of the dystrophin - Glycoprotein complex
    • 10.1016/S0896-6273(00)80894-6 10719885
    • Grady RM Zhou H Cunningham JM Henry MD Campbell KP Sanes JR Maturation and maintenance of the neuromuscular synapse: Genetic evidence for roles of the dystrophin - glycoprotein complex Neuron 2000 25 2 279-293 10.1016/S0896-6273(00)80894-6 10719885
    • (2000) Neuron , vol.25 , Issue.2 , pp. 279-293
    • Grady, R.M.1    Zhou, H.2    Cunningham, J.M.3    Henry, M.D.4    Campbell, K.P.5    Sanes, J.R.6
  • 16
    • 0035809195 scopus 로고    scopus 로고
    • The dystroglycan complex is necessary for stabilization of acetylcholine receptor clusters at neuromuscular junctions and formation of the synaptic basement membrane
    • 10.1083/jcb.152.3.435 11157973
    • Jacobson C Cote PD Rossi SG Rotundo RL Carbonetto S The dystroglycan complex is necessary for stabilization of acetylcholine receptor clusters at neuromuscular junctions and formation of the synaptic basement membrane J Cell Biol 2001 152 3 435-450 10.1083/jcb.152.3.435 11157973
    • (2001) J Cell Biol , vol.152 , Issue.3 , pp. 435-450
    • Jacobson, C.1    Cote, P.D.2    Rossi, S.G.3    Rotundo, R.L.4    Carbonetto, S.5
  • 17
    • 0035957950 scopus 로고    scopus 로고
    • Agrin-induced activation of acetylcholine receptor-bound Src family kinases requires Rapsyn and correlates with acetylcholine receptor clustering
    • 11278328
    • Mittaud P Marangi PA Erb-Vogtli S Fuhrer C Agrin-induced activation of acetylcholine receptor-bound Src family kinases requires Rapsyn and correlates with acetylcholine receptor clustering J Biol Chem 2001 276 17 14505-14513 11278328
    • (2001) J Biol Chem , vol.276 , Issue.17 , pp. 14505-14513
    • Mittaud, P.1    Marangi, P.A.2    Erb-Vogtli, S.3    Fuhrer, C.4
  • 18
    • 0029773535 scopus 로고    scopus 로고
    • Functional interaction of Src family kinases with the acetylcholine receptor in C2 myotubes
    • 10.1074/jbc.271.50.32474 8943314
    • Fuhrer C Hall ZW Functional interaction of Src family kinases with the acetylcholine receptor in C2 myotubes J Biol Chem 1996 271 50 32474-32481 10.1074/jbc.271.50.32474 8943314
    • (1996) J Biol Chem , vol.271 , Issue.50 , pp. 32474-32481
    • Fuhrer, C.1    Hall, Z.W.2
  • 19
    • 0027363678 scopus 로고
    • Molecular cloning of two abundant protein tyrosine kinases in Torpedo electric organ that associate with the acetylcholine receptor
    • 8227079
    • Swope SL Huganir RL Molecular cloning of two abundant protein tyrosine kinases in Torpedo electric organ that associate with the acetylcholine receptor J Biol Chem 1993 268 33 25152-25161 8227079
    • (1993) J Biol Chem , vol.268 , Issue.33 , pp. 25152-25161
    • Swope, S.L.1    Huganir, R.L.2
  • 20
    • 33748365435 scopus 로고    scopus 로고
    • Cholesterol and lipid microdomains stabilize the postsynapse at the neuromuscular junction
    • 10.1038/sj.emboj.7601288 16932745
    • Willmann R Pun S Stallmach L Sadasivam G Santos AF Caroni P Fuhrer C Cholesterol and lipid microdomains stabilize the postsynapse at the neuromuscular junction Embo J 2006 25 17 4050-4060 10.1038/ sj.emboj.7601288 16932745
    • (2006) Embo J , vol.25 , Issue.17 , pp. 4050-4060
    • Willmann, R.1    Pun, S.2    Stallmach, L.3    Sadasivam, G.4    Santos, A.F.5    Caroni, P.6    Fuhrer, C.7
  • 21
    • 0033232527 scopus 로고    scopus 로고
    • Regulation of neuregulin-mediated acetylcholine receptor synthesis by protein tyrosine phosphatase SHP2
    • 10531446
    • Tanowitz M Si J Yu DH Feng GS Mei L Regulation of neuregulin-mediated acetylcholine receptor synthesis by protein tyrosine phosphatase SHP2 J Neurosci 1999 19 21 9426-9435 10531446
    • (1999) J Neurosci , vol.19 , Issue.21 , pp. 9426-9435
    • Tanowitz, M.1    Si, J.2    Yu, D.H.3    Feng, G.S.4    Mei, L.5
  • 22
    • 14644414214 scopus 로고    scopus 로고
    • Tyrosine phosphatase regulation of MuSK-dependent acetylcholine receptor clustering
    • 10.1016/j.mcn.2004.10.005 15737732
    • Madhavan R Zhao XT Ruegg MA Peng HB Tyrosine phosphatase regulation of MuSK-dependent acetylcholine receptor clustering Mol Cell Neurosci 2005 28 3 403-416 10.1016/j.mcn.2004.10.005 15737732
    • (2005) Mol Cell Neurosci , vol.28 , Issue.3 , pp. 403-416
    • Madhavan, R.1    Zhao, X.T.2    Ruegg, M.A.3    Peng, H.B.4
  • 23
    • 0028956758 scopus 로고
    • Regulation of the interaction of nicotinic acetylcholine receptors with the cytoskeleton by agrin-activated protein tyrosine kinase
    • 10.1083/jcb.128.6.1121 7896876
    • Wallace BG Regulation of the interaction of nicotinic acetylcholine receptors with the cytoskeleton by agrin-activated protein tyrosine kinase J Cell Biol 1995 128 6 1121-1129 10.1083/jcb.128.6.1121 7896876
    • (1995) J Cell Biol , vol.128 , Issue.6 , pp. 1121-1129
    • Wallace, B.G.1
  • 24
    • 0026806366 scopus 로고
    • Activation of signal transduction in platelets by the tyrosine phosphatase inhibitor pervanadate (vanadyl hydroperoxide)
    • 1132918 1530576
    • Pumiglia KM Lau LF Huang CK Burroughs S Feinstein MB Activation of signal transduction in platelets by the tyrosine phosphatase inhibitor pervanadate (vanadyl hydroperoxide) Biochem J 1992 286 (Pt 2) 441-449 1132918 1530576
    • (1992) Biochem J , vol.286 , Issue.PART 2 , pp. 441-449
    • Pumiglia, K.M.1    Lau, L.F.2    Huang, C.K.3    Burroughs, S.4    Feinstein, M.B.5
  • 25
    • 0030029143 scopus 로고    scopus 로고
    • Discovery of a novel, potent, and Src family-selective tyrosine kinase inhibitor. Study of Lck- and FynT-dependent T cell activation
    • 10.1074/jbc.271.2.695 8557675
    • Hanke JH Gardner JP Dow RL Changelian PS Brissette WH Weringer EJ Pollok BA Connelly PA Discovery of a novel, potent, and Src family-selective tyrosine kinase inhibitor. Study of Lck- and FynT-dependent T cell activation J Biol Chem 1996 271 2 695-701 10.1074/jbc.271.2.695 8557675
    • (1996) J Biol Chem , vol.271 , Issue.2 , pp. 695-701
    • Hanke, J.H.1    Gardner, J.P.2    Dow, R.L.3    Changelian, P.S.4    Brissette, W.H.5    Weringer, E.J.6    Pollok, B.A.7    Connelly, P.A.8
  • 27
    • 2942589265 scopus 로고    scopus 로고
    • SHP-2 positively regulates myogenesis by coupling to the Rho GTPase signaling pathway
    • 419889 15169898 10.1128/MCB.24.12.5340-5352.2004
    • Kontaridis MI Eminaga S Fornaro M Zito CI Sordella R Settleman J Bennett AM SHP-2 positively regulates myogenesis by coupling to the Rho GTPase signaling pathway Mol Cell Biol 2004 24 12 5340-5352 419889 15169898 10.1128/MCB.24.12.5340-5352.2004
    • (2004) Mol Cell Biol , vol.24 , Issue.12 , pp. 5340-5352
    • Kontaridis, M.I.1    Eminaga, S.2    Fornaro, M.3    Zito, C.I.4    Sordella, R.5    Settleman, J.6    Bennett, A.M.7
  • 28
    • 3042545272 scopus 로고    scopus 로고
    • Conditional gene silencing utilizing the lac repressor reveals a role of SHP-2 in cagA-positive Helicobacter pylori pathogenicity
    • 10.1111/j.1349-7006.2004.tb03229.x 15132773
    • Higuchi M Tsutsumi R Higashi H Hatakeyama M Conditional gene silencing utilizing the lac repressor reveals a role of SHP-2 in cagA-positive Helicobacter pylori pathogenicity Cancer Sci 2004 95 5 442-447 10.1111/ j.1349-7006.2004.tb03229.x 15132773
    • (2004) Cancer Sci , vol.95 , Issue.5 , pp. 442-447
    • Higuchi, M.1    Tsutsumi, R.2    Higashi, H.3    Hatakeyama, M.4
  • 29
    • 0029928633 scopus 로고    scopus 로고
    • Agrin-induced acetylcholine receptor clustering in mammalian muscle requires tyrosine phosphorylation
    • 10.1083/jcb.132.5.937 8603924
    • Ferns M Deiner M Hall Z Agrin-induced acetylcholine receptor clustering in mammalian muscle requires tyrosine phosphorylation J Cell Biol 1996 132 5 937-944 10.1083/jcb.132.5.937 8603924
    • (1996) J Cell Biol , vol.132 , Issue.5 , pp. 937-944
    • Ferns, M.1    Deiner, M.2    Hall, Z.3
  • 30
    • 13544270759 scopus 로고    scopus 로고
    • DOK1 mediates SHP-2 binding to the alphaVbeta3 integrin and thereby regulates insulin-like growth factor I signaling in cultured vascular smooth muscle cells
    • 10.1074/jbc.M411035200 15546884
    • Ling Y Maile LA Badley-Clarke J Clemmons DR DOK1 mediates SHP-2 binding to the alphaVbeta3 integrin and thereby regulates insulin-like growth factor I signaling in cultured vascular smooth muscle cells J Biol Chem 2005 280 5 3151-3158 10.1074/jbc.M411035200 15546884
    • (2005) J Biol Chem , vol.280 , Issue.5 , pp. 3151-3158
    • Ling, Y.1    Maile, L.A.2    Badley-Clarke, J.3    Clemmons, D.R.4
  • 31
    • 0042334863 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the beta3-subunit of the alphaVbeta3 integrin is required for embrane association of the tyrosine phosphatase SHP-2 and its further recruitment to the insulin-like growth factor I receptor
    • 10.1210/me.2003-0143 12791772
    • Ling Y Maile LA Clemmons DR Tyrosine phosphorylation of the beta3-subunit of the alphaVbeta3 integrin is required for embrane association of the tyrosine phosphatase SHP-2 and its further recruitment to the insulin-like growth factor I receptor Mol Endocrinol 2003 17 9 1824-833 10.1210/me.2003-0143 12791772
    • (2003) Mol Endocrinol , vol.17 , Issue.9 , pp. 1824-1833
    • Ling, Y.1    Maile, L.A.2    Clemmons, D.R.3
  • 32
    • 0028342948 scopus 로고
    • SH-PTP2/Syp SH2 domain binding specificity is defined by direct interactions with platelet-derived growth factor beta-receptor, epidermal growth factor receptor, and insulin receptor substrate-1- derived phosphopeptides
    • 8144631
    • Case RD Piccione E Wolf G Benett AM Lechleider RJ Neel BG Shoelson SE SH-PTP2/Syp SH2 domain binding specificity is defined by direct interactions with platelet-derived growth factor beta-receptor, epidermal growth factor receptor, and insulin receptor substrate-1- derived phosphopeptides J Biol Chem 1994 269 14 10467-10474 8144631
    • (1994) J Biol Chem , vol.269 , Issue.14 , pp. 10467-10474
    • Case, R.D.1    Piccione, E.2    Wolf, G.3    Benett, A.M.4    Lechleider, R.J.5    Neel, B.G.6    Shoelson, S.E.7
  • 33
    • 0033604644 scopus 로고    scopus 로고
    • Shp-2 tyrosine phosphatase: Signaling one cell or many
    • 10.1006/excr.1999.4668 10579910
    • Feng GS Shp-2 tyrosine phosphatase: Signaling one cell or many Exp Cell Res 1999 253 1 47-54 10.1006/excr.1999.4668 10579910
    • (1999) Exp Cell Res , vol.253 , Issue.1 , pp. 47-54
    • Feng, G.S.1
  • 34
    • 0032548830 scopus 로고    scopus 로고
    • Crystal structure of the tyrosine phosphatase SHP-2
    • 10.1016/S0092-8674(00)80938-1 9491886
    • Hof P Pluskey S Dhe-Paganon S Eck MJ Shoelson SE Crystal structure of the tyrosine phosphatase SHP-2 Cell 1998 92 4 441-450 10.1016/ S0092-8674(00)80938-1 9491886
    • (1998) Cell , vol.92 , Issue.4 , pp. 441-450
    • Hof, P.1    Pluskey, S.2    Dhe-Paganon, S.3    Eck, M.J.4    Shoelson, S.E.5
  • 35
    • 0033580431 scopus 로고    scopus 로고
    • The Shp-2 tyrosine phosphatase activates the Src tyrosine kinase by a non-enzymatic mechanism
    • 10.1038/sj.onc.1202513 10208413
    • Walter AO Peng ZY Cartwright CA The Shp-2 tyrosine phosphatase activates the Src tyrosine kinase by a non-enzymatic mechanism Oncogene 1999 18 11 1911-1920 10.1038/sj.onc.1202513 10208413
    • (1999) Oncogene , vol.18 , Issue.11 , pp. 1911-1920
    • Walter, A.O.1    Peng, Z.Y.2    Cartwright, C.A.3
  • 36
    • 0028837693 scopus 로고
    • Regulation of the Src tyrosine kinase and Syp tyrosine phosphatase by their cellular association
    • 7478513
    • Peng ZY Cartwright CA Regulation of the Src tyrosine kinase and Syp tyrosine phosphatase by their cellular association Oncogene 1995 11 10 1955-1962 7478513
    • (1995) Oncogene , vol.11 , Issue.10 , pp. 1955-1962
    • Peng, Z.Y.1    Cartwright, C.A.2
  • 37
    • 0028885901 scopus 로고
    • Tyrosine phosphorylation and synapse formation at the neuromuscular junction
    • 10.1016/0024-3205(95)02118-3 7564890
    • Mei L Si J Tyrosine phosphorylation and synapse formation at the neuromuscular junction Life Sci 1995 57 16 1459-1466 10.1016/ 0024-3205(95)02118-3 7564890
    • (1995) Life Sci , vol.57 , Issue.16 , pp. 1459-1466
    • Mei, L.1    Si, J.2
  • 38
    • 0028972120 scopus 로고
    • Immobilization of nicotinic acetylcholine receptors in mouse C2 myotubes by agrin-induced protein tyrosine phosphorylation
    • 10.1083/jcb.131.2.441 7593170
    • Meier T Perez GM Wallace BG Immobilization of nicotinic acetylcholine receptors in mouse C2 myotubes by agrin-induced protein tyrosine phosphorylation J Cell Biol 1995 131 2 441-451 10.1083/jcb.131.2.441 7593170
    • (1995) J Cell Biol , vol.131 , Issue.2 , pp. 441-451
    • Meier, T.1    Perez, G.M.2    Wallace, B.G.3
  • 39
    • 0029153801 scopus 로고
    • c-Src regulates the simultaneous rearrangement of actin cytoskeleton, p190RhoGAP, and p120RasGAP following epidermal growth factor stimulation
    • 10.1083/jcb.130.2.355 7542246
    • Chang JH Gill S Settleman J Parsons SJ c-Src regulates the simultaneous rearrangement of actin cytoskeleton, p190RhoGAP, and p120RasGAP following epidermal growth factor stimulation J Cell Biol 1995 130 2 355-368 10.1083/jcb.130.2.355 7542246
    • (1995) J Cell Biol , vol.130 , Issue.2 , pp. 355-368
    • Chang, J.H.1    Gill, S.2    Settleman, J.3    Parsons, S.J.4
  • 40
    • 0034496280 scopus 로고    scopus 로고
    • Association of cortactin with dynamic actin in lamellipodia and on endosomal vesicles
    • 11082035
    • Kaksonen M Peng HB Rauvala H Association of cortactin with dynamic actin in lamellipodia and on endosomal vesicles J Cell Sci 2000 113 Pt 24 4421-4426 11082035
    • (2000) J Cell Sci , vol.113 , Issue.PART 24 , pp. 4421-4426
    • Kaksonen, M.1    Peng, H.B.2    Rauvala, H.3
  • 41
    • 0034631836 scopus 로고    scopus 로고
    • Agrin-induced acetylcholine receptor clustering is mediated by the small guanosine triphosphatases Rac and Cdc42
    • 10.1083/jcb.150.1.205 10893268
    • Weston C Yee B Hod E Prives J Agrin-induced acetylcholine receptor clustering is mediated by the small guanosine triphosphatases Rac and Cdc42 J Cell Biol 2000 150 1 205-212 10.1083/jcb.150.1.205 10893268
    • (2000) J Cell Biol , vol.150 , Issue.1 , pp. 205-212
    • Weston, C.1    Yee, B.2    Hod, E.3    Prives, J.4
  • 42
    • 0037458558 scopus 로고    scopus 로고
    • Cooperative regulation by Rac and Rho of agrin-induced acetylcholine receptor clustering in muscle cells
    • 10.1074/jbc.M210249200
    • Weston C Gordon C Teressa G Hod E Ren XD Prives J Cooperative regulation by Rac and Rho of agrin-induced acetylcholine receptor clustering in muscle cells J Biol Chem 2003 278 8 6450-6455 10.1074/jbc.M210249200 12473646
    • (2003) J Biol Chem , vol.278 , Issue.8 , pp. 6450-6455
    • Weston, C.1    Gordon, C.2    Teressa, G.3    Hod, E.4    Ren, X.D.5    Prives, J.6
  • 43
    • 0034683659 scopus 로고    scopus 로고
    • The actin-driven movement and formation of acetylcholine receptor clusters
    • 10.1083/jcb.150.6.1321 10995438
    • Dai Z Luo X Xie H Peng HB The actin-driven movement and formation of acetylcholine receptor clusters J Cell Biol 2000 150 6 1321-1334 10.1083/ jcb.150.6.1321 10995438
    • (2000) J Cell Biol , vol.150 , Issue.6 , pp. 1321-1334
    • Dai, Z.1    Luo, X.2    Xie, H.3    Peng, H.B.4
  • 44
    • 33747464356 scopus 로고    scopus 로고
    • Shp2 is dispensable in the formation and maintenance of the neuromuscular junction
    • 10.1159/000094484 16837792
    • Dong XP Li XM Gao TM Zhang EE Feng GS Xiong WC Mei L Shp2 is dispensable in the formation and maintenance of the neuromuscular junction Neurosignals 2006 15 2 53-63 10.1159/000094484 16837792
    • (2006) Neurosignals , vol.15 , Issue.2 , pp. 53-63
    • Dong, X.P.1    Li, X.M.2    Gao, T.M.3    Zhang, E.E.4    Feng, G.S.5    Xiong, W.C.6    Mei, L.7
  • 45
    • 33645649090 scopus 로고    scopus 로고
    • Tyrosine phosphatases regulate AMPA receptor trafficking during metabotropic glutamate receptor-mediated long-term depression
    • 10.1523/JNEUROSCI.4322-05.2006 16510732
    • Moult PR Gladding CM Sanderson TM Fitzjohn SM Bashir ZI Molnar E Collingridge GL Tyrosine phosphatases regulate AMPA receptor trafficking during metabotropic glutamate receptor-mediated long-term depression J Neurosci 2006 26 9 2544-2554 10.1523/JNEUROSCI.4322-05.2006 16510732
    • (2006) J Neurosci , vol.26 , Issue.9 , pp. 2544-2554
    • Moult, P.R.1    Gladding, C.M.2    Sanderson, T.M.3    Fitzjohn, S.M.4    Bashir, Z.I.5    Molnar, E.6    Collingridge, G.L.7
  • 46
    • 23844534710 scopus 로고    scopus 로고
    • The two isoforms of the Caenorhabditis elegans leukocyte-common antigen related receptor tyrosine phosphatase PTP-3 function independently in axon guidance and synapse formation
    • 10.1523/JNEUROSCI.2010-05.2005 16107639
    • Ackley BD Harrington RJ Hudson ML Williams L Kenyon CJ Chisholm AD Jin Y The two isoforms of the Caenorhabditis elegans leukocyte-common antigen related receptor tyrosine phosphatase PTP-3 function independently in axon guidance and synapse formation J Neurosci 2005 25 33 7517-7528 10.1523/JNEUROSCI.2010-05.2005 16107639
    • (2005) J Neurosci , vol.25 , Issue.33 , pp. 7517-7528
    • Ackley, B.D.1    Harrington, R.J.2    Hudson, M.L.3    Williams, L.4    Kenyon, C.J.5    Chisholm, A.D.6    Jin, Y.7
  • 47
    • 0037187643 scopus 로고    scopus 로고
    • Drosophila liprin-alpha and the receptor phosphatase Dlar control synapse morphogenesis
    • 10.1016/S0896-6273(02)00643-8 11931739
    • Kaufmann N DeProto J Ranjan R Wan H Van Vactor D Drosophila liprin-alpha and the receptor phosphatase Dlar control synapse morphogenesis Neuron 2002 34 1 27-38 10.1016/S0896-6273(02)00643-8 11931739
    • (2002) Neuron , vol.34 , Issue.1 , pp. 27-38
    • Kaufmann, N.1    DeProto, J.2    Ranjan, R.3    Wan, H.4    Van Vactor, D.5
  • 49
    • 0027517961 scopus 로고
    • The ability of agrin to cluster AChRs depends on alternative splicing and on cell surface proteoglycans
    • 10.1016/0896-6273(93)90153-I 8398142
    • Ferns MJ Campanelli JT Hoch W Scheller RH Hall Z The ability of agrin to cluster AChRs depends on alternative splicing and on cell surface proteoglycans Neuron 1993 11 3 491-502 10.1016/0896-6273(93)90153-I 8398142
    • (1993) Neuron , vol.11 , Issue.3 , pp. 491-502
    • Ferns, M.J.1    Campanelli, J.T.2    Hoch, W.3    Scheller, R.H.4    Hall, Z.5
  • 50
    • 0030789733 scopus 로고    scopus 로고
    • Association of muscle-specific kinase MuSK with the acetylcholine receptor in mammalian muscle
    • 1170130 9305637 10.1093/emboj/16.16.4951
    • Fuhrer C Sugiyama JE Taylor RG Hall ZW Association of muscle-specific kinase MuSK with the acetylcholine receptor in mammalian muscle Embo J 1997 16 16 4951-4960 1170130 9305637 10.1093/emboj/16.16.4951
    • (1997) Embo J , vol.16 , Issue.16 , pp. 4951-4960
    • Fuhrer, C.1    Sugiyama, J.E.2    Taylor, R.G.3    Hall, Z.W.4
  • 51
    • 0029958839 scopus 로고    scopus 로고
    • Alternative splicing of agrin alters its binding to heparin, dystroglycan, and the putative agrin receptor
    • 10.1016/S0896-6273(00)80096-3 8607994
    • Gesemann M Cavalli V Denzer AJ Brancaccio A Schumacher B Ruegg MA Alternative splicing of agrin alters its binding to heparin, dystroglycan, and the putative agrin receptor Neuron 1996 16 4 755-767 10.1016/S0896-6273(00)80096-3 8607994
    • (1996) Neuron , vol.16 , Issue.4 , pp. 755-767
    • Gesemann, M.1    Cavalli, V.2    Denzer, A.J.3    Brancaccio, A.4    Schumacher, B.5    Ruegg, M.A.6
  • 52
    • 0027941192 scopus 로고
    • Dystroglycan binds nerve and muscle agrin
    • 10.1016/0896-6273(94)90462-6 8043271
    • Sugiyama J Bowen DC Hall ZW Dystroglycan binds nerve and muscle agrin Neuron 1994 13 1 103-115 10.1016/0896-6273(94)90462-6 8043271
    • (1994) Neuron , vol.13 , Issue.1 , pp. 103-115
    • Sugiyama, J.1    Bowen, D.C.2    Hall, Z.W.3
  • 53
    • 0242569304 scopus 로고    scopus 로고
    • Calcium-dependent maintenance of agrin-induced postsynaptic specializations
    • 10.1016/S0306-4522(03)00602-X 14622909
    • Megeath LJ Kirber MT Hopf C Hoch W Fallon JR Calcium-dependent maintenance of agrin-induced postsynaptic specializations Neuroscience 2003 122 3 659-668 10.1016/S0306-4522(03)00602-X 14622909
    • (2003) Neuroscience , vol.122 , Issue.3 , pp. 659-668
    • Megeath, L.J.1    Kirber, M.T.2    Hopf, C.3    Hoch, W.4    Fallon, J.R.5
  • 54
    • 27344437870 scopus 로고    scopus 로고
    • Alpha7 neuronal nicotinic acetylcholine receptors are negatively regulated by tyrosine phosphorylation and Src-family kinases
    • 10.1523/JNEUROSCI.3497-05.2005 16251431
    • Charpantier E Wiesner A Huh KH Ogier R Hoda JC Allaman G Raggenbass M Feuerbach D Bertrand D Fuhrer C Alpha7 neuronal nicotinic acetylcholine receptors are negatively regulated by tyrosine phosphorylation and Src-family kinases J Neurosci 2005 25 43 9836-9849 10.1523/ JNEUROSCI.3497-05.2005 16251431
    • (2005) J Neurosci , vol.25 , Issue.43 , pp. 9836-9849
    • Charpantier, E.1    Wiesner, A.2    Huh, K.H.3    Ogier, R.4    Hoda, J.C.5    Allaman, G.6    Raggenbass, M.7    Feuerbach, D.8    Bertrand, D.9    Fuhrer, C.10
  • 55
    • 0037126630 scopus 로고    scopus 로고
    • Acetylcholine receptors are required for agrin-induced clustering of postsynaptic proteins
    • 125801 11742983 10.1093/emboj/20.24.7060
    • Marangi PA Forsayeth JR Mittaud P Erb-Vogtli S Blake DJ Moransard M Sander A Fuhrer C Acetylcholine receptors are required for agrin-induced clustering of postsynaptic proteins Embo J 2001 20 24 7060-7073 125801 11742983 10.1093/emboj/20.24.7060
    • (2001) Embo J , vol.20 , Issue.24 , pp. 7060-7073
    • Marangi, P.A.1    Forsayeth, J.R.2    Mittaud, P.3    Erb-Vogtli, S.4    Blake, D.J.5    Moransard, M.6    Sander, A.7    Fuhrer, C.8
  • 56
    • 0037470047 scopus 로고    scopus 로고
    • Agrin regulates rapsyn interaction with surface acetylcholine receptors, and this underlies cytoskeletal anchoring and clustering
    • 10.1074/jbc.M210865200 12486121
    • Moransard M Borges LS Willmann R Marangi PA Brenner HR Ferns MJ Fuhrer C Agrin regulates rapsyn interaction with surface acetylcholine receptors, and this underlies cytoskeletal anchoring and clustering J Biol Chem 2003 278 9 7350-7359 10.1074/jbc.M210865200 12486121
    • (2003) J Biol Chem , vol.278 , Issue.9 , pp. 7350-7359
    • Moransard, M.1    Borges, L.S.2    Willmann, R.3    Marangi, P.A.4    Brenner, H.R.5    Ferns, M.J.6    Fuhrer, C.7
  • 57
    • 0033135386 scopus 로고    scopus 로고
    • Constitutively active MuSK is clustered in the absence of agrin and induces ectopic postsynaptic-like membranes in skeletal muscle fibers
    • 10212297
    • Jones G Moore C Hashemolhosseini S Brenner HR Constitutively active MuSK is clustered in the absence of agrin and induces ectopic postsynaptic-like membranes in skeletal muscle fibers J Neurosci 1999 19 9 3376-3383 10212297
    • (1999) J Neurosci , vol.19 , Issue.9 , pp. 3376-3383
    • Jones, G.1    Moore, C.2    Hashemolhosseini, S.3    Brenner, H.R.4
  • 58
    • 0036932947 scopus 로고    scopus 로고
    • SHP-2 mediates target-regulated axonal termination and NGF-dependent neurite growth in sympathetic neurons
    • 10.1006/dbio.2002.0847 12482708
    • Chen B Hammonds-Odie L Perron J Masters BA Bixby JL SHP-2 mediates target-regulated axonal termination and NGF-dependent neurite growth in sympathetic neurons Dev Biol 2002 252 2 170-187 10.1006/dbio.2002.0847 12482708
    • (2002) Dev Biol , vol.252 , Issue.2 , pp. 170-187
    • Chen, B.1    Hammonds-Odie, L.2    Perron, J.3    Masters, B.A.4    Bixby, J.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.