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Volumn 30, Issue 24, 2011, Pages 4955-4969

Proper synaptic vesicle formation and neuronal network activity critically rely on syndapin i

(23)  Koch, Dennis a   Spiwoks Becker, Isabella b   Sabanov, Victor c   Sinning, Anne a   Dugladze, Tamar d   Stellmacher, Anne a   Ahuja, Rashmi a   Grimm, Julia a   Schüler, Susann a   Müller, Anke a   Angenstein, Frank e   Ahmed, Tariq c   Diesler, Alexander b   Moser, Markus f   Tom Dieck, Susanne g   Spessert, Rainer b   Boeckers, Tobias Maria h   Fässler, Reinhard f   Hübner, Christian Andreas a   Balschun, Detlef c   more..


Author keywords

F BAR protein syndapin PACSIN; membrane recruitment of dynamins; rod photoreceptor ribbon synapses; seizures with tonic clonic convulsions; SV formation and recycling

Indexed keywords

ACTIN; AMPHIPHYSIN I; CLATHRIN; CORTACTIN; DYNAMIN; DYNAMIN I; DYNAMIN II; DYNAMIN III; ENDOPHILIN I; GEPHYRIN; ISOPROTEIN; MEMBRANE PROTEIN; MUTANT PROTEIN; POSTSYNAPTIC DENSITY PROTEIN 95; PROTEIN ABP1; PROTEIN AP180; PROTEIN AP2; SOS PROTEIN; SYNAPTOJANIN I; SYNAPTOPHYSIN I; SYNDAPIN I; SYNDAPIN II; SYNDAPIN III; TUBULIN; UNCLASSIFIED DRUG;

EID: 83555176116     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2011.339     Document Type: Article
Times cited : (72)

References (67)
  • 2
    • 43049170419 scopus 로고    scopus 로고
    • Perturbation of syndapin/PACSIN impairs synaptic vesicle recycling evoked by intense stimulation
    • Andersson F, Jakobsson J, Löw P, Shupliakov O, Brodin L (2008) Perturbation of syndapin/PACSIN impairs synaptic vesicle recycling evoked by intense stimulation. J Neurosci 28: 3925-3933
    • (2008) J Neurosci , vol.28 , pp. 3925-3933
    • Andersson, F.1    Jakobsson, J.2    Löw, P.3    Shupliakov, O.4    Brodin, L.5
  • 5
    • 0024283664 scopus 로고
    • Developments in neuronal cell culture
    • Banker G, Goslin K (1988) Developments in neuronal cell culture. Nature 336: 185-186
    • (1988) Nature , vol.336 , pp. 185-186
    • Banker, G.1    Goslin, K.2
  • 6
    • 0036898560 scopus 로고    scopus 로고
    • A receptor-mediated inhibitory postsynaptic currents in hippocampus
    • Banks MI, Hardie JB, Pearce RA (2002) Development of GABA(A) receptor-mediated inhibitory postsynaptic currents in hippocampus. J Neurophysiol 88: 3097-3107 (Pubitemid 35448694)
    • (2002) Journal of Neurophysiology , vol.88 , Issue.6 , pp. 3097-3107
    • Banks, M.I.1    Hardie, J.B.2    Pearce, R.A.3
  • 9
    • 67449143251 scopus 로고    scopus 로고
    • The phospho-dependent dynamin-syndapin interaction triggers activity-dependent bulk endocytosis of synaptic vesicles
    • Clayton EL, Anggono V, Smillie KJ, Chau N, Robinson PJ, Cousin MA (2009) The phospho-dependent dynamin-syndapin interaction triggers activity-dependent bulk endocytosis of synaptic vesicles. J Neurosci 24: 7706-7717
    • (2009) J Neurosci , vol.24 , pp. 7706-7717
    • Clayton, E.L.1    Anggono, V.2    Smillie, K.J.3    Chau, N.4    Robinson, P.J.5    Cousin, M.A.6
  • 10
    • 48349112292 scopus 로고    scopus 로고
    • Differential labelling of bulk en-docytosis in nerve terminals by FM dyes
    • Clayton EL, Cousin MA (2008) Differential labelling of bulk en-docytosis in nerve terminals by FM dyes. Neurochem Int 53: 51-55
    • (2008) Neurochem Int , vol.53 , pp. 51-55
    • Clayton, E.L.1    Cousin, M.A.2
  • 14
    • 71549146571 scopus 로고    scopus 로고
    • The Arp2/3 activator WASH controls the fission of endo-somes through a large multiprotein complex
    • Derivery E, Sousa C, Gautier JJ, Lombard B, Loew D, Gautreau A (2009) The Arp2/3 activator WASH controls the fission of endo-somes through a large multiprotein complex. Dev Cell 5: 712-723
    • (2009) Dev Cell , vol.5 , pp. 712-723
    • Derivery, E.1    Sousa, C.2    Gautier, J.J.3    Lombard, B.4    Loew, D.5    Gautreau, A.6
  • 15
    • 70350348378 scopus 로고    scopus 로고
    • F-BAR proteins of the syndapin family shape the plasma membrane and are crucial for neuro-morphogenesis
    • Dharmalingam E, Haeckel A, Pinyol R, Schwintzer L, Koch D, Kessels MM, Qualmann B (2009) F-BAR proteins of the syndapin family shape the plasma membrane and are crucial for neuro-morphogenesis. J Neurosci 42: 13315-13327
    • (2009) J Neurosci , vol.42 , pp. 13315-13327
    • Dharmalingam, E.1    Haeckel, A.2    Pinyol, R.3    Schwintzer, L.4    Koch, D.5    Kessels, M.M.6    Qualmann, B.7
  • 19
    • 77951172311 scopus 로고    scopus 로고
    • The Cdc42-interacting protein-4 (CIP4) gene knock-out mouse reveals delayed and decreased endocytosis
    • Feng Y, Hartig SM, Bechill JE, Blanchard EG, Caudell E, Corey SJ (2010) The Cdc42-interacting protein-4 (CIP4) gene knock-out mouse reveals delayed and decreased endocytosis. J Biol Chem 285: 4348-4354
    • (2010) J Biol Chem , vol.285 , pp. 4348-4354
    • Feng, Y.1    Hartig, S.M.2    Bechill, J.E.3    Blanchard, E.G.4    Caudell, E.5    Corey, S.J.6
  • 22
    • 0023812298 scopus 로고
    • A morphometric analysis of synaptic vesicle distributions
    • Fox GQ (1988) A morphometric analysis of synaptic vesicle distributions. Brain Res 475: 103-117
    • (1988) Brain Res , vol.475 , pp. 103-117
    • Fox, G.Q.1
  • 24
    • 40049086567 scopus 로고    scopus 로고
    • Structural basis of membrane in-vagination by F-BAR domains
    • DOI 10.1016/j.cell.2007.12.041, PII S0092867408001311
    • Frost A, Perera R, Roux A, Spasov K, Destaing O, Egelman EH, De Camilli P, Unger VM (2008) Structural basis of membrane in-vagination by F-BAR domains. Cell 5: 807-817 (Pubitemid 351320580)
    • (2008) Cell , vol.132 , Issue.5 , pp. 807-817
    • Frost, A.1    Perera, R.2    Roux, A.3    Spasov, K.4    Destaing, O.5    Egelman, E.H.6    De Camilli, P.7    Unger, V.M.8
  • 25
    • 64249110493 scopus 로고    scopus 로고
    • The BAR domain super-family: Membrane-molding macromolecules
    • Frost A, Unger VM, De Camilli P (2009) The BAR domain super-family: membrane-molding macromolecules. Cell 2: 191-196
    • (2009) Cell , vol.2 , pp. 191-196
    • Frost, A.1    Unger, V.M.2    De Camilli, P.3
  • 27
    • 45849110080 scopus 로고    scopus 로고
    • SNX18 is an SNX9 paralog that acts as a membrane tubulator in AP-1-positive endosomal trafficking
    • DOI 10.1242/jcs.028530
    • Haüberg K, Lundmark R, Carlsson SR (2008) SNX18 is an SNX9 paralog that acts as a membrane tubulator in AP-1-positive endosomal trafficking. J Cell Sci 9: 1495-1505 (Pubitemid 351936314)
    • (2008) Journal of Cell Science , vol.121 , Issue.9 , pp. 1495-1505
    • Haberg, K.1    Lundmark, R.2    Carlsson, S.R.3
  • 28
    • 0028858391 scopus 로고
    • Variation in the number, location, and size of synaptic vesicles provides an anatomical basis for the non-uniform probability of release at hippocampal CA1 synapses
    • Harris KM, Sultan P (1995) Variation in the number, location, and size of synaptic vesicles provides an anatomical basis for the non-uniform probability of release at hippocampal CA1 synapses. Neuropharmacology 34: 1387-1395
    • (1995) Neuropharmacology , vol.34 , pp. 1387-1395
    • Harris, K.M.1    Sultan, P.2
  • 30
    • 34447256592 scopus 로고    scopus 로고
    • Structure and Analysis of FCHo2 F-BAR Domain: A Dimerizing and Membrane Recruitment Module that Effects Membrane Curvature
    • DOI 10.1016/j.str.2007.05.002, PII S0969212607001815
    • Henne WM, Kent HM, Ford MG, Hegde BG, Daumke O, Butler PJ, Mittal R, Langen R, Evans PR, McMahon HT (2007) Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature. Structure 15: 839-852 (Pubitemid 47042426)
    • (2007) Structure , vol.15 , Issue.7 , pp. 839-852
    • Henne, W.M.1    Kent, H.M.2    Ford, M.G.J.3    Hegde, B.G.4    Daumke, O.5    Butler, P.J.G.6    Mittal, R.7    Langen, R.8    Evans, P.R.9    McMahon, H.T.10
  • 31
    • 29244446227 scopus 로고    scopus 로고
    • The regulatory subunit of PDE6 interacts with PACSIN in photoreceptors
    • Houdart F, Girard-Nau N, Morin F, Voisin P, Vannier B (2005) The regulatory subunit of PDE6 interacts with PACSIN in photorecep-tors. Mol Vis 11 : 1061-1070 (Pubitemid 41819507)
    • (2005) Molecular Vision , vol.11 , pp. 1061-1070
    • Houdart, F.1    Girard-Nau, N.2    Morin, F.3    Voisin, P.4    Vannier, B.5
  • 32
    • 28444452974 scopus 로고    scopus 로고
    • Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins
    • DOI 10.1016/j.devcel.2005.11.005, PII S1534580705004284
    • Itoh T, Erdmann KS, Roux A, Habermann B, Werner H, De Camilli P (2005) Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. Dev Cell 9: 791-804 (Pubitemid 41724107)
    • (2005) Developmental Cell , vol.9 , Issue.6 , pp. 791-804
    • Itoh, T.1    Erdmann, K.S.2    Roux, A.3    Habermann, B.4    Werner, H.5    De Camilli, P.6
  • 33
    • 33646710836 scopus 로고    scopus 로고
    • Complexes of syndapin II with dynamin II promote vesicle formation at the trans-Golgi network
    • DOI 10.1242/jcs.02877
    • Kessels MM, Dong J, Leibig W, Westermann P, Qualmann B (2006) Complexes of syndapin II with dynamin II promote vesicle formation at the trans-Golgi network. J Cell Sci 8: 1504-1516 (Pubitemid 43738853)
    • (2006) Journal of Cell Science , vol.119 , Issue.8 , pp. 1504-1516
    • Kessels, M.M.1    Dong, J.2    Leibig, W.3    Westermann, P.4    Qualmann, B.5
  • 34
    • 0033980106 scopus 로고    scopus 로고
    • Association of mouse actin-binding protein 1 (mAbp1/SH3P7), an Src kinase target, with dynamic regions of the cortical actin cytoskeleton in response to Rac1 activation
    • Kessels MM, Engqvist-Goldstein AE, Drubin DG (2000) Association of mouse actin-binding protein 1 (mAbp1/SH3P7), an Src kinase target, with dynamic regions of the cortical actin cytoskeleton in response to Rac1 activation. Mol Biol Cell 11 : 393-412 (Pubitemid 30075530)
    • (2000) Molecular Biology of the Cell , vol.11 , Issue.1 , pp. 393-412
    • Kessels, M.M.1    Engqvist-Goldstein, A.E.Y.2    Drubin, D.G.3
  • 35
    • 0035897420 scopus 로고    scopus 로고
    • Mammalian Abp1, a signal-responsive F-actin-binding protein, links the actin cytoskeleton to endocytosis via the GTPase dynamin
    • Kessels MM, Engqvist-Goldstein AE, Drubin DG, Qualmann B (2001) Mammalian Abp1, a signal-responsive F-actin-binding protein, links the actin cytoskeleton to endocytosis via the GTPase dynamin. J Cell Biol 153: 351-366
    • (2001) J Cell Biol , vol.153 , pp. 351-366
    • Kessels, M.M.1    Engqvist-Goldstein, A.E.2    Drubin, D.G.3    Qualmann, B.4
  • 36
    • 0037112944 scopus 로고    scopus 로고
    • Syndapins integrate N-WASP in receptor-mediated endocytosis
    • DOI 10.1093/emboj/cdf604
    • Kessels MM, Qualmann B (2002) Syndapins integrate N-WASP in receptor-mediated endocytosis. EMBO J 21: 6083-6094 (Pubitemid 35422657)
    • (2002) EMBO Journal , vol.21 , Issue.22 , pp. 6083-6094
    • Kessels, M.M.1    Qualmann, B.2
  • 37
    • 4344619558 scopus 로고    scopus 로고
    • The syndapin protein family: Linking membrane trafficking with the cytoskeleton
    • DOI 10.1242/jcs.01290
    • Kessels MM, Qualmann B (2004) The syndapin protein family: linking membrane trafficking with the cytoskeleton. J Cell Sci 117: 3077-3086 (Pubitemid 39144341)
    • (2004) Journal of Cell Science , vol.117 , Issue.15 , pp. 3077-3086
    • Kessels, M.M.1    Qualmann, B.2
  • 38
    • 33745000739 scopus 로고    scopus 로고
    • Syndapin oligomers interconnect the machineries for endocytic vesicle formation and actin polymerization
    • DOI 10.1074/jbc.M510226200
    • Kessels MM, Qualmann B (2006) Syndapin oligomers interconnect the machineries for endocytic vesicle formation and actin polymerization. J Biol Chem 281: 13285-13299 (Pubitemid 43862164)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.19 , pp. 13285-13299
    • Kessels, M.M.1    Qualmann, B.2
  • 40
    • 0032538636 scopus 로고    scopus 로고
    • The pleckstrin homology domains of dynamin isoforms require oligomerization for high affinity phosphoinositide binding
    • DOI 10.1074/jbc.273.42.27725
    • Klein DE, Lee A, Frank DW, Marks MS, Lemmon MA (1998) The pleckstrin homology domains of dynamin isoforms require oli-gomerization for high affinity phosphoinositide binding. J Biol Chem 273: 27725-27733 (Pubitemid 28500499)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.42 , pp. 27725-27733
    • Klein, D.E.1    Lee, A.2    Frank, D.W.3    Marks, M.S.4    Lemmon, M.A.5
  • 41
    • 59049089760 scopus 로고    scopus 로고
    • Syndapin is dispensable for synaptic vesicle endocytosis at the Drosophila larval neuromuscular junction
    • Kumar V, Alla SR, Krishnan KS, Ramaswami M (2009) Syndapin is dispensable for synaptic vesicle endocytosis at the Drosophila larval neuromuscular junction. Mol Cell Neurosci 2: 234-241
    • (2009) Mol Cell Neurosci , vol.2 , pp. 234-241
    • Kumar, V.1    Alla, S.R.2    Krishnan, K.S.3    Ramaswami, M.4
  • 47
    • 0034611006 scopus 로고    scopus 로고
    • Syndapin isoforms participate in receptor-mediated endocytosis and actin organization
    • Qualmann B, Kelly RB (2000) Syndapin isoforms participate in receptor-mediated endocytosis and actin organization. J Cell Biol 148: 1047-1062
    • (2000) J Cell Biol , vol.148 , pp. 1047-1062
    • Qualmann, B.1    Kelly, R.B.2
  • 48
    • 80052194357 scopus 로고    scopus 로고
    • Let's go bananas: Revisiting the endocytic bar code
    • Qualmann B, Koch D, Kessels MM (2011) Let's go bananas: revisiting the endocytic bar code. EMBO J 30: 3501-3515
    • (2011) EMBO J , vol.30 , pp. 3501-3515
    • Qualmann, B.1    Koch, D.2    Kessels, M.M.3
  • 49
    • 0032919866 scopus 로고    scopus 로고
    • Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein
    • Qualmann B, Roos J, DiGregorio PJ, Kelly RB (1999) Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein. Mol Biol Cell 10: 501-513 (Pubitemid 29156487)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.2 , pp. 501-513
    • Qualmann, B.1    Roos, J.2    DiGregorio, P.J.3    Kelly, R.B.4
  • 50
    • 0014468553 scopus 로고
    • Formation and properties of thin-walled phospholipid vesicles
    • Reeves JP, Dowben RM (1969) Formation and properties of thin-walled phospholipid vesicles. J Cell Physiol 1: 49-60
    • (1969) J Cell Physiol , vol.1 , pp. 49-60
    • Reeves, J.P.1    Dowben, R.M.2
  • 51
    • 33745755751 scopus 로고    scopus 로고
    • A pre-synaptic to-do list for coupling exocytosis to endocytosis
    • DOI 10.1016/j.ceb.2006.06.013, PII S0955067406000895
    • Ryan TA (2006) A pre-synaptic to-do list for coupling exocytosis to endocytosis. Curr Opin Cell Biol 4: 416-421 (Pubitemid 44016062)
    • (2006) Current Opinion in Cell Biology , vol.18 , Issue.4 , pp. 416-421
    • Ryan, T.A.1
  • 53
    • 0030820683 scopus 로고    scopus 로고
    • Quantitative ultrastructural analysis of hippocampal excitatory synapses
    • Schikorski T, Stevens CF (1997) Quantitative ultrastructural analysis of hippocampal excitatory synapses. J Neurosci 17: 5858-5867 (Pubitemid 27310500)
    • (1997) Journal of Neuroscience , vol.17 , Issue.15 , pp. 5858-5867
    • Schikorski, T.1    Stevens, C.F.2
  • 54
    • 77956880594 scopus 로고    scopus 로고
    • A Dyn2-CIN85 complex mediates degradative traffic of the EGFR by regulation of late endosomal budding
    • Schroeder B, Weller SG, Chen J, Billadeau D, McNiven MA (2010) A Dyn2-CIN85 complex mediates degradative traffic of the EGFR by regulation of late endosomal budding. EMBO J 29: 3039-3053
    • (2010) EMBO J , vol.29 , pp. 3039-3053
    • Schroeder, B.1    Weller, S.G.2    Chen, J.3    Billadeau, D.4    McNiven, M.A.5
  • 55
    • 79961021014 scopus 로고    scopus 로고
    • The functions of the actin nucleator Cobl in cellular morphogenesis critically depend on syndapin i
    • Schwintzer L, Koch N, Ahuja R, Grimm J, Kessels MM, Qualmann B (2011) The functions of the actin nucleator Cobl in cellular morphogenesis critically depend on syndapin I. EMBO J 30: 3147-3159
    • (2011) EMBO J , vol.30 , pp. 3147-3159
    • Schwintzer, L.1    Koch, N.2    Ahuja, R.3    Grimm, J.4    Kessels, M.M.5    Qualmann, B.6
  • 59
    • 0035834813 scopus 로고    scopus 로고
    • Synaptic vesicle alterations in rod photoreceptors of synaptophysin-deficient mice
    • DOI 10.1016/S0306-4522(01)00345-1, PII S0306452201003451
    • Spiwoks-Becker I, Vollrath L, Seeliger MW, Jaissle G, Eshkind LG, Leube RE (2001) Synaptic vesicle alterations in rod photoreceptors of synaptophysin-deficient mice. Neuroscience 107: 127-142 (Pubitemid 34020691)
    • (2001) Neuroscience , vol.107 , Issue.1 , pp. 127-142
    • Spiwoks-Becker, I.1    Vollrath, L.2    Seeliger, M.W.3    Jaissle, G.4    Eshkind, L.G.5    Leube, R.E.6
  • 60
    • 0033128097 scopus 로고    scopus 로고
    • Nucleotide-dependent conformational changes in dynamin: Evidence for a mechanochemical molecular spring
    • Stowell MH, Marks B, Wigge P, McMahon HT (1999) Nucleotide-dependent conformational changes in dynamin: evidence for a mechanochemical molecular spring. Nat Cell Biol 1: 27-32 (Pubitemid 129495006)
    • (1999) Nature Cell Biology , vol.1 , Issue.1 , pp. 27-32
    • Stowell, M.H.B.1    Marks, B.2    Wigge, P.3    McMahon, H.T.4
  • 61
    • 2942556680 scopus 로고    scopus 로고
    • The synaptic vesicle cycle
    • DOI 10.1146/annurev.neuro.26.041002.131412
    • Südhof TC (2004) The synaptic vesicle cycle. Annu Rev Neurosci 27: 509-547 (Pubitemid 39050412)
    • (2004) Annual Review of Neuroscience , vol.27 , pp. 509-547
    • Sudhof, T.C.1
  • 65
    • 34249950244 scopus 로고    scopus 로고
    • Do different endocytic pathways make different synaptic vesicles?
    • DOI 10.1016/j.conb.2007.04.002, PII S0959438807000566, Signalling mechanisms Edited by Stuart Cull-Candy and Rudiger Klein
    • Voglmaier SM, Edwards RH (2007) Do different endocytic pathways make different synaptic vesicles? Curr Opin Neurobiol 17: 374-380 (Pubitemid 46880322)
    • (2007) Current Opinion in Neurobiology , vol.17 , Issue.3 , pp. 374-380
    • Voglmaier, S.M.1    Edwards, R.H.2


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