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Volumn 558, Issue 3, 2004, Pages 857-871

Regulation of syntaxin 1A-munc18 complex for SNARE pairing in HEK293 cells

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CHANNEL N TYPE; CALCIUM ION; NEUROTRANSMITTER; SNARE PROTEIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNTAXIN; SYNTAXIN 1A; UNCLASSIFIED DRUG; MEMBRANE ANTIGEN; MUNC18 PROTEIN; NERVE PROTEIN; SYNTAXIN 1; VESICULAR TRANSPORT PROTEIN; MEMBRANE PROTEIN; MUNC13 1 PROTEIN; MUNC13 2 PROTEIN; MUNC13 3 PROTEIN;

EID: 4444256694     PISSN: 00223751     EISSN: None     Source Type: Journal    
DOI: 10.1113/jphysiol.2004.067249     Document Type: Article
Times cited : (17)

References (58)
  • 3
    • 0033084096 scopus 로고    scopus 로고
    • Differential expression of two novel Munc13 proteins in rat brain
    • Augustin I, Betz A, Herrmann C, Jo T & Brose N (1999a). Differential expression of two novel Munc13 proteins in rat brain. Biochem J 337, 363-371.
    • (1999) Biochem. J. , vol.337 , pp. 363-371
    • Augustin, I.1    Betz, A.2    Herrmann, C.3    Jo, T.4    Brose, N.5
  • 4
    • 0033615054 scopus 로고    scopus 로고
    • Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles
    • Augustin I, Rosenmund C, Sudhof TC & Brose N (1999b). Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles. Nature 400, 457-461.
    • (1999) Nature , vol.400 , pp. 457-461
    • Augustin, I.1    Rosenmund, C.2    Sudhof, T.C.3    Brose, N.4
  • 6
    • 0034660461 scopus 로고    scopus 로고
    • Syntaxin modulation of calcium channels in cortical synaptosomes as revealed by botulinum toxin C1
    • Bergsman JB & Tsien RW (2000). Syntaxin modulation of calcium channels in cortical synaptosomes as revealed by botulinum toxin C1.J Neuroscience 20, 4368-4378.
    • (2000) J. Neuroscience , vol.20 , pp. 4368-4378
    • Bergsman, J.B.1    Tsien, R.W.2
  • 7
    • 0031027591 scopus 로고    scopus 로고
    • Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin
    • Betz A, Okamoto M, Benseler F & Brose N (1997). Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin. J Biol Chem 272, 2520-2526.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2520-2526
    • Betz, A.1    Okamoto, M.2    Benseler, F.3    Brose, N.4
  • 8
    • 0028783997 scopus 로고
    • Functional impact of syntaxin on gating of N-type and Q-type calcium channels
    • Bezprozvanny I, Scheller RH & Tsien RW (1995). Functional impact of syntaxin on gating of N-type and Q-type calcium channels. Nature 378, 623-626.
    • (1995) Nature , vol.378 , pp. 623-626
    • Bezprozvanny, I.1    Scheller, R.H.2    Tsien, R.W.3
  • 9
    • 0034082054 scopus 로고    scopus 로고
    • Regulation of transmitter release by Unc-13 and its homologues
    • Brose N, Rosenmund C & Rettig J (2000). Regulation of transmitter release by Unc-13 and its homologues. Current Opinion Neurobiol 10, 303-311.
    • (2000) Current Opinion Neurobiol. , vol.10 , pp. 303-311
    • Brose, N.1    Rosenmund, C.2    Rettig, J.3
  • 10
    • 0035119963 scopus 로고    scopus 로고
    • The taming of the SNARE
    • Carr CM (2001). The taming of the SNARE. Nature Structural Biol 8, 186-188.
    • (2001) Nature Structural Biol. , vol.8 , pp. 186-188
    • Carr, C.M.1
  • 12
    • 0028605474 scopus 로고
    • Mutations in the VPS45 gene, a SEC1 homologue, result in vacuolar protein sorting defects and accumulation of membrane vesicles
    • Cowles CR, Emr SD & Horazdovsky BF (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
  • 13
    • 0034659740 scopus 로고    scopus 로고
    • Syntaxin modulation of slow inactivation of N-type calcium channels
    • Degtiar VE, Scheller RH & Tsien RW (2000). Syntaxin modulation of slow inactivation of N-type calcium channels. J Neuroscience 20, 4355-4367.
    • (2000) J. Neuroscience , vol.20 , pp. 4355-4367
    • Degtiar, V.E.1    Scheller, R.H.2    Tsien, R.W.3
  • 14
    • 0031963368 scopus 로고    scopus 로고
    • Mechanisms of modulation of voltage-dependent calcium channels by G proteins
    • Dolphin AC (1998). Mechanisms of modulation of voltage-dependent calcium channels by G proteins. J Physiol 506, 3-11.
    • (1998) J. Physiol. , vol.506 , pp. 3-11
    • Dolphin, A.C.1
  • 21
    • 0034101479 scopus 로고    scopus 로고
    • Sec1 gets a grip on syntaxin
    • Hanson PI (2000). Sec1 gets a grip on syntaxin. Nature Structural Biol 7, 347-349.
    • (2000) Nature Structural Biol. , vol.7 , pp. 347-349
    • Hanson, P.I.1
  • 22
    • 0027938531 scopus 로고
    • Mutations in the Drosophila Rop gene suggest a function in general secretion and synaptic transmission
    • Harrison SD, Broadie K, van de Goor J & Rubin GM (1994). Mutations in the Drosophila Rop gene suggest a function in general secretion and synaptic transmission. Neuron 13, 555-566.
    • (1994) Neuron , vol.13 , pp. 555-566
    • Harrison, S.D.1    Broadie, K.2    van de Goor, J.3    Rubin, G.M.4
  • 23
    • 0003694894 scopus 로고
    • Pulse control V4.5: IGOR XOPs for patch clamp data acquistion and capaticance measurements
    • University of Miami, Miami, FL, USA
    • Herrington J, Newton K & Bookman R (1995). Pulse control V4.5: IGOR XOPs for patch clamp data acquistion and capaticance measurements. University of Miami, Miami, FL, USA..
    • (1995)
    • Herrington, J.1    Newton, K.2    Bookman, R.3
  • 24
    • 0026582816 scopus 로고
    • The unc-18 gene encodes a novel protein affecting the kinetics of acetylcholine metabolism in the nematode Caenorhabditis elegans
    • Hosono R, Hekimi S, Kamiya Y, Sassa T, Murakami S, Nishiwaki K, Miwa J, Taketo A & Kodaira KI (1992). The unc-18 gene encodes a novel protein affecting the kinetics of acetylcholine metabolism in the nematode Caenorhabditis elegans. J Neurochem 58, 1517-1525.
    • (1992) J. Neurochem. , vol.58 , pp. 1517-1525
    • Hosono, R.1    Hekimi, S.2    Kamiya, Y.3    Sassa, T.4    Murakami, S.5    Nishiwaki, K.6    Miwa, J.7    Taketo, A.8    Kodaira, K.I.9
  • 25
    • 0032617253 scopus 로고    scopus 로고
    • Voltage-dependent modulation of N-type calcium channels: Role of G protein subunits
    • Ikeda SR & Dunlap K (1999). Voltage-dependent modulation of N-type calcium channels: role of G protein subunits. Adv Second Messenger Phosphoprotein Research 33, 131-151.
    • (1999) Adv. Second Messenger Phosphoprotein Research , vol.33 , pp. 131-151
    • Ikeda, S.R.1    Dunlap, K.2
  • 26
    • 0034054672 scopus 로고    scopus 로고
    • G protein modulation of N-type calcium channels is facilitated by physical interactions between syntaxin 1A and Gβ γ
    • Jarvis SE, Magga JM, Beedle AM, Braun JE & Zamponi GW (2000). G protein modulation of N-type calcium channels is facilitated by physical interactions between syntaxin 1A and Gβγ. J Biol Chem 275, 6388-6394.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6388-6394
    • Jarvis, S.E.1    Magga, J.M.2    Beedle, A.M.3    Braun, J.E.4    Zamponi, G.W.5
  • 27
    • 0035341357 scopus 로고    scopus 로고
    • Distinct molecular determinants govern syntaxin 1A-mediated inactivation and G-protein inhibition of N-type calcium channels
    • Jarvis SE & Zamponi GW (2001). Distinct molecular determinants govern syntaxin 1A-mediated inactivation and G-protein inhibition of N-type calcium channels. J Neuroscience 21, 2939-2948.
    • (2001) J. Neuroscience , vol.21 , pp. 2939-2948
    • Jarvis, S.E.1    Zamponi, G.W.2
  • 28
    • 0034713847 scopus 로고    scopus 로고
    • Structural analysis of the neuronal SNARE protein syntaxin-1A
    • Lerman JC, Robblee J, Fairman R & Hughson FM (2000). Structural analysis of the neuronal SNARE protein syntaxin-1A. Biochemistry 39, 8470-8479.
    • (2000) Biochemistry , vol.39 , pp. 8470-8479
    • Lerman, J.C.1    Robblee, J.2    Fairman, R.3    Hughson, F.M.4
  • 30
    • 0037187635 scopus 로고    scopus 로고
    • Prime movers of synaptic vesicle exocytosis
    • Martin TF (2002). Prime movers of synaptic vesicle exocytosis. Neuron 34, 9-12.
    • (2002) Neuron , vol.34 , pp. 9-12
    • Martin, T.F.1
  • 31
    • 0034704771 scopus 로고    scopus 로고
    • Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex
    • Misura KM, Scheller RH & Weis WI (2000). Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex. Nature 404, 355-362.
    • (2000) Nature , vol.404 , pp. 355-362
    • Misura, K.M.1    Scheller, R.H.2    Weis, W.I.3
  • 32
    • 0000756130 scopus 로고
    • Secretion and cell-surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae
    • Novick P & Schekman R (1979). Secretion and cell-surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 76, 1858-1862.
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 1858-1862
    • Novick, P.1    Schekman, R.2
  • 36
    • 0033349884 scopus 로고    scopus 로고
    • UNC-13 is required for synaptic vesicle fusion in C. elegans
    • Richmond JE, Davis WS & Jorgensen EM (1999). UNC-13 is required for synaptic vesicle fusion in C. elegans. Nat Neurosci 2, 959-964.
    • (1999) Nat. Neurosci. , vol.2 , pp. 959-964
    • Richmond, J.E.1    Davis, W.S.2    Jorgensen, E.M.3
  • 37
    • 0035913332 scopus 로고    scopus 로고
    • An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming
    • Richmond JE, Weimer RM & Jorgensen EM (2001). An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming. Nature 412, 338-341.
    • (2001) Nature , vol.412 , pp. 338-341
    • Richmond, J.E.1    Weimer, R.M.2    Jorgensen, E.M.3
  • 38
    • 0036673069 scopus 로고    scopus 로고
    • Snares and Munc18 in synaptic vesicle fusion
    • Rizo J & Sudhof TC (2002). Snares and Munc18 in synaptic vesicle fusion. Nat Rev Neurosci 3, 641-653.
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 641-653
    • Rizo, J.1    Sudhof, T.C.2
  • 39
    • 0037204063 scopus 로고    scopus 로고
    • Differential control of vesicle priming and short-term plasticity by Munc13 isoforms
    • Rosenmund C, Sigler A, Augustin I, Reim K, Brose N & Rhee JS (2002). Differential control of vesicle priming and short-term plasticity by Munc13 isoforms. Neuron 33, 411-424.
    • (2002) Neuron , vol.33 , pp. 411-424
    • Rosenmund, C.1    Sigler, A.2    Augustin, I.3    Reim, K.4    Brose, N.5    Rhee, J.S.6
  • 40
    • 0032775945 scopus 로고    scopus 로고
    • Blockade of membrane transport and disassembly of the Golgi complex by expression of syntaxin 1A in neurosecretion-incompetent cells: Prevention by rbSEC1
    • Rowe J, Corradi N, Malosio ML, Taverna E, Halban P, Meldolesi J & Rosa P (1999). Blockade of membrane transport and disassembly of the Golgi complex by expression of syntaxin 1A in neurosecretion-incompetent cells: prevention by rbSEC1. J Cell Sci 112, 1865-1877.
    • (1999) J. Cell Sci. , vol.112 , pp. 1865-1877
    • Rowe, J.1    Corradi, N.2    Malosio, M.L.3    Taverna, E.4    Halban, P.5    Meldolesi, J.6    Rosa, P.7
  • 43
    • 0029065548 scopus 로고
    • A syntaxin-related protein controls acetylcholine release by different mechanisms in Aplysia
    • Smirnova T, Fossier P, Stinnakre J, Mallet J & Baux G (1995). A syntaxin-related protein controls acetylcholine release by different mechanisms in Aplysia. Neuroscience 68, 125-133.
    • (1995) Neuroscience , vol.68 , pp. 125-133
    • Smirnova, T.1    Fossier, P.2    Stinnakre, J.3    Mallet, J.4    Baux, G.5
  • 44
    • 0038050215 scopus 로고    scopus 로고
    • Regulated exocytosis and SNARE function
    • Sollner TH (2003). Regulated exocytosis and SNARE function. Mol Membrane Biol 20, 209-220.
    • (2003) Mol. Membrane Biol. , vol.20 , pp. 209-220
    • Sollner, T.H.1
  • 45
    • 0031750748 scopus 로고    scopus 로고
    • Cloning of a novel gene in the human kidney homologous to rat munc13s: Its potential role in diabetic nephropathy
    • Song Y, Ailenberg M & Silverman M (1998). Cloning of a novel gene in the human kidney homologous to rat munc13s: its potential role in diabetic nephropathy. Kidney Int 53, 1689-1695.
    • (1998) Kidney Int. , vol.53 , pp. 1689-1695
    • Song, Y.1    Ailenberg, M.2    Silverman, M.3
  • 46
    • 0031029132 scopus 로고    scopus 로고
    • Cleavage of syntaxin prevents G-protein regulation of presynaptic calcium channels
    • Stanley EF & Mirotznik RR (1997). Cleavage of syntaxin prevents G-protein regulation of presynaptic calcium channels. Nature 385, 340-343.
    • (1997) Nature , vol.385 , pp. 340-343
    • Stanley, E.F.1    Mirotznik, R.R.2
  • 47
    • 0032978370 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-phosphate binding protein Vac1p interacts with a Rab GTPase and a Sec1p homologue to facilitate vesicle-mediated vacuolar protein sorting
    • Tall GG, Hama H, DeWald DB & Horazdovsky BF (1999). The phosphatidylinositol 3-phosphate binding protein Vac1p interacts with a Rab GTPase and a Sec1p homologue to facilitate vesicle-mediated vacuolar protein sorting. Mol Biol Cell 10, 1873-1889.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1873-1889
    • Tall, G.G.1    Hama, H.2    DeWald, D.B.3    Horazdovsky, B.F.4
  • 48
    • 0037172972 scopus 로고    scopus 로고
    • Total arrest of spontaneous and evoked synaptic transmission but normal synaptogenesis in the absence of Munc13-mediated vesicle priming
    • Varoqueaux F, Sigler A, Rhee JS, Brose N, Enk C, Reim K & Rosenmund C (2002). Total arrest of spontaneous and evoked synaptic transmission but normal synaptogenesis in the absence of Munc13-mediated vesicle priming. Proc Natl Acad Sci U S A 99, 9037-9042.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 9037-9042
    • Varoqueaux, F.1    Sigler, A.2    Rhee, J.S.3    Brose, N.4    Enk, C.5    Reim, K.6    Rosenmund, C.7
  • 49
    • 0030932857 scopus 로고    scopus 로고
    • DOC2 proteins in rat brain: Complementary distribution and proposed function as vesicular adapter proteins in early stages of secretion
    • Verhage M, de Vries KJ, Roshol H, Burbach JP, Gispen WH & Sudhof TC (1997). DOC2 proteins in rat brain: complementary distribution and proposed function as. vesicular adapter proteins in early stages of secretion. Neuron 18, 453-461.
    • (1997) Neuron , vol.18 , pp. 453-461
    • Verhage, M.1    de Vries, K.J.2    Roshol, H.3    Burbach, J.P.4    Gispen, W.H.5    Sudhof, T.C.6
  • 51
    • 0034723194 scopus 로고    scopus 로고
    • Targeting of SNAP-25 to membranes is mediated by its association with the target SNARE syntaxin
    • Vogel K, Cabaniols JP & Roche PA (2000). Targeting of SNAP-25 to membranes is mediated by its association with the target SNARE syntaxin. J Biol Chem 275, 2959-2965.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2959-2965
    • Vogel, K.1    Cabaniols, J.P.2    Roche, P.A.3
  • 53
    • 0035425203 scopus 로고    scopus 로고
    • Cysteine residues of SNAP-25 are required for SNARE disassembly and exocytosis, but not for membrane targeting
    • Washbourne P, Cansino V, Mathews JR, Graham M, Burgoyne RD & Wilson MC (2001). Cysteine residues of SNAP-25 are required for SNARE disassembly and exocytosis, but not for membrane targeting. Biochem J 357, 625-634.
    • (2001) Biochem. J. , vol.357 , pp. 625-634
    • Washbourne, P.1    Cansino, V.2    Mathews, J.R.3    Graham, M.4    Burgoyne, R.D.5    Wilson, M.C.6
  • 54
    • 0030774801 scopus 로고    scopus 로고
    • Genetic interactions between a pep7 mutation and the PEP12 and VPS45 genes: Evidence for a novel SNARE component in transport between the Saccharomyces cerevisiae Golgi complex and endosome
    • Webb GC, Hoedt M, Poole LJ & Jones EW (1997). Genetic interactions between a pep7 mutation and the PEP12 and VPS45 genes: evidence for a novel SNARE component in transport between the Saccharomyces cerevisiae Golgi complex and endosome. Genetics 147, 467-478.
    • (1997) Genetics , vol.147 , pp. 467-478
    • Webb, G.C.1    Hoedt, M.2    Poole, L.J.3    Jones, E.W.4
  • 56
    • 0028946769 scopus 로고
    • Optimization of calcium phosphate transfection for bovine chromaffin cells: Relationship to calcium phosphate precipitate formation
    • Wilson SP, Liu F, Wilson RE & Housley PR (1995). Optimization of calcium phosphate transfection for bovine chromaffin cells: relationship to calcium phosphate precipitate formation. Anal Biochem 226, 212-220.
    • (1995) Anal. Biochem. , vol.226 , pp. 212-220
    • Wilson, S.P.1    Liu, F.2    Wilson, R.E.3    Housley, P.R.4


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