메뉴 건너뛰기




Volumn 126, Issue 13, 2013, Pages 2914-2923

Tracking Ca2+-dependent and Ca2+ - Independent conformational transitions in syntaxin 1A during exocytosis in neuroendocrine cells

Author keywords

Exocytosis; FRET; PC12 cells; SNARE; Syntaxin 1A

Indexed keywords

CALCIUM ION; CYAN FLUORESCENT PROTEIN; SNARE PROTEIN; SYNAPTOBREVIN 2; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNTAXIN 1A; YELLOW FLUORESCENT PROTEIN; CALCIUM; FLUORESCENT DYE; STX1A PROTEIN, RAT; SYNTAXIN 1; VAMP2 PROTEIN, RAT;

EID: 84880690854     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.124743     Document Type: Article
Times cited : (9)

References (58)
  • 1
    • 8344255773 scopus 로고    scopus 로고
    • Tracking SNARE complex formation in live endocrine cells
    • An, S. J. and Aimers, W. (2004). Tracking SNARE complex formation in live endocrine cells. Science 306, 1042-1046.
    • (2004) Science , vol.306 , pp. 1042-1046
    • An, S.J.1    Aimers, W.2
  • 2
    • 33750580538 scopus 로고    scopus 로고
    • Movement of 'gating charge' is coupled to ligand binding in a G-protein- coupled receptor
    • Ben-Chaim, Y., Chanda, B., Dascal, N., Bezanilla, F., Parnas, I. and Parnas, H. (2006). Movement of 'gating charge' is coupled to ligand binding in a G-protein- coupled receptor. Nature 444, 106-109.
    • (2006) Nature , vol.444 , pp. 106-109
    • Ben-Chaim, Y.1    Ch, B.2    Dascal, N.3    Bezanilla, F.4    Parnas, I.5    Parnas, H.6
  • 3
    • 0034660461 scopus 로고    scopus 로고
    • Syntaxin modulation of calcium channels in cortical synaptosomes as revealed by botulinum toxin C1
    • Bergsman, J. B. and Tsien, R W. (2000). Syntaxin modulation of calcium channels in cortical synaptosomes as revealed by botulinum toxin C1. J. Neurosci. 20, 4368-4378.
    • (2000) J. Neurosci. , vol.20 , pp. 4368-4378
    • Bergsman, J.B.1    Tsien, R.W.2
  • 4
    • 77949893099 scopus 로고    scopus 로고
    • G alpha(i) and G betagamma jointly regulate the conformations of a G betagamma effector, the neuronal G protein-activated K+ channel (GIRK)
    • Berlin, S., Keren-Raifman, T., Castel, R., Rubinstein, M., Dessauer, C. W., Ivanina, T. and Dascal, N. (2010). G alpha(i) and G betagamma jointly regulate the conformations of a G betagamma effector, the neuronal G protein-activated K+ channel (GIRK). J. Biol. Chem. 285, 6179-6185.
    • (2010) J. Biol. Chem. , vol.285 , pp. 6179-6185
    • Berlin, S.1    Keren-Raifman, T.2    Castel, R.3    Rubinstein, M.4    Dessauer, C.W.5    Ivanina, T.6    Dascal, N.7
  • 5
    • 0028783997 scopus 로고
    • Functional impact of syntaxin on gating of N-type and Q-type calcium channels
    • Bezprozvanny, I., Scheller, R. H. and Tsien, R W. (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
  • 6
    • 0035312565 scopus 로고    scopus 로고
    • Structural insights into the molecular mechanism of calcium- dependent vesicle-membrane fusion
    • Brunger, A. T. (2001). Structural insights into the molecular mechanism of calcium- dependent vesicle-membrane fusion. Curr. Opin. Struct. Biol. 11, 163-173.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 163-173
    • Brunger, A.T.1
  • 7
    • 0036151862 scopus 로고    scopus 로고
    • Molecular determinants of exocytosis
    • Bruns, D. and Jahn, R. (2002). Molecular determinants of exocytosis. Pflugers Arch. 443, 333-338.
    • (2002) Pflugers Arch , pp. 333-338
    • Bruns, D.1    Jahn, R.2
  • 10
    • 43649085762 scopus 로고    scopus 로고
    • NMR analysis of the closed conformation of syntaxin-1
    • Chen, X., Lu, J., Dulubova, I. and Rizo, J. (2008). NMR analysis of the closed conformation of syntaxin-1. J. Biomol. 41, 43-54.
    • (2008) J. Biomol. , vol.41 , pp. 43-54
    • Chen, X.1    Lu, J.2    Dulubova, I.3    Rizo, J.4
  • 11
    • 0000677660 scopus 로고
    • Expression of exogenous ion channels and neurotransmitter receptors in RNA-injected Xenopus oocytes
    • Dascal,N.andLotan,I.(1992). Expression of exogenous ion channels and neurotransmitter receptors in RNA-injected Xenopus oocytes. Methods Mol. Biol. 13, 205-225.
    • (1992) Methods Mol. Biol , vol.13 , pp. 205-225
    • Dascal, N.1    Lotan, I.2
  • 12
    • 0033575749 scopus 로고    scopus 로고
    • A conformational switch in syntaxin during exocytosis: role of munc18
    • Dulubova, I., Sugita, S., Hill, S., Hosaka, M., Fernandez, I., Sudhof, T. C. and Rizo, J. (1999). A conformational switch in syntaxin during exocytosis: role of munc18. EMBOJ. 18, 4372-4382.
    • (1999) EMBOJ. , vol.18 , pp. 4372-4382
    • Dulubova, I.1    Sugita, S.2    Hill, S.3    Hosaka, M.4    Fernz, I.5    Sudhof, T.C.6    Rizo, J.7
  • 14
    • 67650865950 scopus 로고    scopus 로고
    • Simple and efficient site-directed mutagenesis using two single-primer reactions in parallel to generate mutants for protein structure-function studies
    • Edelheit, O., Hanukoglu, A. and Hanukoglu, I. (2009). Simple and efficient site-directed mutagenesis using two single-primer reactions in parallel to generate mutants for protein structure-function studies. BMC Biotechnol. 9, 61.
    • (2009) BMC Biotechnol. , vol.9 , pp. 61
    • Edelheit, O.1    Hanukoglu, A.2    Hanukoglu, I.3
  • 15
    • 80053624518 scopus 로고    scopus 로고
    • Regulation of neuronal M-channel gating in an isoform-specific manner: functional interplay between calmodulin and syntaxin 1A
    • Etzioni, A., Siloni, S., Chikvashvilli, D., Strulovich, R., Sachyani, D., Regev, N., Greitzer-Antes, D., Hirsch, J. A. and Lotan, I. (2011). Regulation of neuronal M-channel gating in an isoform-specific manner: functional interplay between calmodulin and syntaxin 1A. J. Neurosci. 31, 14158-14171.Fasshauer, D. and Margittai, M. (2004). A transient N-terminal interaction of SNAP- 25 and syntaxin nucleates SNARE assembly. J. Biol. Chem. 279, 7613-7621.
    • (2011) J. Neurosci. , vol.279 , pp. 14158-14171
    • Etzioni, A.1    Siloni, S.2    Chikvashvilli, D.3    Strulovich, R.4    Sachyani, D.5    Regev, N.6    Greitzer-Antes, D.7    Hirsch, J.A.8    Lotan, I.9
  • 16
    • 0031041456 scopus 로고    scopus 로고
    • A structural change occurs upon binding of syntaxin to SNAP-25
    • Fasshauer, D., Bruns, D., Shen, B., Jahn, R. and Brunger, A. T. (1997). A structural change occurs upon binding of syntaxin to SNAP-25. J. Biol. Chem. 272, 4582-4590.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4582-4590
    • Fasshauer, D.1    Bruns, D.2    Shen, B.3    Jahn, R.4    Brunger, A.T.5
  • 18
    • 34249742093 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer analysis of subunit assembly of the ASIC channel
    • Gao, Y., Liu, S. S., Qiu, S., Cheng, W., Zheng, J. and Luo, J. H. (2007). Fluorescence resonance energy transfer analysis of subunit assembly of the ASIC channel. Biochem. Biophys. Res. Commun. 359, 143-150.
    • (2007) , vol.359 , pp. 143-150
    • Gao, Y.1    Liu, S.S.2    Qiu, S.3    Cheng, W.4    Zheng, J.5    Luo, J.H.6
  • 20
    • 0344289516 scopus 로고    scopus 로고
    • NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin
    • Hazzard, J., Sudhof, T. C. and Rizo, J. (1999). NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin. J. Biomol. NMR 14, 203-207.
    • (1999) J. Biomol. NMR , vol.14 , pp. 203-207
    • Hazzard, J.1    Sudhof, T.C.2    Rizo, J.3
  • 21
    • 28644443374 scopus 로고    scopus 로고
    • Dynamics of receptor/G protein coupling in living cells
    • Hein, P., Frank, M., Hoffmann, C., Lohse, M. J. and Bunemann, M. (2005). Dynamics of receptor/G protein coupling in living cells. EMBO J. 24, 4106-4114.
    • (2005) EMBO J. , vol.24 , pp. 4106-4114
    • Hein, P.1    Frank, M.2    Hoffmann, C.3    Lohse, M.J.4    Bunemann, M.5
  • 23
    • 0003443746 scopus 로고    scopus 로고
    • Ion Channels ofExcitable Membranes
    • Third edition
    • Hille, B. (2001). Ion Channels ofExcitable Membranes. Third edition, pp. 603-634.
    • (2001) , pp. 603-634
    • Hille, B.1
  • 24
    • 0032737648 scopus 로고    scopus 로고
    • Molecular aspects of the excitation-contraction coupling in skeletal muscle
    • Sinauer Associates Inc. Iino, M. (1999). Molecular aspects of the excitation-contraction coupling in skeletal muscle. Jpn. J. Physiol. 49, 325-333.
    • (1999) Jpn. J. Physiol. , vol.49 , pp. 325-333
    • Sinauer Associates, Inc.1    Iino, M.2
  • 25
    • 33747622293 scopus 로고    scopus 로고
    • SNAREs - engines for membrane fusion
    • Jahn, R. and Scheller, R. H. (2006). SNAREs - engines for membrane fusion. Nat. Rev. Mol. Cell Biol. 7, 631-643.
    • (2006) Nat. Rev , vol.7 , pp. 631-643
    • Jahn, R.1    Scheller, R.H.2
  • 26
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn, R. and Sudhof, T. C. (1999). Membrane fusion and exocytosis. Annu. Rev. Biochem. 68, 863-911.
    • (1999) Annu. Rev , vol.68 , pp. 863-911
    • Jahn, R.1    Sudhof, T.C.2
  • 27
    • 77955283450 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate regulation of SNARE function in membrane fusion mediated by CAPS
    • James, D. J., Khodthong, C., Kowalchyk, J. A. and Martin, T. F. (2010). Phosphatidylinositol 4,5-bisphosphate regulation of SNARE function in membrane fusion mediated by CAPS. Adv. Enzyme Regul. 50, 62-70.
    • (2010) Adv. Enzyme Regul. , vol.50 , pp. 62-70
    • James, D.J.1    Khodthong, C.2    Kowalchyk, J.A.3    Martin, T.F.4
  • 28
    • 78650581415 scopus 로고    scopus 로고
    • Single secretory granules oflive cells recruit syntaxin-1 andsynaptosomal associated protein 25 (SNAP-25) in large copy numbers
    • Knowles, M. K., Barg, S., Wan, L., Midorikawa, M., Chen, X. and Almers, W. (2010). Single secretory granules oflive cells recruit syntaxin-1 andsynaptosomal associated protein 25 (SNAP-25) in large copy numbers. Proc. Natl. Acad. Sci. USA 107, 20810-20815.
    • (2010) Proc. Natl. Acad. Sci. US , vol.107 , pp. 20810-20815
    • Knowles, M.K.1    Barg, S.2    Wan, L.3    Midorikawa, M.4    Chen, X.5    Almers, W.6
  • 29
    • 39449106371 scopus 로고    scopus 로고
    • SNARE-catalyzed fusion events are regulated by Syntaxin1A-lipid interactions
    • Lam, A. D., Tryoen-Toth, P., Tsai, B., Vitale, N. and Stuenkel, E. L. (2008). SNARE-catalyzed fusion events are regulated by Syntaxin1A-lipid interactions. Mol. Biol. Cell 19, 485-497.
    • (2008) Mol. Biol , vol.19 , pp. 485-497
    • Lam, A.D.1    Tryoen-Toth, P.2    Tsai, B.3    Vitale, N.4    Stuenkel, E.L.5
  • 30
    • 0030715302 scopus 로고    scopus 로고
    • Voltage-dependent interaction between the muscarinic ACh receptor and proteins of the exocytic machinery
    • Linial, M., Ilouz, N. and Parnas, H. (1997). Voltage-dependent interaction between the muscarinic ACh receptor and proteins of the exocytic machinery. J. Physiol. 504, 251-258.
    • (1997) J. Physiol. , vol.504 , pp. 251-258
    • Linial, M.1    Ilouz, N.2    Parnas, H.3
  • 31
  • 32
    • 0345269748 scopus 로고    scopus 로고
    • The Habc domain and the SNARE core complex are connected by a highly flexible linker
    • Margittai, M., Fasshauer, D., Jahn, R. and Langen, R. (2003a). The Habc domain and the SNARE core complex are connected by a highly flexible linker. Biochemistry 42, 4009-4014.
    • (2003) Biochemistry , vol.42 , pp. 4009-4014
    • Margittai, M.1    Fasshauer, D.2    Jahn, R.3    Langen, R.4
  • 34
    • 34248209602 scopus 로고    scopus 로고
    • Putting the clamps on membrane fusion: how complexin sets the stage for calcium-mediated exocytosis
    • Melia, T. J., Jr (2007). Putting the clamps on membrane fusion: how complexin sets the stage for calcium-mediated exocytosis. FEBS Lett. 581, 2131-2139.
    • (2007) FEBS Lett. , vol.581 , pp. 2131-2139
    • Melia Jr., T.J.1
  • 35
    • 0141668934 scopus 로고    scopus 로고
    • Direct interaction of target SNAREs with the Kv2.1 channel. Modal regulation of channel activation and inactivation gating
    • Michaelevski, I., Chikvashvili, D., Tsuk, S., Singer-Lahat, D., Kang, Y., Linial, M., Gaisano, H. Y., Fili, O. and Lotan, I. (2003). Direct interaction of target SNAREs with the Kv2.1 channel. Modal regulation of channel activation and inactivation gating. J. Biol. Chem. 278, 34320-34330.
    • (2003) J. Biol. Chem , vol.278 , pp. 34320-34330
    • Michaelevski, I.1    Chikvashvili, D.2    Tsuk, S.3    Singer-Lahat, D.4    Kang, Y.5    Linial, M.6    Gaisano, H.Y.7    Fili, O.8    Lotan, I.9
  • 36
    • 0035918229 scopus 로고    scopus 로고
    • Self-association of the H3 region of syntaxin 1A
    • Misura, K. M., Scheller, R. H. and Weis, W. I. (2001). Self-association of the H3 region of syntaxin 1A. Implications for intermediates in SNARE complex assembly. J. Biol. Chem. 276, 13273-13282.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13273-13282
    • Misura, K.M.1    Scheller, R.H.2    Weis, W.I.3
  • 37
    • 66349122907 scopus 로고    scopus 로고
    • Clustering of syntaxin-1A in model membranes is modulated by phosphatidylinositol 4,5-bisphosphate and cholesterol
    • Murray, D. H. and Tamm, L. K. (2009). Clustering of syntaxin-1A in model membranes is modulated by phosphatidylinositol 4,5-bisphosphate and cholesterol. Biochemistry 48, 4617-4625.
    • (2009) Biochemistry , vol.48 , pp. 4617-4625
    • Murray, D.H.1    Tamm, L.K.2
  • 39
    • 7044267351 scopus 로고    scopus 로고
    • Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity
    • Okamoto, K., Nagai, T., Miyawaki, A. and Hayashi, Y. (2004). Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity. Nat. Neurosci. 7, 1104-1112.
    • (2004) Nat. Neurosci. , vol.7 , pp. 1104-1112
    • Okamoto, K.1    Nagai, T.2    Miyawaki, A.3    Hayashi, Y.4
  • 40
    • 84866093345 scopus 로고    scopus 로고
    • SNAREpinassemblybyMunc18-1 requires previous vesicle docking bysynaptotagmin I
    • Parisotto, D., Malsam, J., Scheutzow, A., Krause, J. M. and Sollner, T. H. (2012). SNAREpinassemblybyMunc18-1 requires previous vesicle docking bysynaptotagmin I. J. Biol. Chem. 287, 31041-31049.
    • (2012) J. Biol. Chem. , vol.287 , pp. 31041-31049
    • Parisotto, D.1    Malsam, J.2    Scheutzow, A.3    Krause, J.M.4    Sollner, T.H.5
  • 41
    • 0037012061 scopus 로고    scopus 로고
    • G(alpha)(i) controls the gating ofthe G protein-activated K(+) channel, GIRK
    • Peleg, S., Varon, D., Ivanina, T., Dessauer, C. W. and Dascal, N. (2002). G(alpha)(i) controls the gating ofthe G protein-activated K(+) channel, GIRK. Neuron 33, 87-99.
    • (2002) Neuron , vol.33 , pp. 87-99
    • Peleg, S.1    Varon, D.2    Ivanina, T.3    Dessauer, C.W.4    Dascal, N.5
  • 42
    • 0035913332 scopus 로고    scopus 로고
    • An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming
    • Richmond, J. E., Weimer, R. M. and Jorgensen, E. M. (2001). An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming. Nature 412, 338341.
    • (2001) Nature , vol.412 , pp. 338341
    • Richmond, J.E.1    Weimer, R.M.2    Jorgensen, E.M.3
  • 43
    • 0028922592 scopus 로고
    • Botulinum neurotoxin type C cleaves a single Lys-Ala bond within the carboxyl-terminal region of syntaxins
    • Schiavo, G., Shone, C. C., Bennett, M. K., Scheller, R. H. and Montecucco, C. (1995). Botulinum neurotoxin type C cleaves a single Lys-Ala bond within the carboxyl-terminal region of syntaxins. J. Biol. Chem. 270, 10566-10570.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10566-10570
    • Schiavo, G.1    Shone, C.C.2    Bennett, M.K.3    Scheller, R.H.4    Montecucco, C.5
  • 45
    • 3442879896 scopus 로고    scopus 로고
    • Formation, stabilisation and fusion of the readily releasable pool of secretory vesicles
    • Sorensen, J. B. (2004). Formation, stabilisation and fusion of the readily releasable pool of secretory vesicles. Pflugers Arch. 448, 347-362.
    • (2004) Pflugers Arch. , vol.448 , pp. 347-362
    • Sorensen, J.B.1
  • 46
    • 67749120188 scopus 로고    scopus 로고
    • Helical extension of the neuronal SNARE complex into the membrane
    • Stein, A., Weber, G., Wahl, M. C. and Jahn, R. (2009). Helical extension of the neuronal SNARE complex into the membrane. Nature 460, 525-528.
    • (2009) Nature , vol.460 , pp. 525-528
    • Stein, A.1    Weber, G.2    Wahl, M.C.3    Jahn, R.4
  • 47
    • 58849092285 scopus 로고    scopus 로고
    • Membrane fusion: grappling with SNARE and SM proteins
    • Sudhof, T. C. and Rothman, J. E. (2009). Membrane fusion: grappling with SNARE and SM proteins. Science 323, 474-477.
    • (2009) Science , vol.323 , pp. 474-477
    • Sudhof, T.C.1    Rothman, J.E.2
  • 48
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2
    • Sutton, R. B., Fasshauer, D., Jahn, R. and Brunger, A. T. (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
  • 49
    • 77956630627 scopus 로고    scopus 로고
    • SNARE conformational changes that prepare vesicles for exocytosis
    • Takahashi, N., Hatakeyama, H., Okado, H., Noguchi, J., Ohno, M. and Kasai, H. (2010). SNARE conformational changes that prepare vesicles for exocytosis. Cell Metab. 12, 19-29.
    • (2010) Cel , vol.12 , pp. 19-29
    • Takahashi, N.1    Hatakeyama, H.2    Okado, H.3    Noguchi, J.4    Ohno, M.5    Kasai, H.6
  • 51
    • 0037452792 scopus 로고    scopus 로고
    • Secretory granules are recaptured largely intact after stimulated exocytosis in cultured endocrine cells
    • Taraska, J. W., Perrais, D., Ohara-Imaizumi, M., Nagamatsu, S. and Almers, W. (2003). Secretory granules are recaptured largely intact after stimulated exocytosis in cultured endocrine cells. Proc. Natl. Acad. Sci. USA 100, 2070-2075.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2070-2075
    • Taraska, J.W.1    Perrais, D.2    Ohara-Imaizumi, M.3    Nagamatsu, S.4    Almers, W.5
  • 54
    • 55549123198 scopus 로고    scopus 로고
    • The structural and functional implications of linked SNARE motifs in SNAP25
    • Wang, L., Bittner, M. A., Axelrod, D. and Holz, R. W. (2008). The structural and functional implications of linked SNARE motifs in SNAP25. Mol. Biol. Cell 19, 3944-3955.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3944-3955
    • Wang, L.1    Bittner, M.A.2    Axelrod, D.3    Holz, R.W.4
  • 56
    • 34250857340 scopus 로고    scopus 로고
    • Regulation of membrane fusion in synaptic excitation-secretion coupling: speed and accuracy matter
    • Wojcik, S. M. and Brose, N. (2007). Regulation of membrane fusion in synaptic excitation-secretion coupling: speed and accuracy matter. Neuron 55, 11-24.
    • (2007) Neuron , vol.55 , pp. 11-24
    • Wojcik, S.M.1    Brose, N.2
  • 57
    • 2342554303 scopus 로고    scopus 로고
    • Stoichiometry and assembly of olfactory cyclic nucleotide-gated channels
    • Zheng, J. and Zagotta, W. N. (2004). Stoichiometry and assembly of olfactory cyclic nucleotide-gated channels. Neuron 42, 411-421.
    • (2004) Neuron , vol.42 , pp. 411-421
    • Zheng, J.1    Zagotta, W.N.2
  • 58
    • 0042336988 scopus 로고    scopus 로고
    • 2+-calmodulin modulation of cyclic nucleotide-gated channels
    • 2+-calmodulin modulation of cyclic nucleotide-gated channels. J. Neurosci. 23, 8167-8175.
    • (2003) J. Neurosci. , vol.23 , pp. 8167-8175
    • Zheng, J.1    Varnum, M.D.2    Zagotta, W.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.