메뉴 건너뛰기




Volumn 19, Issue 22, 1999, Pages 9803-9812

Subcellular localization of tetanus neurotoxin-insensitive vesicle- associated membrane protein (VAMP)/VAMP7 in neuronal cells: Evidence for a novel membrane compartment

Author keywords

Clostridial neurotoxin; Exocytosis; Neurite outgrowth; SNARE; Synaptobrevin 2; TI VAMP VAMP7

Indexed keywords

MEMBRANE PROTEIN; NEUROTOXIN; SYNAPTOBREVIN;

EID: 0033571899     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/jneurosci.19-22-09803.1999     Document Type: Article
Times cited : (97)

References (52)
  • 2
    • 0017350927 scopus 로고
    • Rat hippocampal neurons in dispersed cell culture
    • Banker GA, Cowan WM (1977) Rat hippocampal neurons in dispersed cell culture. Brain Res 126:397-425.
    • (1977) Brain Res , vol.126 , pp. 397-425
    • Banker, G.A.1    Cowan, W.M.2
  • 3
    • 0021629684 scopus 로고
    • An electron microscopic study of the development of axons and dendrites by hippocampal neurons in culture. I. Cells which develop without intercellular contacts
    • Bartlett WP, Banker GA (1984) An electron microscopic study of the development of axons and dendrites by hippocampal neurons in culture. I. Cells which develop without intercellular contacts. J Neurosci 4:1944-1953.
    • (1984) J Neurosci , vol.4 , pp. 1944-1953
    • Bartlett, W.P.1    Banker, G.A.2
  • 4
    • 0029029882 scopus 로고
    • Specific association of CD63 with the VLA-3 and VLA-6 integrins
    • Berditchevski F, Bazzoni G, Hemler ME (1995) Specific association of CD63 with the VLA-3 and VLA-6 integrins. J Biol Chem 270:17784-17790.
    • (1995) J Biol Chem , vol.270 , pp. 17784-17790
    • Berditchevski, F.1    Bazzoni, G.2    Hemler, M.E.3
  • 5
    • 0031559252 scopus 로고    scopus 로고
    • Protein transport - A fusion of new ideas
    • Bock JB, Scheller RH (1997) Protein transport - a fusion of new ideas. Nature 387:133-135.
    • (1997) Nature , vol.387 , pp. 133-135
    • Bock, J.B.1    Scheller, R.H.2
  • 7
    • 0019465123 scopus 로고
    • Dendritic release of dopamine in the substantia nigra
    • Cheramy A, Leviel V, Glowinski J (1981) Dendritic release of dopamine in the substantia nigra. Nature 289:537-542.
    • (1981) Nature , vol.289 , pp. 537-542
    • Cheramy, A.1    Leviel, V.2    Glowinski, J.3
  • 10
    • 0033007616 scopus 로고    scopus 로고
    • Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the beta 3A subunit of the AP-3 adaptor
    • Dell'Angelica EC, Shotelersuk V, Aguilar RC, Gahl WA, Bonifacino JS (1999) Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the beta 3A subunit of the AP-3 adaptor. Mol Cell 3:11-21.
    • (1999) Mol Cell , vol.3 , pp. 11-21
    • Dell'Angelica, E.C.1    Shotelersuk, V.2    Aguilar, R.C.3    Gahl, W.A.4    Bonifacino, J.S.5
  • 11
    • 0030051441 scopus 로고    scopus 로고
    • The AP-1 adaptor complex binds to immature secretory granules from PC12 cells, and is regulated by ADP-ribosylation factor
    • Dittie AS, Hajibagheri N, Tooze SA (1996) The AP-1 adaptor complex binds to immature secretory granules from PC12 cells, and is regulated by ADP-ribosylation factor. J Cell Biol 132:523-536.
    • (1996) J Cell Biol , vol.132 , pp. 523-536
    • Dittie, A.S.1    Hajibagheri, N.2    Tooze, S.A.3
  • 12
    • 0032554906 scopus 로고    scopus 로고
    • Membrane fusion: All done with SNAREpins?
    • Edwardson JM (1998) Membrane fusion: all done with SNAREpins? Curr Biol 8:R390-R393.
    • (1998) Curr Biol , vol.8
    • Edwardson, J.M.1
  • 13
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
    • Fasshauer D, Sutton RB, Brunger AT, Jahn R (1998) Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc Natl Acad Sci USA 95:15781-15786.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brunger, A.T.3    Jahn, R.4
  • 14
    • 0033034407 scopus 로고    scopus 로고
    • Mixed and non-cognate SNARE complexes. Characterization of assembly and biophysical properties
    • Fasshauer D, Antonin W, Margittai M, Pabst S, Jahn R (1999) Mixed and non-cognate SNARE complexes. Characterization of assembly and biophysical properties. J Biol Chem 274:15440-15446.
    • (1999) J Biol Chem , vol.274 , pp. 15440-15446
    • Fasshauer, D.1    Antonin, W.2    Margittai, M.3    Pabst, S.4    Jahn, R.5
  • 15
    • 0032944111 scopus 로고    scopus 로고
    • Evidence for calcium-dependent vesicular transmitter release insensitive to tetanus toxin and botulinum toxin type F
    • Fassio A, Sala R, Bonanno G, Marchi M, Raiteri M (1999) Evidence for calcium-dependent vesicular transmitter release insensitive to tetanus toxin and botulinum toxin type F. Neuroscience 90:893-902.
    • (1999) Neuroscience , vol.90 , pp. 893-902
    • Fassio, A.1    Sala, R.2    Bonanno, G.3    Marchi, M.4    Raiteri, M.5
  • 16
    • 0028291894 scopus 로고
    • Tetanus toxin-mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor-containing vesicles in CHO cells
    • Galli T, Chilcote T, Mundigl O, Binz T, Niemann H, De Camilli P (1994) Tetanus toxin-mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor-containing vesicles in CHO cells. J Cell Biol 125:1015-1024.
    • (1994) J Cell Biol , vol.125 , pp. 1015-1024
    • Galli, T.1    Chilcote, T.2    Mundigl, O.3    Binz, T.4    Niemann, H.5    De Camilli, P.6
  • 17
    • 0028880697 scopus 로고
    • v- and t-SNAREs in neuronal exocytosis: A need for additional components to define sites of release
    • Galli T, Garcia EP, Mundigl O, Chilcote TJ, De Camilli P (1995) v- and t-SNAREs in neuronal exocytosis: a need for additional components to define sites of release. Neuropharmacology 34:1351-1360.
    • (1995) Neuropharmacology , vol.34 , pp. 1351-1360
    • Galli, T.1    Garcia, E.P.2    Mundigl, O.3    Chilcote, T.J.4    De Camilli, P.5
  • 18
    • 0031814298 scopus 로고    scopus 로고
    • A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells
    • Galli T, Zahraoui A, Vaidyanathan VV, Raposo G, Tian JM, Karin M, NiemannH, Louvard D (1998) A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells. Mol Biol Cell 9:1437-1448.
    • (1998) Mol Biol Cell , vol.9 , pp. 1437-1448
    • Galli, T.1    Zahraoui, A.2    Vaidyanathan, V.V.3    Raposo, G.4    Tian, J.M.5    Karin, M.6    Niemann, H.7    Louvard, D.8
  • 19
    • 0029005106 scopus 로고
    • A targeting signal in VAMP regulating transport to synaptic vesicles
    • Grote E, Hao JC, Bennett MK, Kelly RB (1995) A targeting signal in VAMP regulating transport to synaptic vesicles. Cell 81:581-589.
    • (1995) Cell , vol.81 , pp. 581-589
    • Grote, E.1    Hao, J.C.2    Bennett, M.K.3    Kelly, R.B.4
  • 20
    • 0030796026 scopus 로고    scopus 로고
    • SNAREs and NSF in targeted membrane fusion
    • Hay JC, Scheller RH (1997) SNAREs and NSF in targeted membrane fusion. Curr Opin Cell Biol 9:505-512.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 505-512
    • Hay, J.C.1    Scheller, R.H.2
  • 21
    • 0033558032 scopus 로고    scopus 로고
    • The sec6/8 complex is located at neurite outgrowth and axonal synapse-assembly domains
    • Hazuka CD, Foletti DL, Hsu SC, Kee Y, Hopf FW, Scheller RH (1999) The sec6/8 complex is located at neurite outgrowth and axonal synapse-assembly domains. J Neurosci 19:1324-1334.
    • (1999) J Neurosci , vol.19 , pp. 1324-1334
    • Hazuka, C.D.1    Foletti, D.L.2    Hsu, S.C.3    Kee, Y.4    Hopf, F.W.5    Scheller, R.H.6
  • 23
    • 0019423594 scopus 로고
    • Use of avidin-biotin-peroxydase complex (ABC) in immunoperoxydase techniques: A comparison between ABC and unlabeled antibody (PAP) procedures
    • Hsu S-M, Raine L, Fanger H (1981) Use of avidin-biotin-peroxydase complex (ABC) in immunoperoxydase techniques: a comparison between ABC and unlabeled antibody (PAP) procedures. J Histochem Cytochem 29:577-580.
    • (1981) J Histochem Cytochem , vol.29 , pp. 577-580
    • Hsu, S.-M.1    Raine, L.2    Fanger, H.3
  • 24
    • 0029949638 scopus 로고    scopus 로고
    • Growth cone collapse and inhibition of neurite growth by Botulinum neurotoxin C1: A t-SNARE is involved in axonal growth
    • Igarashi M, Kozaki S, Terakawa S, Kawano S, Ide C, Komiya Y (1996) Growth cone collapse and inhibition of neurite growth by Botulinum neurotoxin C1: a t-SNARE is involved in axonal growth. J Cell Biol 134:205-215.
    • (1996) J Cell Biol , vol.134 , pp. 205-215
    • Igarashi, M.1    Kozaki, S.2    Terakawa, S.3    Kawano, S.4    Ide, C.5    Komiya, Y.6
  • 25
    • 0029062772 scopus 로고
    • Different requirements for NSF, SNAP, and rab proteins in apical and basolateral transport in MDCK cells
    • Ikonen E, Tagaya M, Ullrich O, Montecucco C, Simons K (1995) Different requirements for NSF, SNAP, and rab proteins in apical and basolateral transport in MDCK cells. Cell 81:571-580.
    • (1995) Cell , vol.81 , pp. 571-580
    • Ikonen, E.1    Tagaya, M.2    Ullrich, O.3    Montecucco, C.4    Simons, K.5
  • 26
    • 0032525142 scopus 로고    scopus 로고
    • Extrasynaptic vesicular transmitter release from the somata of substantia nigra neurons in rat midbrain slices
    • Jaffe EH, Marty A, Schulte A, Chow RH (1998) Extrasynaptic vesicular transmitter release from the somata of substantia nigra neurons in rat midbrain slices. J Neurosci 18:3548-3553.
    • (1998) J Neurosci , vol.18 , pp. 3548-3553
    • Jaffe, E.H.1    Marty, A.2    Schulte, A.3    Chow, R.H.4
  • 28
    • 0031841676 scopus 로고    scopus 로고
    • Exocytosis: SNAREs drum up
    • Johannes L, Galli T (1998) Exocytosis: SNAREs drum up. Eur J Neurosci 10:415-422.
    • (1998) Eur J Neurosci , vol.10 , pp. 415-422
    • Johannes, L.1    Galli, T.2
  • 31
    • 0029847075 scopus 로고    scopus 로고
    • Differential localization of syntaxin isoforms in polarized Madin-Darby canine kidney cells
    • Low SH, Chapin SJ, Weimbs T, Komuves LG, Bennett MK, Mostov KE (1996) Differential localization of syntaxin isoforms in polarized Madin-Darby canine kidney cells. Mol Biol Cell 7:2007-2018.
    • (1996) Mol Biol Cell , vol.7 , pp. 2007-2018
    • Low, S.H.1    Chapin, S.J.2    Weimbs, T.3    Komuves, L.G.4    Bennett, M.K.5    Mostov, K.E.6
  • 32
    • 0030947554 scopus 로고    scopus 로고
    • The tetraspanin superfamily: Molecular facilitators
    • Maecker HT, Todd SC, Levy S (1997) The tetraspanin superfamily: molecular facilitators. FASEB J 11:428-442.
    • (1997) FASEB J , vol.11 , pp. 428-442
    • Maecker, H.T.1    Todd, S.C.2    Levy, S.3
  • 33
    • 0032171172 scopus 로고    scopus 로고
    • Calcium-evoked dendritic exocytosis in cultured hippocampal neurons. I. Trans-Golgi network-derived organelles undergo regulated exocytosis
    • MaleticSavatic M, Malinow R (1998) Calcium-evoked dendritic exocytosis in cultured hippocampal neurons. I. Trans-Golgi network-derived organelles undergo regulated exocytosis. J Neurosci 18:6803-6813.
    • (1998) J Neurosci , vol.18 , pp. 6803-6813
    • MaleticSavatic, M.1    Malinow, R.2
  • 34
    • 0032171363 scopus 로고    scopus 로고
    • Calcium-evoked dendritic exocytosis in cultured hippocampal neurons. II. Mediation by calcium/calmodulin-dependent protein kinase II
    • MaleticSavatic M, Koothan T, Malinow R (1998) Calcium-evoked dendritic exocytosis in cultured hippocampal neurons. II. Mediation by calcium/calmodulin-dependent protein kinase II. J Neurosci 18:6814-6821.
    • (1998) J Neurosci , vol.18 , pp. 6814-6821
    • MaleticSavatic, M.1    Koothan, T.2    Malinow, R.3
  • 35
    • 0033583022 scopus 로고    scopus 로고
    • Rapid dendritic morphogenesis in CA1 hippocampal dendrites induced by synaptic activity
    • MaleticSavatic M, Malinow R, Svoboda K (1999) Rapid dendritic morphogenesis in CA1 hippocampal dendrites induced by synaptic activity. Science 283:1923-1927.
    • (1999) Science , vol.283 , pp. 1923-1927
    • MaleticSavatic, M.1    Malinow, R.2    Svoboda, K.3
  • 42
    • 0002478233 scopus 로고    scopus 로고
    • Immunogold labeling of ultrathin cryosections: Application in immunology
    • Herzenberg LA, Weir DM, Blackwell C, eds, Malden, MA: Blackwell
    • Raposo G, Kleijmer KJ, Posthuma G, Slot JW, Geuze HJ (1997) Immunogold labeling of ultrathin cryosections: application in immunology. In: Handbook of experimental immunology (Herzenberg LA, Weir DM, Blackwell C, eds), pp 1-11. Malden, MA: Blackwell.
    • (1997) Handbook of Experimental Immunology , pp. 1-11
    • Raposo, G.1    Kleijmer, K.J.2    Posthuma, G.3    Slot, J.W.4    Geuze, H.J.5
  • 44
    • 0029990197 scopus 로고    scopus 로고
    • On the possible origin of giant or slow-rising miniature end-plate potentials at the neuromuscular junction
    • Sellin LC, Molgo J, Tornquist K, Hansson B, Thesleff S (1996) On the possible origin of giant or slow-rising miniature end-plate potentials at the neuromuscular junction. Pflügers Arch 431:325-334.
    • (1996) Pflügers Arch , vol.431 , pp. 325-334
    • Sellin, L.C.1    Molgo, J.2    Tornquist, K.3    Hansson, B.4    Thesleff, S.5
  • 45
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E (1997) Functional rafts in cell membranes. Nature 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 46
    • 0032978225 scopus 로고    scopus 로고
    • Vesicle-associated membrane protein 4 is implicated in trans-Golgi network vesicle trafficking
    • Steegmaier M, Klumperman J, Foletti DL, Yoo JS, Scheller RH (1999) Vesicle-associated membrane protein 4 is implicated in trans-Golgi network vesicle trafficking. Mol Biol Cell 10:1957-1972.
    • (1999) Mol Biol Cell , vol.10 , pp. 1957-1972
    • Steegmaier, M.1    Klumperman, J.2    Foletti, D.L.3    Yoo, J.S.4    Scheller, R.H.5
  • 49
    • 0030990122 scopus 로고    scopus 로고
    • The yeast v-SNARE Vtilp mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p
    • Von Mollard GF, Nothwehr SF, Stevens TH (1997) The yeast v-SNARE Vtilp mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p. J Cell Biol 137:1511-1524.
    • (1997) J Cell Biol , vol.137 , pp. 1511-1524
    • Von Mollard, G.F.1    Nothwehr, S.F.2    Stevens, T.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.