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Volumn 23, Issue 4, 2004, Pages 681-689

Constitutive versus regulated SNARE assembly: A structural basis

Author keywords

EPR; Membrane fusion; SNARE

Indexed keywords

SNARE PROTEIN;

EID: 1842614413     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600083     Document Type: Article
Times cited : (33)

References (50)
  • 1
    • 0027527762 scopus 로고
    • Yeast syntaxins Sso1p and Sso2p belong to a family of related membrane proteins that function in vesicular transport
    • Aalto MK, Ronne H, Keranen S (1993) Yeast syntaxins Sso1p and Sso2p belong to a family of related membrane proteins that function in vesicular transport. EMBO J 12: 4095-4104
    • (1993) EMBO J , vol.12 , pp. 4095-4104
    • Aalto, M.K.1    Ronne, H.2    Keranen, S.3
  • 2
    • 0026766835 scopus 로고
    • Calibration of the parallax fluorescence quenching method for determination of membrane penetration depth: Refinement and comparison of quenching by spin-labeled and brominated lipids
    • Abrams FS, London E (1992) Calibration of the parallax fluorescence quenching method for determination of membrane penetration depth: refinement and comparison of quenching by spin-labeled and brominated lipids. Biochemistry 31: 5312-5322
    • (1992) Biochemistry , vol.31 , pp. 5312-5322
    • Abrams, F.S.1    London, E.2
  • 3
    • 0028346566 scopus 로고
    • A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: Application to spin-labeled mutants of bacteriorhodopsin
    • Altenbach C, Greenhalgh DA, Khorana HG, Hubbell WL (1994) A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: application to spin-labeled mutants of bacteriorhodopsin. Proc Natl Acad Sci USA 91: 1667-1671
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1667-1671
    • Altenbach, C.1    Greenhalgh, D.A.2    Khorana, H.G.3    Hubbell, W.L.4
  • 4
    • 0036166318 scopus 로고    scopus 로고
    • Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs
    • Antonin W, Fasshauer D, Becker S, Jahn R, Schneider TR (2002) Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs. Nat Struct Biol 9: 107-111
    • (2002) Nat Struct Biol , vol.9 , pp. 107-111
    • Antonin, W.1    Fasshauer, D.2    Becker, S.3    Jahn, R.4    Schneider, T.R.5
  • 5
    • 0033615054 scopus 로고    scopus 로고
    • Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles
    • Augustin I, Rosenmund C, Südhof TC, Brose N (1999) 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    Südhof, T.C.3    Brose, N.4
  • 6
    • 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, Kearns B, Champion K, Keranen S, Bankaitis V, Novick P (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
  • 7
    • 0035312565 scopus 로고    scopus 로고
    • Structural insights into the molecular mechanism of calcium-dependent vesicle-membrane fusion
    • Brunger AT (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
  • 8
    • 0036304982 scopus 로고    scopus 로고
    • 2+ sensor that triggers exocytosis?
    • 2+ sensor that triggers exocytosis? Nat Rev Mol Cell Biol 3: 498-508
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 498-508
    • Chapman, E.R.1
  • 9
    • 0023652259 scopus 로고
    • Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids
    • Chattopadhyay A, London E (1987) Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids. Biochemistry 26: 39-45
    • (1987) Biochemistry , vol.26 , pp. 39-45
    • Chattopadhyay, A.1    London, E.2
  • 12
    • 0027992040 scopus 로고
    • Yeast Snc proteins complex with Sec9. Functional interactions between putative SNARE proteins
    • Couve A, Gerst JE (1994) Yeast Snc proteins complex with Sec9. Functional interactions between putative SNARE proteins. J Biol Chem 269: 23391-23394
    • (1994) J Biol Chem , vol.269 , pp. 23391-23394
    • Couve, A.1    Gerst, J.E.2
  • 13
    • 0028070987 scopus 로고
    • Vesicle fusion from yeast to man
    • Ferro-Novick S, Jahn R (1994) Vesicle fusion from yeast to man. Nature 370: 191-193
    • (1994) Nature , vol.370 , pp. 191-193
    • Ferro-Novick, S.1    Jahn, R.2
  • 14
    • 0042160134 scopus 로고    scopus 로고
    • SNARE regulators: Matchmakers and match-breakers
    • Gerst JE (2003) SNARE regulators: matchmakers and match-breakers. Biochim Biophys Acta 1641: 99-110
    • (2003) Biochim Biophys Acta , vol.1641 , pp. 99-110
    • Gerst, J.E.1
  • 15
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson PI, Roth R, Morisaki H, Jahn R, Heuser JE (1997) Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 90: 523-535
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 16
    • 0037033997 scopus 로고    scopus 로고
    • Vesicular restriction of synaptobrevin suggests a role for calcium in membrane fusion
    • Hu K, Carroll J, Fedorovich S, Rickman C, Sukhodub A, Davletov B (2002) Vesicular restriction of synaptobrevin suggests a role for calcium in membrane fusion. Nature 415: 646-650
    • (2002) Nature , vol.415 , pp. 646-650
    • Hu, K.1    Carroll, J.2    Fedorovich, S.3    Rickman, C.4    Sukhodub, A.5    Davletov, B.6
  • 17
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • Hubbell ML, Cafiso DS, Altenbach C (2000) Identifying conformational changes with site-directed spin labeling. Nat Struct Biol 7: 735-739
    • (2000) Nat Struct Biol , vol.7 , pp. 735-739
    • Hubbell, M.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 21
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn R, Südhof TC (1999) Membrane fusion and exocytosis. Annu Rev Biochem 68: 863-911
    • (1999) Annu Rev Biochem , vol.68 , pp. 863-911
    • Jahn, R.1    Südhof, T.C.2
  • 22
    • 0032476605 scopus 로고    scopus 로고
    • Genetic and morphological analyses reveal a critical interaction between the C-termini of two SNARE proteins and a parallel four helical arrangement for the exocytic SNARE complex
    • Katz L, Hanson PI, Heuser JE, Brennwald P (1998) Genetic and morphological analyses reveal a critical interaction between the C-termini of two SNARE proteins and a parallel four helical arrangement for the exocytic SNARE complex. EMBO J 17: 6200-6209
    • (1998) EMBO J , vol.17 , pp. 6200-6209
    • Katz, L.1    Hanson, P.I.2    Heuser, J.E.3    Brennwald, P.4
  • 23
    • 0036712185 scopus 로고    scopus 로고
    • Membrane topologies of neuronal SNARE folding intermediates
    • Kim CS, Kweon DH, Shin YK (2002) Membrane topologies of neuronal SNARE folding intermediates. Biochemistry 41: 10928-10933
    • (2002) Biochemistry , vol.41 , pp. 10928-10933
    • Kim, C.S.1    Kweon, D.H.2    Shin, Y.K.3
  • 24
    • 0037162413 scopus 로고    scopus 로고
    • The membrane-dipped neuronal SNARE complex: A site-directed spin labeling electron paramagnetic resonance study
    • Kweon DH, Kim CS, Shin YK (2002) The membrane-dipped neuronal SNARE complex: a site-directed spin labeling electron paramagnetic resonance study. Biochemistry 41: 9264-9268
    • (2002) Biochemistry , vol.41 , pp. 9264-9268
    • Kweon, D.H.1    Kim, C.S.2    Shin, Y.K.3
  • 25
    • 0038413760 scopus 로고    scopus 로고
    • Insertion of the membrane-proximal region of the neuronal SNARE coiled coil into the membrane
    • Kweon DH, Kim CS, Shin YK (2003a) Insertion of the membrane-proximal region of the neuronal SNARE coiled coil into the membrane. J Biol Chem 278: 12367-12373
    • (2003) J Biol Chem , vol.278 , pp. 12367-12373
    • Kweon, D.H.1    Kim, C.S.2    Shin, Y.K.3
  • 26
    • 0038103601 scopus 로고    scopus 로고
    • Regulation of neuronal SNARE assembly by the membrane
    • Kweon DH, Kim CS, Shin YK (2003b) Regulation of neuronal SNARE assembly by the membrane. Nat Struct Biol 10: 440-447
    • (2003) Nat Struct Biol , vol.10 , pp. 440-447
    • Kweon, D.H.1    Kim, C.S.2    Shin, Y.K.3
  • 27
    • 0030807735 scopus 로고    scopus 로고
    • Structural organization of the synaptic exocytosis core complex
    • Lin RC, Scheller RH (1997) Structural organization of the synaptic exocytosis core complex. Neuron 19: 1087-1094
    • (1997) Neuron , vol.19 , pp. 1087-1094
    • Lin, R.C.1    Scheller, R.H.2
  • 28
    • 0034523701 scopus 로고    scopus 로고
    • Mechanisms of synaptic vesicle exocytosis
    • Lin RC, Scheller RH (2000) Mechanisms of synaptic vesicle exocytosis. Annu Rev Cell Dev Biol 16: 19-49
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 19-49
    • Lin, R.C.1    Scheller, R.H.2
  • 29
    • 0031576994 scopus 로고    scopus 로고
    • The membrane topology of the fusion peptide region of influenza hemagglutinin determined by spin-labeling EPR
    • Macosko JC, Kim CH, Shin YK (1997) The membrane topology of the fusion peptide region of influenza hemagglutinin determined by spin-labeling EPR. J Mol Biol 267: 1139-1148
    • (1997) J Mol Biol , vol.267 , pp. 1139-1148
    • Macosko, J.C.1    Kim, C.H.2    Shin, Y.K.3
  • 30
    • 0035253856 scopus 로고    scopus 로고
    • t-SNARE dephosphorylation promotes SNARE assembly and exocytosis in yeast
    • Marash M, Gerst JE (2001) t-SNARE dephosphorylation promotes SNARE assembly and exocytosis in yeast. EMBO J 20: 411-421
    • (2001) EMBO J , vol.20 , pp. 411-421
    • Marash, M.1    Gerst, J.E.2
  • 31
    • 0029905422 scopus 로고    scopus 로고
    • Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics
    • Mchaourab HS, Lietzow MA, Hideg K, Hubbell WL (1996) Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics. Biochemistry 35: 7692-7704
    • (1996) Biochemistry , vol.35 , pp. 7692-7704
    • Mchaourab, H.S.1    Lietzow, M.A.2    Hideg, K.3    Hubbell, W.L.4
  • 34
    • 0037040873 scopus 로고    scopus 로고
    • Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis
    • Pabst S, Margittai M, Vainius D, Langen R, Jahn R, Fasshauer D (2002) Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis. J Biol Chem 277: 7838-7848
    • (2002) J Biol Chem , vol.277 , pp. 7838-7848
    • Pabst, S.1    Margittai, M.2    Vainius, D.3    Langen, R.4    Jahn, R.5    Fasshauer, D.6
  • 35
    • 0033607279 scopus 로고    scopus 로고
    • Rapid and efficient fusion of phospholipid vesicles by the alpha-helical core of a SNARE complex in the absence of an N-terminal regulatory domain
    • Parlati F, Weber T, McNew JA, Westermann B, Sollner TH, Rothman JE (1999) Rapid and efficient fusion of phospholipid vesicles by the alpha-helical core of a SNARE complex in the absence of an N-terminal regulatory domain. Proc Natl Acad Sci USA 96: 12565-12570
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 12565-12570
    • Parlati, F.1    Weber, T.2    McNew, J.A.3    Westermann, B.4    Sollner, T.H.5    Rothman, J.E.6
  • 37
    • 0027249359 scopus 로고
    • Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae
    • Protopopov V, Govindan B, Novick P, Gerst JE (1993) Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae. Cell 74: 855-861
    • (1993) Cell , vol.74 , pp. 855-861
    • Protopopov, V.1    Govindan, B.2    Novick, P.3    Gerst, J.E.4
  • 38
    • 0028838458 scopus 로고
    • A peptide from the heptad repeat of human immunodeficiency virus gp41 shows both membrane binding and coiled-coil formation
    • Rabenstein M, Shin YK (1995) A peptide from the heptad repeat of human immunodeficiency virus gp41 shows both membrane binding and coiled-coil formation. Biochemistry 34: 13390-13397
    • (1995) Biochemistry , vol.34 , pp. 13390-13397
    • Rabenstein, M.1    Shin, Y.K.2
  • 39
    • 0036673069 scopus 로고    scopus 로고
    • SNAREs and Munc18 in synaptic vesicle fusion
    • Rizo J, Südhof 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    Südhof, T.C.2
  • 40
    • 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
  • 41
    • 0030952226 scopus 로고    scopus 로고
    • Analysis of a yeast SNARE complex reveals remarkable similarity to the neuronal SNARE complex and a novel function for the C terminus of the SNAP-25 homolog, Sec9
    • Rossi G, Salminen A, Rice LM, Brünger AT, Brennwald P (1997) Analysis of a yeast SNARE complex reveals remarkable similarity to the neuronal SNARE complex and a novel function for the C terminus of the SNAP-25 homolog, Sec9. J Biol Chem 272: 16610-16617
    • (1997) J Biol Chem , vol.272 , pp. 16610-16617
    • Rossi, G.1    Salminen, A.2    Rice, L.M.3    Brünger, A.T.4    Brennwald, P.5
  • 42
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman JE (1994) Mechanisms of intracellular protein transport. Nature 372: 55-63
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 43
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Söllner T, Bennett MK, Whiteheart SW, Scheller RH, Rothman JE (1993) A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 75: 409-418
    • (1993) Cell , vol.75 , pp. 409-418
    • Söllner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 44
    • 0037040890 scopus 로고    scopus 로고
    • Synaptotagmins: Why so many?
    • Südhof TC (2002) Synaptotagmins: why so many? J Biol Chem 277: 7629-7632
    • (2002) J Biol Chem , vol.277 , pp. 7629-7632
    • Südhof, T.C.1
  • 45
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
    • Sutton RB, Fasshauer D, Jahn R, Brunger AT (1998) Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å 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
  • 46
    • 0030029471 scopus 로고    scopus 로고
    • Direct determination of the membrane affinities of individual amino acids
    • Thorgeirsson TE, Russell CJ, King DS, Shin YK (1996) Direct determination of the membrane affinities of individual amino acids. Biochemistry 35: 1803-1809
    • (1996) Biochemistry , vol.35 , pp. 1803-1809
    • Thorgeirsson, T.E.1    Russell, C.J.2    King, D.S.3    Shin, Y.K.4
  • 48
    • 12644298688 scopus 로고    scopus 로고
    • A conserved domain is present in different families of vesicular fusion proteins: A new superfamily
    • Weimbs T, Low SH, Chapin SJ, Mostov KE, Bucher P, Hofmann K (1997) A conserved domain is present in different families of vesicular fusion proteins: a new superfamily. Proc Natl Acad Sci USA 94: 3046-3051
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3046-3051
    • Weimbs, T.1    Low, S.H.2    Chapin, S.J.3    Mostov, K.E.4    Bucher, P.5    Hofmann, K.6
  • 49
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley WC, White SH (1996) Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat Struct Biol 10: 842-848
    • (1996) Nat Struct Biol , vol.10 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 50
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • Yau WM, Wimley WC, Gawrisch K, White SH (1998) The preference of tryptophan for membrane interfaces. Biochemistry 37: 14713-14718
    • (1998) Biochemistry , vol.37 , pp. 14713-14718
    • Yau, W.M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4


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