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Volumn 148, Issue 2, 2000, Pages 247-252

nSec1 binds a closed conformation of syntaxin1A

Author keywords

Exocytosis; Membrane fusion; SNARE; Synapse; Synaptic vesicles

Indexed keywords

NEUROTOXIN; SNARE PROTEIN; SYNAPTOBREVIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNTAXIN;

EID: 0034707644     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.148.2.247     Document Type: Article
Times cited : (231)

References (27)
  • 1
    • 0029127250 scopus 로고
    • SNAREs and the specificity of transport vesicle targeting
    • Bennett, M.K. 1995. SNAREs and the specificity of transport vesicle targeting. Curr. Opin. Cell Biol. 7:581-586.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 581-586
    • Bennett, M.K.1
  • 2
    • 0028245594 scopus 로고
    • A molecular description of synaptic vesicle membrane trafficking
    • Bennett, M.K., and R.H. Scheller. 1994. A molecular description of synaptic vesicle membrane trafficking. Annu. Rev. Biochem. 63:63-100.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 63-100
    • Bennett, M.K.1    Scheller, R.H.2
  • 3
    • 0028030275 scopus 로고
    • Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis
    • Brennwald, P., B. Kearns, K. Champion, S. Keranen, V. Bankaitis, and P. Novick. 1994. Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis. Cell. 79:245-258.
    • (1994) Cell , vol.79 , pp. 245-258
    • Brennwald, P.1    Kearns, B.2    Champion, K.3    Keranen, S.4    Bankaitis, V.5    Novick, P.6
  • 4
    • 0027971368 scopus 로고
    • Vesicle-associated membrane protein and synaptophysin are associated or the synaptic vesicle
    • Calakos, N., and R.H. Serieller. 1994. Vesicle-associated membrane protein and synaptophysin are associated or the synaptic vesicle. J. Biol. Chem. 269: 24534-24537.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24534-24537
    • Calakos, N.1    Serieller, R.H.2
  • 5
    • 0028350057 scopus 로고
    • Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking
    • Calakos, N., M.K. Bennett, K.E. Peterson, and R.H. Scheller. 1994. Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking. Science. 263:1146-1149.
    • (1994) Science , vol.263 , pp. 1146-1149
    • Calakos, N.1    Bennett, M.K.2    Peterson, K.E.3    Scheller, R.H.4
  • 6
    • 0033606766 scopus 로고    scopus 로고
    • Sec1p binds to SNARE complexes and concentrates at sites of secretion
    • Carr, C.M., E. Grote, M. Munson, F.M. Hughson, and P.J. Novick. 1999. Sec1p binds to SNARE complexes and concentrates at sites of secretion. J. Cell Biol. 146:333-344.
    • (1999) J. Cell Biol. , vol.146 , pp. 333-344
    • Carr, C.M.1    Grote, E.2    Munson, M.3    Hughson, F.M.4    Novick, P.J.5
  • 8
    • 0028605474 scopus 로고
    • Mutations in the VPS45 gene, a SEC1 homologue, result in vacuolar protein sorting defects and accumulation of membrane vesicles
    • Cowles, C.R., S.D. Emr, and B.F. Horazdovsky. 1994. Mutations in the VPS45 gene, a SEC1 homologue, result in vacuolar protein sorting defects and accumulation of membrane vesicles. J. Cell Sci. 107:3449-3459.
    • (1994) J. Cell Sci. , vol.107 , pp. 3449-3459
    • Cowles, C.R.1    Emr, S.D.2    Horazdovsky, B.F.3
  • 10
    • 0032544441 scopus 로고    scopus 로고
    • Three-dimensional structure of an evolutionary conserved N-terminal domain of syntaxin 1A
    • Fernandez, I., J. Ubach, I. Dulubova, X. Zhang, T.C. Sudhof, and J. Rizo. 1998. Three-dimensional structure of an evolutionary conserved N-terminal domain of syntaxin 1A. Cell. 94:841-849.
    • (1998) Cell , vol.94 , pp. 841-849
    • Fernandez, I.1    Ubach, J.2    Dulubova, I.3    Zhang, X.4    Sudhof, T.C.5    Rizo, J.6
  • 12
    • 0027364502 scopus 로고
    • Synaptic vesicle fusion complex contains unc-18 homologue hound to syntaxin
    • Hata, Y., C.A. Slaughter, and T.C. Sudhof. 1993. Synaptic vesicle fusion complex contains unc-18 homologue hound to syntaxin. Nature. 366:347-351.
    • (1993) Nature , vol.366 , pp. 347-351
    • Hata, Y.1    Slaughter, C.A.2    Sudhof, T.C.3
  • 14
    • 0028244421 scopus 로고
    • In chromaffin cells, the mammalian Sec1p homologue is a syntaxin 1A-binding protein associated with chromaffin granules
    • Hodel, A., T. Schafer, D. Gerosa, and M.M. Burger. 1994. In chromaffin cells, the mammalian Sec1p homologue is a syntaxin 1A-binding protein associated with chromaffin granules. J. Biol Chem. 269:8623-8626.
    • (1994) J. Biol Chem. , vol.269 , pp. 8623-8626
    • Hodel, A.1    Schafer, T.2    Gerosa, D.3    Burger, M.M.4
  • 15
    • 0028216869 scopus 로고
    • Synaptic vesicles and exocytosis
    • Jahn, R., and T.C. Südhof. 1994. Synaptic vesicles and exocytosis. Annu. Rev. Neurosci. 17:219-246.
    • (1994) Annu. Rev. Neurosci. , vol.17 , pp. 219-246
    • Jahn, R.1    Südhof, T.C.2
  • 16
    • 0000756130 scopus 로고
    • Secretion and cell surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae
    • Novick, P., and R. Scheckman. 1979. Secretion and cell surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA. 76:1858-1862.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 1858-1862
    • Novick, P.1    Scheckman, R.2
  • 17
    • 0025891541 scopus 로고
    • The yeast SLY gene products, suppressors of defects in the essential GTP-binding Ypt1 protein, may act in endoplasmic reticulum-to-Golgi transport
    • Ossig, R., C. Dascher, H.H. Trepte, H.D. Schmitt, and D. Gallwitz. 1991. The yeast SLY gene products, suppressors of defects in the essential GTP-binding Ypt1 protein, may act in endoplasmic reticulum-to-Golgi transport. Mol. Cell. Biol. 11:2980-2993.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2980-2993
    • Ossig, R.1    Dascher, C.2    Trepte, H.H.3    Schmitt, H.D.4    Gallwitz, D.5
  • 18
    • 0033545389 scopus 로고    scopus 로고
    • Vac1p coordinates Rab and phosphatidylinositol 3-kinase signaling in Vps45p-dependent vesicle docking/fusion at the endosome
    • Peterson, M.R., C.G. Burd, and S.D. Emr. 1999. Vac1p coordinates Rab and phosphatidylinositol 3-kinase signaling in Vps45p-dependent vesicle docking/fusion at the endosome. Curr. Biol. 9:159-162.
    • (1999) Curr. Biol. , vol.9 , pp. 159-162
    • Peterson, M.R.1    Burd, C.G.2    Emr, S.D.3
  • 22
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J.E. 1994. Mechanisms of intracellular protein transport. Nature. 372: 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 23
    • 0028102686 scopus 로고
    • rop, a Drosophila homolog of yeast Sec1 and vertebrate n-Sec1/Munc-18 proteins, is a negative regulator of neurotransmitter release in vivo
    • Schulze, K.L., J.T. Littleton, A. Salzberg, N. Halachmi, M. Stern, Z. Lev, and H.J. Bellen. 1994. rop, a Drosophila homolog of yeast Sec1 and vertebrate n-Sec1/Munc-18 proteins, is a negative regulator of neurotransmitter release in vivo. Neuron. 13:1099-1108.
    • (1994) Neuron. , vol.13 , pp. 1099-1108
    • Schulze, K.L.1    Littleton, J.T.2    Salzberg, A.3    Halachmi, N.4    Stern, M.5    Lev, Z.6    Bellen, H.J.7
  • 24
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
    • Sutton, R.B., D. Fasshauer, R. Jahn, and A.T. Brunger. 1998. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature. 395:347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 26
    • 0032472409 scopus 로고    scopus 로고
    • ROP, the Drosophila Sec1 homolog, interacts with syntaxin and regulates neurotransmitter release in a dosage-dependent manner
    • Wu, M.N., J.T. Littleton, M.A. Bhal, A. Prokop, and H.J. Bellen. 1998. ROP, the Drosophila Sec1 homolog, interacts with syntaxin and regulates neurotransmitter release in a dosage-dependent manner. EMBO (Eur. Mol. Biol. Organ.) J. 17:127-139.
    • (1998) EMBO (Eur. Mol. Biol. Organ.) J. , vol.17 , pp. 127-139
    • Wu, M.N.1    Littleton, J.T.2    Bhal, M.A.3    Prokop, A.4    Bellen, H.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.