SNAREs and SNARE regulators in membrane fusion and exocytosis

Cellular and Molecular Life Sciences

Volumn 55, Issue 5, 1999, Pages 707-734

  Gerst, J E ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

Exocytosis; Munc18; NSF; SNAP; SNAP 25; SNARE; Synaptic vesicle; Synaptobrevin VAMP; Synaptophysin; Synaptotagmin; Syntaxin

Indexed keywords

LIPID; MEMBRANE PROTEIN; PROTEIN; REGULATOR PROTEIN; SYNAPTOBREVIN; SYNAPTOPHYSIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNAPTOTAGMIN; SYNTAXIN;

EXOCYTOSIS; LIPID TRANSPORT; MEMBRANE FUSION; PROTEIN FAMILY; PROTEIN TRANSPORT; REVIEW; SYNAPSE VESICLE;

ANIMALS; EXOCYTOSIS; HUMANS; MAMMALS; MEMBRANE FUSION; MEMBRANE PROTEINS; MODELS, BIOLOGICAL; NERVE TISSUE PROTEINS; QA-SNARE PROTEINS; R-SNARE PROTEINS; SNARE PROTEINS; SYNAPTOSOMAL-ASSOCIATED PROTEIN 25; VESICULAR TRANSPORT PROTEINS; YEASTS;

EUKARYOTA;

EID: 0033065245     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050328     Document Type: Review

References (351)

1. 1 Söllner T., Whiteheart S. W., Brunner M., Erdjument B. H., Geromanos S., Tempst P. et al. (1993) SNAP receptors implicated in vesicle targeting and fusion. Nature 362: 318-324
2. 2 Rothman J. E. and Warren G. (1994) Implications of the SNARE hypothesis for intracellular membrane topology and dynamics. Curr. Biol. 4: 220-233
3. 3 Söllner T., Bennett M. K., Whiteheart S. W., Scheller R. H. and Rothman J. E. (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
4. 4 Hanson P. I., Roth R., Morisaki H., Jahn R. and Heuser J. E. (1997) Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/ deep-etch electron microscopy. Cell 90: 523-535
5. 5 Lin R. C. and Scheller R. H. (1997) Structural organization of the synaptic exocytosis core complex. Neuron 19: 1087-1094
6. 6 Jahn R. and Hanson P. I. (1998) Membrane fusion. SNAREs line up in new environment. Nature 393: 14-15
7. 7 Fasshauer D., Otto H., Eliason W. K., Jahn R. and Brunger A. T. (1997) Structural changes are associated with soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor complex formation. J. Biol. Chem. 272: 28036-28041
8. 8 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
9. 9 Rice L. M., Brennwald P. and Brunger A.T. (1997) Formation of a yeast SNARE complex is accompanied by significant structural changes. FEBS Lett. 415: 49-55
10. 10 Hanson P. I., Roth R., Morisaki H., Jahn R. and Heuser J. E. (1997) Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/ deep-etch electron microscopy. Cell 90: 523-535
11. 11 Katz L., Hanson P. I., Heuser J. E. and 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
12. 12 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 Å resolution. Nature 395: 347-353
13. 13 White J. M. (1992) Membrane fusion. Science 258: 917-924
14. 14 Hughson F. M. (1995) Molecular mechanisms of protein-mediated membrane fusion. Curr. Opin. Struct. Biol. 5: 507-513
15. 15 Hernandez L. D., Hoffman L. R., Wolfsberg T. G. and White J. M. (1996) Virus-cell and cell-cell fusion. Ann. Rev. Cell Dev. Biol. 12: 627-661
16. 16 White J. M., Danieli T., Henis Y. I., Melikyan G. and Cohen F. S. (1996) Membrane fusion by the influenza hemagglutinin: the fusion pore. Soc. Gen. Physiol. Ser. 51: 223-229
17. 17 Hughson F. M. (1997) Enveloped viruses: a common mode of membrane fusion? Curr. Biol. 7: 565-569
18. 18 Ramalho-Santos J. and de Lima M. C. (1998) The influenza virus hemagglutinin: a model protein in the study of membrane fusion. Biochim. Biophys. Acta 1376: 147-154
19. 19 Chernomordik L. V. and Zimmerberg J. (1995) Bending membranes to the task: structural intermediates in bilayer fusion. Curr. Opin. Struct. Biol. 5: 541-547
20. 20 Zimmerberg J., Vogel S. S., Whalley T., Plonsky I., Sokoloff A., Chanturia A. et al. (1995) Intermediates in membrane fusion. Cold Spring Harb. Symp. Quant. Biol. 60: 589-599
21. 21 Chernomordik L. V., Frolov V. A., Leikina E., Bronk P. and Zimmerberg J. (1998) The pathway of membrane fusion catalyzed by influenza hemagglutinin: restriction of lipids, hemifusion, and lipidic fusion pore formation. J. Cell Biol. 140: 1369-1382
22. 22 Weber T., Zemelman B. V., McNew J. A., Westermann B., Gmachl M., Parlati F. et al. (1998) SNAREpins: minimal machinery for membrane fusion. Cell 92: 759-772
23. 23 Trimble W. S., Cowan D. M. and Scheller R. H. (1988) VAMP-1: a synaptic vesicle-associated integral membrane protein. Proc. Natl. Acad. Sci. USA 85: 4538-4542
24. 24 Baumert M., Maycox P. R., Navone F., De Camilli P. and Jahn R. (1989) Synaptobrevin: an integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain. EMBO J. 8: 379-384
25. 25 Schiavo G., Benfenati F., Poulain B., Rossetto O., Polverino D. L. P., DasGupta B. R. et al. (1992) Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin. Nature 359: 832-835
26. 26 Montecucco C. and Schiavo G. (1993) Tetanus and botulism neurotoxins: a new group of zinc proteases. Trends Biochem. Sci. 18: 324-327
27. 27 Herreros J. and Blasi J. (1998) Botulinum neurotoxins and their substrates. In: Secretory Systems and Toxins, Linial M., Grasso A. and Lazarovici P. (eds), vol. 2, pp. 299-314, Harwood Academic Publishers, Amsterdam
28. 28 Montecucco C., Pellizzari R., Rossetto O., Schiavo G., Tonello F. and Washbourne P. (1998) Clostrial neurotoxins as enzymes: structure and function. In: Secretory Systems and Toxins Linial M., Grasso A. and Lazarovici P. (eds), vol. 2, pp. 315-332, Harwood Academic Publishers, Amsterdam
29. 29 Rossetto O., Schiavo G., Montecucco C., Poulain B., Deloye F., Lozzi L. et al. (1994) SNARE motif and neurotoxins. Nature 372: 415-416
30. 30 Bauerfeind R., Ohashi M. and Huttner W. B. (1994) Biogenesis of secretory granules and synaptic vesicles. Facts and hypotheses. Ann. N.Y. Acad. Sci. 733: 233-244
31. 31 Huttner W. B., Ohashi M., Kehlenbach R. H., Barr F. A., Bauerfeind R., Braunling O. et al. (1995) Bíogenesis of neurosecretory vesicles. Cold Spring Harb. Symp. Quant. Biol. 60: 315-327
32. 32 Rothman J. E. and Wieland F. T. (1996) Protein sorting by transport vesicles. Science 272: 227-234
33. 33 De Camilli P. and Mirsky R. (1997) Neuronal and glial cell biology. Curr. Opin. Neurobiol. 7: 595-597
34. 34 Betz W. J. and Angleson J. K. (1998) The synaptic vesicle cycle. Ann. Rev. Physiol. 60: 347-363
35. 35 Grote E., Hao J. C., Bennett M. K. and Kelly R. B. (1995) A targeting signal in VAMP regulating transport to synaptic vesicles. Cell 81: 581-589
36. 2+-induced insulin exocytosis. EMBO J. 15: 6951-6959
37. 37 Gerst J. E. (1997) Conserved alpha-helical segments on yeast homologs of the synaptobrevin/VAMP family of v-SNAREs mediate exocytic function. J. Biol. Chem. 272: 16591-16598
38. 38 Hayashi T., McMahon H., Yamasaki S., Binz T., Hata Y., Sudhof T. C. et al. (1994) Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly. EMBO J. 13: 5051-5061
39. 39 Hao J. C., Salem N., Peng X. R., Kelly R. B. and Bennett M. K. (1997) Effect of mutations in vesicle-associated membrane protein (VAMP) on the assembly of multimeric protein complexes. J. Neurosci. 17: 1596-1603
40. 40 Chapman E. R. and Jahn R. (1994) Calcium-dependent interaction of the cytoplasmic region of synaptotagmin with membranes. Autonomous function of a single C2-homologous domain. J. Biol. Chem. 269: 5735-5741
41. 41 Chapman E. R., An S., Barton N. and Jahn R. (1994) SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils. J. Biol. Chem. 169: 27427-27432
42. 42 Calakos N., Bennett M. K., Peterson K. E. and Scheller R. H. (1994) Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking. Science 263: 1146-1149
43. 43 Hayashi T., Yamasaki S., Nauenburg S., Binz T. and Niemann H. (1995) Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro. EMBO J. 14: 2317-2325
44. 44 Kee Y., Lin R. C., Hsu S. C. and Scheller R. H. (1995) Distinct domains of syntaxin are required for synaptic vesicle fusion complex formation and dissociation. Neuron 14: 991-998
45. 45 Fasshauer D., Eliason W. K., Brunger A. T. and Jahn R. (1998) Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly. Biochemistry 37: 10354-10362
46. 46 Regazzi R., Wollheim C. B., Lang J., Theler J. M., Rossetto O., Montecucco C. et al. (1995) VAMP-2 and cellubrevin are expressed in pancreatic beta-cells and are essential for Ca(2 + ) but not for GTP gamma S-induced insulin secretion. EMBO J. 14: 2723-2730
47. 47 Gaisano H. Y., Sheu L., Foskett J. K. and Trimble W. S. (1994) Tetanus toxin light chain cleaves a vesicle-associated membrane protein (VAMP) isoform 2 in rat pancreatic zymogen granules and inhibits enzyme secretion. J. Biol. Chem. 269: 17062-17066
48. 48 Misonou H., Ohara-Imaizumi M. and Kumakura K. (1997) Regulation of the priming of exocytosis and the dissociation of SNAP-25 and VAMP-2 in adrenal chromaffin cells. Neurosci. Lett. 232: 182-184
49. 49 Olson A. L., Knight J. B. and Pessin J. E. (1997) Syntaxin 4, VAMP2 and/or VAMP3/cellubrevin are functional target membrane and vesicle SNAP receptors for insulin-stimulated GLUT4 translocation in adipocytes. Mol. Cell. Biol. 17: 2425-2435
50. 50 Elferink L. A., Trimble W. S. and Scheller R. H. (1989) Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system. J. Biol. Chem. 264: 11061-11064
51. 51 Martin S., Tellam J., Livingstone C., Slot J. W., Gould G. W. and James D. E. (1996) The glucose transporter (GLUT-4) and vesicle-associated membrane protein-2 (VAMP-2) are segregated from recycling endosomes in insulin-sensitive cells. J. Cell Biol. 134: 625-635
52. 52 Calhoun B. C. and Goldenring J. R. (1997) Two Rab proteins, vesicle-associated membrane protein 2 (VAMP-2) and secretory carrier membrane proteins (SCAMPs), are present on immunoisolated parietal cell tubulovesicles. Biochem. J. 325: 559-564
53. 53 Nielsen S., Marples D., Birn H., Mohtashami M., Dalby N. O., Trimble M. et al. (1995) Expression of VAMP-2-like protein in kidney collecting duet intracellular vesicles. Colocalization with Aquaporin-2 water channels. J. Clin. Invest. 96: 1834-1844
54. 54 Rossetto O., Gorza L., Schiavo G., Schiavo N., Scheller R. H. and Montecucco C. (1996) VAMP/synaptobrevin isoforms 1 and 2 are widely and differentially expressed in nonneuronal tissues. J. Cell Biol. 132: 167-179
55. 55 Tamori Y., Hashiramoto M., Araki S., Kamata Y., Takahashi M., Kozaki S. et al. (1996) Cleavage of vesicle-associated membrane protein (VAMP)-2 and cellubrevin on GLUT4-containing vesicles inhibits the translocation of GLUT4 in 3T3-L1 adipocytes. Biochem. Biophys. Res. Commun. 220: 740-745
56. 56 Papini E., Rossetto O. and Cutler D. F. (1995) Vesicle-associated membrane protein (VAMP)/synaptobrevin-2 is associated with dense core secretory granules in PC12 neuroendocrine cells. J. Biol. Chem. 270: 1332-1336
57. 57 Mandic R., Trimble W. S. and Lowe A. W. (1997) Tissue-specific alternative RNA splicing of rat vesicle-associated membrane protein-1 (VAMP-1). Gene 199: 173-179
58. 58 Isenmann S., Khew-Goodall Y., Gamble J., Vadas M. and Wattenberg B. W. (1998) A splice-isoform of vesicle-associated membrane protein-1 (VAMP-1) contains a mitochondrial targeting signal. Mol. Biol. Cell 9: 1649-1660
59. 59 McMahon H. T., Ushkaryov Y. A., Edelmann L., Link E., Binz T., Niemann H. et al. (1993) Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion protein. Nature 364: 346-394
60. 60 Galli T., Zahraoui A., Vaidyanathan V. V., Raposo G., Tain J. M., Karin M. et al. (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
61. 61 Aledo J. C., Hajduch E., Darakhshan F. and Hundal H. S. (1996) Analyses of the co-localization of cellubrevin and the GLUT4 glucose transporter in rat and human insulin-responsive tissues. FEBS Lett. 395: 211-216
62. 62 Volchuk A., Mitsumoto Y., He L., Liu Z., Habermann E., Trimble W. et al. (1994) Expression of vesicle-associated membrane protein 2 (VAMP-2)/synaptobrevin II and cellubrevin in rat skeletal muscle and in a muscle cell line. Bioehem. J. 304: 139-145
63. 63 Sengupta D., Gumkowski F. D., Tang L. H., Chilcote T. J. and Jamieson J. D. (1996) Localization of cellubrevin to the Golgi complex in pancreatic acinar cells. Eur. J. Cell Biol. 70: 306-314
64. 64 Franki N., Macaluso F., Gao Y. and Hays R. M. (1995) Vesicle fusion proteins in rat inner medullary collecting duct and amphibian bladder. Am. J. Physiol. 268: 792-797
65. 65 Chilcote T. J., Galli T., Mundigl O., Edelmann L., McPherson P. S., Takei K. et al. (1995) Cellubrevin and synaptobrevins: similar subcellular localization and biochemical properties in PC12 cells. J. Cell Biol. 129: 213-231
66. 66 Galli T., Chilcote T., Mundigl O., Binz T., Niemann H. and 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
67. 67 Galli C., Piccini A., Ciotti M. T., Castellani L., Calissano P., Zaccheo D. et al. (1998) Increased amyloidogenic secretion in cerebellar granule cells undergoing apoptosis. Proc. Natl. Acad. Sci. USA 95: 1247-1252
68. 68 Braun J. E., Fritz B. A., Wong S. M. and Lowe A. W. (1994) Identification of a vesicle-associated membrane protein (VAMP)-like membrane protein in zymogen granules of the rat exocrine pancreas. J. Biol. Chem. 269: 5328-5335
69. 69 Advani R. J., Bae H. R., Bock J. B., Chao D. S., Doung Y. C., Prekeris R. et al. (1998) Seven novel mammalian SNARE proteins localize to distinct membrane compartments. J. Biol. Chem. 273: 10317-10324
70. 70 Wong S. H., Zhang T., Xu Y., Subramaniam V. N., Griffiths G. and Hong W. (1998) Endobrevin, a novel synaptobrevin/VAMP-like protein preferentially associated with the early endosome. Mol. Biol. Cell 9: 1549-1563
71. 71 Zeng Q., Subramaniam V. N., Wong S. H., Tang B. L., Parton R. G., Rea S. et al. (1998) A novel synaptobrevin/ VAMP homologous protein (VAMP5) is increased during in vitro myogenesis and present in the plasma membrane. Mol. Biol. Cell 9: 2423-2437
72. 72 Gerst J. E., Rodgers L., Riggs M. and Wigler M. (1992) SNC1, a yeast homolog of the synaptic vesicle-associated membrane protein/synaptobrevin gene family: genetic interactions with the RAS and CAP genes. Proc. Natl. Acad. Sci. USA 89: 4338-4342
73. 73 Protopopov V., Govindan B., Novick P. and Gerst J. E. (1993) Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. ceretisiae. Cell 74: 855-861
74. 74 Lustgarten V. and Gerst J. E. (1998) Yeast VSM1 encodes a v-SNARE binding protein that may act as a negative regulator of constitutive exocytosis. Mol. Cell Biol., in press
75. 75 David D., Sundarababu S. and Gerst J. E. (1998) Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeast. J. Cell Biol. 143: 1167-1182
76. 76 Rossi G., Salminen A., Rice L. M., Brunger A. T. and 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
77. 77 Brennwald P., Kearns B., Champion K., Keranen S., Bankaitis V. and 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
78. 78 Aalto M. K., Ronne H. and 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
79. 79 Couve A. and Gerst J. E. (1994) Yeast Snc proteins complex with Sec9. Functional interactions between putative SNARE proteins. J. Biol. Chem. 269: 23391-23394
80. 80 Couve A., Protopopov V. and Gerst J. E. (1995) Yeast synaptobrevin homologs are modified posttranslationally by the addition of palmitate. Proc. Natl. Acad. Sci. USA 92: 5987-5991
81. 81 Gerst J. E. (1998) unpublished results
82. 82 Ferro-Novick S. and Jahn R. (1994) Vesicle fusion from yeast to man. Nature 370: 191-193
83. 83 Bennett M. K. and Scheller R. H. (1993) The molecular machinery for secretion is conserved from yeast to neurons. Proc. Natl. Acad. Sci. USA 90: 2559-2563
84. 84 Nonet M. L., Saifee O., Zhao H., Rand J. B. and Wei L. (1998) Synaptic transmission deficits in Caenorhabditis elegans synaptobrevin mutants. J. Neurosci. 18: 70-80
85. 85 Sweeney S. T., Broadie K., Keane J., Niemann H. and O'Kane C. J. (1995) Targeted expression of tetanus toxin light chain in Drosophila specifically eliminates synaptic transmission and causes behavioral defects. Neuron 14: 341-351
86. 86 Sudhof T. C., Baumert M., Perin M. S. and Jahn R. (1989) A synaptic vesicle membrane protein is conserved from mammals to Drosophila. Neuron 2: 1475-1481
87. 87 Schiavo G., Gmachl M. J., Stenbeck G., Sollner T. H. and Rothman J. E. (1995) A possible docking and fusion particle for synaptic transmission. Nature 378: 733-736
88. 88 Schiavo G., Stenbeck G., Rothman J. E. and Sollner T. H. (1997) Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses. Proc. Natl. Acad. Sci. USA 94: 997-1001
89. 89 Deitcher D. L., Ueda A., Stewart B. A., Burgess R. W., Kidokoro Y. and Schwarz T. L. (1998) Distinct requirements for evoked and spontaneous release of neurotransmitter are revealed by mutations in the Drosophila gene neuronal-synaptobrevin. J. Neurosci. 18: 2028-2039
90. 90 Bennett M. K., Calakos N. and Scheller R. H. (1992) Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Science 257: 255-259
91. 91 Inoue A., Obata K. and Akagawa K. (1992) Cloning and sequence analysis of cDNA for a neuronal cell membrane antigen, HPC-I. J. Biol. Chem. 267: 10613-10619
92. 92 Bennett M. K., Garcia-Arraras J. E., Elferink L. A., Peterson K., Fleming A. M., Hazuka C. D. et al. (1993) The syntaxin family of vesicular transport receptors. Cell 74: 863-873
93. 93 Jagadish M. N., Tellam J. T., Macaulay S. L., Gough K. H., James D. E. and Ward C. W. (1997) Novel isoform of syntaxin 1 is expressed in mammalian cells. Biochem. J. 321: 151-156
94. 94 Nagamatsu S., Fujiwara T., Nakamichi Y., Watanabe T., Katahira H., Sawa H. et al. (1996) Expression and functional role of syntaxin 1/HPC-I in pancreatic beta cells. Syntaxin 1A, but not 1B, plays a negative role in regulatory insulin release pathway. J. Biol. Chem. 27: 1160-1165
95. 95 Delgrossi M. H., Breuza L., Mirre C., Chavrier P. and Le-Bivic A. (1997) Human syntaxin 3 is localized apically in human intestinal cells. J. Cell Sci. 110: 2207-2214
96. 96 Peng X. R., Yao X., Chow D. C., Forte J. G. and Bennett M. K. (1997) Association of syntaxin 3 and vesicle-associated membrane protein (VAMP) with H + /K( + )-ATPase-containing tubulovesicles in gastric parietal cells. Mol. Biol. Cell 8: 399-407
97. 97 Fujita H., Tuma P. L., Finnegan C. M., Locco L. and Hubbard A. L. (1998) Endogenous syntaxins 2, 3 and 4 exhibit distinct but overlapping patterns of expression at the hepatocyte plasma membrane. Biochem. J. 329: 527-538
98. 98 Mandon B., Chou C. L., Nielsen S. and Knepper M. A. (1996) Syntaxin-4 is localized to the apical plasma membrane of rat renal collecting duct cells: possible role in aquaporin-2 trafficking. J. Clin. Invest. 98: 906-913
99. 99 Gaisano H. Y., Ghai M., Malkus P. N., Sheu L., Bouquillon A., Bennett M. K. et al. (1996) Distinct cellular locations of the syntaxin family of proteins in rat pancreatic acinar cells. Mol. Biol. Cell 7: 2019-2027
100. 100 Low S. H., Chapin S. J., Weimbs T., Komuves L. G., Bennett M. K. and Mostov K. E. (1996) Differential localization of syntaxin isoforms in polarized Madin-Darby canine kidney cells. Mol. Biol. Cell 7: 2007-2018
101. 101 Volchuk A., Wang Q., Ewart H. S., Liu Z., He L., Bennett M. K. et al. (1996) Syntaxin 4 in 3T3-L1 adipocytes: regulation by insulin and participation in insulin-dependent glucose transport. Mol. Biol. Cell 7: 1075-1082
102. 102 Nicholson K. L., Munson M., Miller R. B., Filip T. J., Fairman R. and Hughson F. M. (1998) Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p. Nature Struct. Biol. 5: 793-802
103. 103 Zhong P., Chen Y. A., Tam D., Chung D., Scheller R. H. and Miljanich G. P. (1997) An alpha-helical minimal binding domain within the H3 domain of syntaxin is required for SNAP-25 binding. Biochemistry 36: 4317-4326
104. 104 Hanson P. I., Otto H., Barton N. and Jahn R. (1995) The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin. J. Biol. Chem. 270: 16955-16961
105. 105 McMahon H. T. and Sudhof T. C. (1995) Synaptic core complex of synaptobrevin, syntaxin, and SNAP25 forms high affinity alpha-SNAP binding site. J. Biol. Chem. 270: 2213-2217
106. 106 el Far O, Charvin N, Leveque C., Martin-Moutot N., Takahashi M. and Seagar M. J. (1995) Interaction of a synaptobrevin (VAMP)-syntaxin complex with presynaptic calcium channels. FEBS Lett. 36: 101-105
107. 107 Sheng Z. H., Rettig J., Cook T. and Catterall W. A. (1996) Calcium-dependent interaction of N-type calcium channels with the synaptic core complex. Nature 379: 451-454
108. 108 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
109. 109 Naren A. P., Nelson D. J., Xie W., Jovov B., Pevsner J., Bennett M. K. et al. (1997) Regulation of CFTR chloride channels by syntaxin and Munc18 isoforms. Nature 390: 302-305
110. 2 + regulates the interaction between synaptotagmin and syntaxin. J. Biol. Chem. 1: 23667-23671
111. 2 + -dependent electrostatic switch. Neuron 18: 133-142
112. 112 Ravichandran V., Chawla A., and Roche P. A. (1996) Identification of a novel syntaxin-and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues. J. Biol. Chem. 271: 1330-13303
113. 113 Wang G., Witkin J. W., Hao G., Bankaitis V. A., Scherer P. E. and Baldini G. (1997) Syndet is a novel SNAP-25 related protein expressed in many tissues. J. Cell Sci. 110: 505-513
114. 114 Garcia E. P., Gatti E., Butler M., Burton J. and De Camilli P. (1994) A rat brain See1 homologue related to Rop and UNC18 interacts with syntaxin. Proc. Natl. Acad. Sci. USA 91: 2003-2007
115. 115 Pevsner J., Hsu S. C., Braun J. E., Calakos N., Ting A. E., Bennett M. K. et al. (1994) Specificity and regulation of a synaptic vesicle docking complex. Neuron 13: 353-361
116. 116 Fujita Y., Sasaki T., Fukui K., Kotani H., Kimura T., Hata Y. et al. (1996) Phosphorylation of Munc-18/n-Sec1/rbSec1 by protein kinase C: its implication in regulating the interaction of Munc-18/n-Sec1/rbSec1 with syntaxin. J. Biol. Chem. 271: 7265-7268
117. 117 Betz A., Okamoto M., Benseler F. and 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
118. 2( + )-sensitive manner. Cell 90: 325-333
119. 119 Saifee O., Wei L. and Nonet M. L. (1998) The Caenorhabditis elegans unc-64 locus encodes a syntaxin that interacts genetically with synaptobrevin. Mol. Biol. Cell 9: 1235-1252
120. 120 Ogawa H., Harada S., Sassa T., Yamamoto H. and Hosono R. (1998) Functional properties of the unc-64 gene encoding a Caenorhabditis elegans syntaxin. J. Biol. Chem. 273: 2192-2198
121. 121 Schulze K. L., Broadie K., Perin M. S. and Bellen H. J. (1995) Genetic and electrophysiological studies of Drosophila syntaxin-1A demonstrate its role in nonneuronal secretion and neurotransmission. Cell 80: 311-320
122. 122 Cerezo J. R., Jimenez F. and Moya F. (1995) Characterization and gene cloning of Drosophila syntaxin 1 (DsyntI): the fruit fly homologue of rat syntaxin 1. Mol. Brain Res. 29: 245-252
123. 123 Broadie K., Prokop A., Bellen H. J., O'Kane C. J., Schulze K. L. and Sweeney S. T. (1995) Syntaxin and synaptobrevin function downstream of vesicle docking in Drosophila. Neuron 15: 663-673
124. 124 Burgess R. W., Deitcher D. L. and Schwarz T. L. (1997) The synaptic protein syntaxin1 is required for cellularization of Drosophila embryos. J. Cell Biol. 138: 861-875
125. 125 Oyler G. A., Higgins G. A., Hart R. A., Battenberg E., Billingsley M., Bloom F. E. et al. (1989) The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations. J. Cell Biol. 109: 3039-3052
126. 126 Bark L. C., Hahn K. M., Ryabinin A. E. and Wilson M. C. (1995) Differential expression of SNAP-25 protein isoforms during divergent vesicle fusion events of neural development. Proc. Natl. Acad. Sci. USA 92: 1510-1514
127. 127 Roth D. and Burgoyne R. D. (1994) SNAP-25 is present in a SNARE complex in adrenal chromaffin cells. FEBS Lett. 351: 207-210
128. 128 Sadoul K., Lang J., Montecucco C., Weller U., Regazzi R., Catsicas S. et al. (1995) SNAP-25 is expressed in islets of Langerhans and is involved in insulin release. J. Cell Biol. 128: 1019-1028
129. 129 Jagadish M. N., Fernandez C. S., Hewish D. R., Macaulay S. L., Gough K. H., Grusovin J. et al. (1996) Insulin-responsive tissues contain the core complex protein SNAP-25 (synaptosomal-associated protein 25) A and B isoforms in addition to syntaxin 4 and synaptobrevins 1 and 2. Biochem. J. 317: 945-954
130. 130 Kannan R., Grant N. J., Aunis D. and Langley K. (1996) SNAP-25 is differentially expressed by noradrenergic and adrenergic chromaffin cells. FEBS Lett. 385: 159-164
131. 131 Blasi J., Chapman E. R., Link E., Binz T., Yamasaki S., DeCamilli P. et al. (1993) Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-25. Nature 365: 160-163
132. 132 Lawrence G. W., Foran P. and Dolly J. O. (1996) Distinct exocytotic responses of intact and permeabilised chromaffin cells after cleavage of the 25-kDa synaptosomal-associated protein (SNAP-25) or synaptobrevin by botulinum toxin A or B. Eur. J. Biochem. 236: 877-886
133. 2 + -dependent exocytosis. J. Biol. Chem. 271: 20227-20230
134. 134 Osen-Sand A., Catsicas M., Staple J. K., Jones K. A., Ayala G., Knowles J. et al. (1993) Inhibition of axonal growth by SNAP-25 antisense oligonucleotides in vitro and in vivo. Nature 364: 445-448
135. 135 Gutierrez L. M., Canaves J. M., Ferrer-Montiel A. V., Reig J. A., Montal M. and Viniegra S. (1995) A peptide that mimics the carboxy-terminal domain of SNAP-25 blocks Ca(2 + )-dependent exocytosis in chromaffin cells. FEBS Lett. 372: 39-43
136. 136 Gutierrez L. M., Viniegra S., Rueda J., Ferrer-Montiel A. V., Canaves J. M. and Montal M. (1997) A peptide that mimics the C-terminal sequence of SNAP-25 inhibits secretory vesicle docking in chromaffin cells. J. Biol. Chem. 272: 2634-2639
137. 137 Veit M., Sollner T. H. and Rothman J. E. (1996) Multiple palmitoylation of synaptotagmin and the t-SNARE SNAP-25. FEBS Lett. 385: 119-123
138. 138 Lane S. R. and Liu Y. (1997) Characterization of the palmitoylation domain of SNAP-25. J. Neurochem. 69: 1864-1869
139. 139 Garcia E. P., McPherson P. S., Chilcote T. J., Takei K. and De Camilli P. (1995) rbSec1A and B colocalize with syntaxin 1 and SNAP-25 throughout the axon, but are not in a stable complex with syntaxin. J. Cell Biol. 129: 105-120
140. 140 Walch-Solimena C., Blasi J., Edelmann L., Chapman E. R., von-Mollard G. F. and Jahn R. (1995) The t-SNAREs syntaxin 1 and SNAP-25 are present on organelles that participate in synaptic vesicle recycling. J. Cell Biol. 128: 637-645
141. 2 + channels with the presynaptic proteins syntaxin and SNAP-25. Proc. Natl. Acad. Sci. USA 93: 7363-7368
142. 142 Yokoyama C. T., Sheng Z. H. and Catterall W. A. (1997) Phosphorylation of the synaptic protein interaction site on N-type calcium channels inhibits interactions with SNARE proteins. J. Neurosci. 17: 6929-6938
143. 2 + channels. EMBO J. 15: 4100-4110
144. 144 Zhou J. and Egan J. M. (1997) SNAP-25 is phosphorylated by glucose and GLP-1 in RIN 1046-38 cells. Biochem. Biophys. Res. Commun. 238: 297-300
145. 145 Hirling H. and Scheller R. H. (1996) Phosphorylation of synaptic vesicle proteins: modulation of the alpha SNAP interaction with the core complex. Proc. Natl. Acad. Sci. USA 93: 11945-11949
146. 146 Shimazaki Y., Nishiki T., Omori A., Sekiguchi M., Kamata Y., Kozaki S. et al. (1996) Phosphorylation of 25-kDa synaptosome-associated protein. Possible involvement in protein kinase C-mediated regulation of neurotransmitter release. J. Biol. Chem. 271: 14548-14553
147. 147 Chen F., Foran P., Shone C. C., Foster K. A., Melling J. and Dolly J. O. (1997) Botulinum neurotoxin B inhibits insulin-stimulated glucose uptake into 3T3-I.1 adipocytes and cleaves cellubrevin unlike type A toxin which failed to proteolyze the SNAP-23 present. Biochemistry 36: 5719-5728
148. 148 Sadoul K., Berger A., Niemann H., Weller U., Roche P. A., Klip A. et al. (1997) SNAP-23 is not cleaved by botulinum neurotoxin E and can replace SNAP-25 in the process of insulin secretion. J. Biol. Chem. 272: 33023-33037
149. 149 Leung S. M., Chen D., DasGupta B. R., Whiteheart S. W. and Apodaca G. (1998) SNAP-23 requirement for transferrin recycling in Streptolysin-O-permeabilized Madin-Darby canine kidney cells. J. Biol. Chem. 273: 17732-17741
150. 150 Guo Z., Turner C. and Castle D. (1998) Relocation of the t-SNARE SNAP-23 from lamellipodia-like cell surface projections regulates compound exocytosis in mast cells. Cell 94: 537-548
151. 151 Rea S., Martin L. B., McIntosh S., Macaulay S. L., Ramsdale T., Baldini G. et al. (1998) Syndet, an adipocyte target SNARE involved in the insulin-induced translocation of GLUT4 to the cell surface. J. Biol. Chem. 273: 18784-18792
152. 152 Washbourne P., Pellizzari R., Baldini G., Wilson M. C. and Montecucco C. (1997) Botulinum neurotoxin types A and E require the SNARE motif in SNAP-25 for proteolysis. FEBS Lett. 418: 1-5
153. 153 Novick P., Field C. and Schekman R. (1980) Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell 21: 205-215
154. 154 Risinger C., Deitcher D. L., Lundell I., Schwarz T. L. and Larhammar D. (1997) Complex gene organization of synaptic protein SNAP-25 in Drosophila melanogaster. Gene 194: 169-177
155. 155 Perin M. S., Brose N., Jahn R. and Sudhof T. C. (1991) Domain structure of synaptotagmin (p65). J. Biol. Chem. 266: 623-629
156. 156 Geppert M., Archer B. T. and Sudhof T. C. (1991) Synaptotagmin II. A novel differentially distributed form of synaptotagmin. J. Biol. Chem. 266: 13548-13552
157. 157 Mizuta M., Inagaki N., Nemoto Y., Matsukura S., Takahashi M. and Scino S. (1994) Synaptotagmin III is a novel isoform of rat synaptotagmin expressed in endocrine and neuronal cells. J. Biol. Chem. 269: 11675-11678
158. 158 Craxton M., Olsen A. and Goedert M. (1997) Human synaptotagmin V (SYT5): sequence, genomic structure, and chromosomal location. Genomics 42: 165-169
159. 159 Hudson A. W. and Birnbaum M. J. (1995) Identification of a nonneuronal isoform of synaptotagmin. Proc. Natl. Acad. Sci. USA 92: 5895-5899
160. 160 Perin M. S., Johnston P. A., Ozcelik T., Jahn R., Francke U. and Sudhof T. C. (1991) Structural and functional conservation of synaptotagmin (p65) in Drosophila and humans. J. Biol. Chem. 266: 615-622
161. 2 + -dependent phospholipid binding to the C2A domain of synaptotagmin IV. J. Biol. Chem. 271: 8430-8434
162. 162 Niinobe M., Yamaguchi Y., Fukuda M. and Mikoshiba K. (1994) Synaptotagmin is an inositol polyphosphate binding protein: isolation and characterization as an Ins 1,3,4,5-P4 binding protein. Biochem. Biophys. Res. Commun. 205: 1036-1042
163. 163 Fukuda M., Aruga J., Niinobe M., Aimoto S. and Mikoshiba K. (1994) Inositol-1,3,4,5-tetrakisphosphate binding to C2B domain of IP4BP/synaptotagmin II. J. Biol. Chem. 269: 29206-29211
164. 164 Schiavo G., Gu Q. M., Prestwich G. D., Sollner T. H. and Rothman J. E. (1996) Calcium-dependent switching of the specificity of phosphoinositide binding to synaptotagmin. Proc. Natl. Acad. Sci. USA 93: 13327-13332
165. 2 + regulates the interaction between synaptotagmin and syntaxin 1. J. Biol. Chem. 270: 23667-23671
166. 2 + -triggered dimerization. J. Biol. Chem. 271: 5844-5849
167. 167 Sugita S., Hata Y. and Sudhof T. C. (1996) Distinct Ca(2 + )-dependent properties of the first and second C2-domains of synaptotagmin I. J. Biol. Chem. 271: 1262-1265
168. 168 Schivell A. E., Batchelor R. H. and Bajjalieh S. M. (1996) Isoform-specific, calcium-regulated interaction of the synaptic vesicle proteins SV2 and synaptotagmin. J. Biol. Chem. 271: 27770-27775
169. 169 Petrenko A. G., Perin M. S., Davletov B. A., Ushkaryov Y. A., Geppert M. and Sudhof T. C. (1991) Binding of synaptotagmin to the alpha-latrotoxin receptor implicates both in synaptic vesicle exocytosis. Nature 353: 65-68
170. 170 Leveque C., el Far O., Martin-Moutot N., Sato K., Kato R., Takahashi M. et al. (1994) Purification of the N-type calcium channel associated with syntaxin and synaptotagmin. A complex implicated in synaptic vesicle exocytosis. J. Biol. Chem. 269: 6306-6312
171. 171 Charvin N., L'Eveque C., Walker D., Berton F., Raymond C., Kataoka M. et al. (1997) Direct interaction of the calcium sensor protein synaptotagmin I with a cytoplasmic domain of the alpha1A subunit of the P/Q-type calcium channel. EMBO J. 16: 4591-4596
172. 2 + channels with the C2B domain of synaptotagmin I. Proc. Natl. Acad. Sci. USA 94: 5405-5410
173. 173 Brose N., Petrenko A. G., Sudhof T. C. and Jahn R. (1992) Synaptotagmin: a calcium sensor on the synaptic vesicle surface. Science 256: 1021-1025
174. 174 Elferink L. A., Peterson M. R. and Scheller R. H. (1993) A role for synaptotagmin (p65) in regulated exocytosis. Cell 72: 153-159
175. 2 + sensor for transmitter release at a central synapse. Cell 79: 717-727
176. 176 Kelly R. B. (1995) Neural transmission. Synaptotagmin is just a calcium sensor. Curr. Biol. 5: 257-259
177. 177 Shoji-Kasai Y., Yoshida A., Sato K., Hoshino T., Ogura A., Kondo S. et al. (1992) Neurotransmitter release from synaptotagmin-deficient clonal variants of PC12 cells. Science 256: 1821-1823
178. 178 Littleton J. T., Stern M., Schulze K., Perin M. and Bellen H. J. (1993) Mutational analysis of Drosophila synaptotagmin demonstrates its essential role in Ca(2 + )-activated neurotransmitter release [see comments]. Cell 74: 1125-1134
179. 179 Littleton J. T., Stern M., Perin M. and Bellen H. J. (1994) Calcium dependence of neurotransmitter release and rate of spontaneous vesicle fusions are altered in Drosophila synaptotagmin mutants. Proc. Natl. Acad. Sci. USA 91: 10888-10892
180. 180 Broadie K., Bellen H. J., DiAntonio A., Littleton J. T. and Schwarz T. L. (1994) Absence of synaptotagmin disrupts excitation-secretion coupling during synaptic transmission. Proc. Natl. Acad. Sci. USA 91: 10727-10731
181. 181 DiAntonio A. and Schwarz T. L. (1994) The effect on synaptic physiology of synaptotagmin mutations in Drosophila. Neuron 12: 909-920
182. 182 Nonet M. L., Grundahl K., Meyer B. J. and Rand J. B. (1993) Synaptic function is impaired but not eliminated in C. elegans mutants lacking synaptotagmin. Cell 73: 1291 -1305
183. 183 Bommert K., Charlton M. P., DeBello W. M., Chin G. J., Betz H. and Augustine G. J. (1993) Inhibition of neurotransmitter release by C2-domain peptides implicates synaptotagmin in exocytosis. Nature 363: 163-165
184. 184 Lang J., Fukuda M., Zhang H., Mikoshiba K. and Wollheim C. B. (1997) The first C2 domain of synaptotagmin is required for exocytosis of insulin from pancreatic beta-cells: action of synaptotagmin at low micromolar calcium. EMBO J. 16: 5837-5846
185. 185 Mikoshiba K., Fukuda M., Moreira J. E., Lewis F. M., Sugimori M., Niinobe M. et al. (1995) Role of the C2A domain of synaptotagmin in transmitter release as determined by specific antibody injection into the squid giant synapse preterminal. Proc. Natl. Acad. Sci. USA 92: 10703-10707
186. 186 Geppert M. and Sudhof T. C. (1998) RAB3 and synaptotagmin: the yin and yang of synaptic membrane fusion. Ann. Rev. Neurosci. 21: 75-95
187. 187 Sudlow A. W., McFerran B. W., Bodill H., Barnard R. J., Morgan A. and Burgoyne R. D. (1996) Similar effects of alpha-and beta-SNAP on Ca(2 + )-regulated exocytosis. FEBS Lett. 393: 185-188
188. 188 Mayer A., Wickner W. and Haas A. (1996) Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles. Cell 85: 83-94
189. 189 Otto H., Hanson P. I. and Jahn R. (1997) Assembly and disassembly of a ternary complex of synaptobrevin, syntaxin, and SNAP-25 in the membrane of synaptic vesicles. Proc. Natl. Acad. Sci. USA 94: 6197-6201
190. 190 Ungermann C., Nichols B. J., Pelham H. R. and Wickner W. (1998) A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion. J. Cell Biol. 140: 61-69
191. 191 Swanton E., Sheehan J., Bishop N., High S. and Woodman P. (1998) Formation and turnover of NSF-and SNAP-containing 'Fusion' complexes occur on undocked, clathrin-coated vesicle-derived membranes [In Process Citation]. Mol. Biol. Cell 9: 1633-1647
192. 192 Gerst J. E. (1998) Vesicular trafficking on the late secretory pathway in the budding yeast, S. cerevisiae. In: Secretory Systems and Toxins, Linial M., Grasso A., Lazarovici P., (eds), pp. 81-108, Harwood Academic Publishers, Amsterdam
193. 193 Aalto M. K., Ruohonen L., Hosono K. and Keranen S. (1991) Cloning and sequencing of the yeast Saccharomyces cerevisiae SEC1 gene localized on chromosome IV. Yeast 7: 643-650
194. 194 Gengyo-Ando K., Kamiya Y., Yamakawa A., Kodaira K., Nishiwaki K., Miwa J. et al. (1993) The C. elegans unc-18 gene encodes a protein expressed in motor neurons. Neuron 11: 703-711
195. 195 Hata Y., Slaughter C. A. and Sudhof T. C. (1993) Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin. Nature 366: 347-351
196. 196 Salzberg A., Cohen N., Halachmi N., Kimchie Z. and Lev Z. (1993) The Drosophila Ras2 and Rop gene pair: a dual homology with a yeast Ras-like gene and a suppressor of its loss-of-function phenotype. Development 117: 1309-1319
197. 197 Pevsner J., Hsu S. C. and Scheller R. H. (1994) n-Sec1: a neural-specific syntaxin-binding protein. Proc. Natl. Acad. Sci. USA 91: 1445-1449
198. 198 Aalto M. K., Jantti J., Ostling J., Keranen S. and Ronne H. (1997) Mso1p: a yeast protein that functions in secretion and interacts physically and genetically with Sec1p. Proc. Natl. Acad. Sci. USA 94: 7331-7336
199. 199 Harrison S. D., Broadie K., van de Goor J. and Rubin G. M. (1994) Mutations in the Drosophila Rop gene suggest a function in general secretion and synaptic transmission. Neuron 13: 555-566
200. 200 Schulze K. L., Littleton J. T., Salzberg A., Halachmi N., Stern M., Lev Z. et al. (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
201. 201 Wu M. N., Littleton J. T., Bhat M. A., Prokop A. and Bellen H. J. (1998) ROP, the Drosophila Sec1 homolog, interacts with syntaxin and regulates neurotransmitter release in a dosage-dependent manner. EMBO J. 17: 127-139
202. 202 Shuang R., Zhang L., Fletcher A., Groblewski G. E., Pevsner J. and Stuenkel E. L. (1998) Regulation of Munc-18/syntaxin 1A interaction by cyclin-dependent kinase 5 in nerve endings. J. Biol. Chem. 273: 4957-4966
203. 203 Jahn R., Schiebler W., Ouimet C. and Greengard P. (1985) A 38,000-dalton membrane protein (p38) present in synaptic vesicles. Proc. Natl. Acad. Sci. USA 82: 4137-4141
204. 204 Wiedenmann B. and Franke W. W. (1985) Identification and localization of synaptophysin, an integral membrane glycoprotein of Mr 38,000 characteristic of presynaptic vesicles. Cell 41: 1017-1028
205. 205 Calakos N. and Scheller R. H. (1994) Vesicle-associated membrane protein and synaptophysin are associated on the synaptic vesicle. J. Biol. Chem. 269: 24534-24537
206. 206 Edelmann L., Hanson P. I., Chapman E. R. and Jahn R. (1995) Synaptobrevin binding to synaptophysin: a potential mechanism for controlling the exocytotic fusion machine. EMBO J. 14: 224-231
207. 207 Washbourne P., Schiavo G. and Montecucco C. (1995) Vesicle-associated membrane protein-2 (synaptobrevin-2) forms a complex with synaptophysin. Biochem. J. 305: 721-724
208. 208 Galli T., McPherson P. S. and De Camilli P. (1996) The V0 sector of the V-ATPase, synaptobrevin and synaptophysin are associated on synaptic vesicles in a Triton X-100-resistant, freeze-thawing sensitive, complex. J. Biol. Chem. 271: 2193-2198
209. 209 Lustgarten V. and Gerst J. E. (1998) Unpublished results
210. 210 Rothman J. E. and Orci L. (1992) Molecular dissection of the secretory pathway. Nature 355: 409-415
211. 211 Rothman J. E. (1994) Mechanisms of intracellular protein transport. Nature 372: 55-63
212. 212 Hay J. C. and Scheller R. H. (1997) SNAREs and NSF in targeted membrane fusion. Curr. Opin. Cell Biol. 9: 505-512
213. 213 Wilson D. W., Wilcox C. A., Flynn G. C., Chen E., Kuang W. J., Henzel W. J. et al. (1989) A fusion protein required for vesicle-mediated transport in both mammalian cells and yeast. Nature 339: 355-359
214. 214 Clary D. O., Griff I. C. and Rothman J. E. (1990) SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast. Cell 61: 709-721
215. 215 Wilson D. W., Whiteheart S. W., Wiedmann M., Brunner M. and Rothman J. E. (1992) A multisubunit particle implicated in membrane fusion. J. Cell Biol. 117: 531-538
216. 216 Xu Z., Sato K. and Wickner W. (1998) LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex and is released during fusion. Cell 93: 1125-1134
217. 217 Rothman J. E. and Fries E. (1981) Transport of newly synthesized vesicular stomatitis viral glycoprotein to purified Golgi membranes. J. Cell Biol. 89: 162-168
218. 218 Rothman J. E., Urbani L. J. and Brands R. (1984) Transport of protein between cytoplasmic membranes of fused cells: correspondence to processes reconstituted in a cell-free system. J. Cell Biol. 99: 248-259
219. 219 Rothman J. E., Miller R. I., and Urbani L. J. (1984) Intercompartmental transport in the Golgi complex is a dissociative process: facile transfer of membrane protein between two Golgi populations. J. Cell Biol. 99: 260-371
220. 220 Clary D. O. and Rothman J. E. (1990) Purification of three related peripheral membrane proteins needed for vesicular transport. J. Biol. Chem. 265: 10109-10117
221. 221 Whiteheart S. W., Griff I. C., Brunner M., Clary D. O., Mayer T., Buhrow S. A. et al. (1993) SNAP family of NSF attachment proteins includes a brain-specific isoform. Nature 362: 353-355
222. 222 Whiteheart S. W., Brunner M., Wilson D. W., Wiedmann M. and Rothman J. E. (1992) Soluble N-ethylmaleimide-sensitive fusion attachment proteins (SNAPs) bind to a multi-SNAP receptor complex in Golgi membranes. J. Biol. Chem. 267: 12239-12243
223. 223 Tagaya M., Wilson D. W., Brunner M., Arango N. and Rothman J. E. (1993) Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport. J. Biol. Chem. 268: 2662-2666
224. 224 Wattenberg B. W., Raub T. J., Hiebsch R. R. and Weidman P. J. (1992) The activity of Golgi transport vesicles depends on the presence of the N-ethylmaleimide-sensitive factor (NSF) and a soluble NSF attachment protein (alpha SNAP) during vesicle formation. J. Cell Biol. 118: 1321-1332
225. 225 Fleming K. G., Hohl T. M., Yu R. C., Muller S. A., Wolpensinger B., Engel A. et al. (1998) A revised model for the oligomeric state of the N-ethylmaleimide-sensitive fusion protein, NSF. J. Biol. Chem. 273: 15675-15681
226. 226 Morgan A. and Burgoyne R. D. (1995) Is NSF a fusion protein? Trends Cell Biol. 5: 335-339
227. 227 Xu Z. and Wickner W. (1996) Thioredoxin is required for vacuole inheritance in Saccharomyces cerevisiae. J. Cell Biol. 132: 787-794
228. 228 Xu Z., Mayer A., Muller E. and Wickner W. (1997) A heterodimer of thioredoxin and I(B)2 cooperates with Sec18p (NSF) to promote yeast vacuole inheritance. J. Cell Biol. 136: 299-306
229. 229 Barlowe C. (1997) Coupled ER to Golgi transport reconstituted with purified cytosolic proteins. J. Cell Biol. 139: 1097-1108
230. 230 Legesse-Miller A., Sagiv Y., Porat A. and Elazar Z. (1998) Isolation and characterization of a novel low molecular weight protein involved in intra-Golgi traffic. J. Biol. Chem. 273: 3105-3109
231. 231 Elazar Z. (1998) Unpublished results
232. 232 Chamberlain L. H., Roth D., Morgan A. and Burgoyne R. D. (1995) Distinct effects of alpha-SNAP, 14-3-3 proteins, and calmodulin on priming and triggering of regulated exocytosis. J. Cell Biol. 130: 1063-1070
233. 233 Burgoyne R D., Morgan A., Barnard R. J., Chamberlain L. H., Glenn D. E. and Kibble A. V. (1996) SNAPs and SNAREs in exocytosis in chromaffin cells. Biochem. Soc. Trans. 24: 653-657
234. 234 Barnard R. J., Morgan A. and Burgoyne R. D. (1997) Stimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosis. J. Cell Biol. 139: 875-883
235. 235 DeBello W. M., O'Connor V., Dresbach T., Whiteheart S. W., Wang S. S., Schweizer F. E. et al. (1995) SNAP-mediated protein-protein interactions essential for neurotransmitter release. Nature 373: 626-630
236. 236 Pfeffer S. R. (1996) Transport vesicle docking: SNAREs and associates. Ann. Rev. Cell Dev. Biol. 12: 441-461
237. 237 Novick P. and Zerial M. (1997) The diversity of Rab proteins in vesicle transport. Curr. Opin. Cell Biol. 9: 496-504
238. 238 Bean A. J. and Scheller R. H. (1997) Better late than never: a role for rabs late in exocytosis. Neuron 19: 751-754
239. 239 Colombo M. I., Gelberman S. C., Whiteheart S. W. and Stahl P. D. (1998) N-ethylmaleimide-sensitive factor-dependent alpha-SNAP release, an early event in the docking/fusion process, is not regulated by Rab GTPases. J. Biol. Chem. 273: 1334-1338
240. 240 Lupashin V. V. and Waters M. G. (1997) t-SNARE activation through transient interaction with a rab-like guanosine triphosphatase. Science 276: 1255-1258
241. 241 Dascher C., Ossig R., Gallwitz D. and Schmitt H. D. (1991) Identification and structure of four yeast genes (SLY) that are able to suppress the functional loss of YPT1, a member of the RAS superfamily. Mol. Cell. Biol. 11: 872-885
242. 242 Lian J. P., Stone S., Jiang Y., Lyons P. and Ferro-Novick S. (1994) Ypt1p implicated in v-SNARE activation. Nature 372: 698-701
243. 243 Farnsworth C. C., Seabra M. C., Ericsson L. H., Gelb M. H. and Glomset J. A. (1994) Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A. Proc. Natl. Acad. Sci. USA 91: 11963-11967
244. 244 Fischer von Mollard G., Mignery G. A., Baumert M., Perin M. S., Hanson T. J., Burger P. M. et al. (1990) rab3 is a small GTP-binding protein exclusively localized to synaptic vesicles. Proc. Natl. Acad. Sci. USA 87: 1988-1992
245. 245 Garrett M. D., Zahner J. E., Cheney C. M. and Novick P. J. (1994) GDII encodes a GDP dissociation inhibitor that plays an essential role in the yeast secretory pathway. EMBO J. 13: 1718-1728
246. 246 Fischer von Mollard G., Stahl B., Khokhlatchev A., Sudhof T. C. and Jahn R. (1994) Rab3C is a synaptic vesicle protein that dissociates from synaptic vesicles after stimulation of exocytosis. J. Biol. Chem. 269: 10971-10974
247. 247 Jena B. P., Gumkowski F. D., Konieczko E. M., von Mollard G. F., Jahn R. and Jamieson J. D. (1994) Redistribution of a rab3-like GTP-binding protein from secretory granules to the Golgi complex in pancreatic acinar cells during regulated exocytosis. J. Cell Biol. 124: 43-53
248. 248 Salminen A. and Novick P. J. (1987) A ras-like protein is required for a post-Golgi event in yeast secretion. Cell 49: 527-538
249. 249 Walworth N. C., Goud B., Habcenell K. and Novick P. J. (1989) Mutational analysis of SEC4 suggests a cyclical mechanism for the regulation of vesicular trafic. Eur. Mol. Biol. Organ. J. 8: 1685-1693
250. 250 Walworth N. C., Brennwald P., Kabeenell A. K., Garrett M. and Novick P. (1992) Hydrolysis of GTP by Sec4 protein plays an important role in vesicular transport and is stimulated by a GTPase-activating protein in Saccharomyces cerevisiae. Mol. Cell. Biol. 12: 2017-2028
251. 251 Walch Solimena C., Collins R. N. and Novick P. J. (1997) Sec2p mediates nucleotide exchange on Sec4p and is involved in polarized delivery of post-Golgi vesicles. J. Cell Biol. 137: 1495-1509
252. 252 Geppert M., Bolshakov V. Y., Siegelbaum S. A., Takei K., De C. P., Hammer R. E. et al. (1994) The role of Rab3A in neurotransmitter release. Nature 369: 493-497
253. 253 Jorgensen E. M., Hartwieg E., Schuske K., Nonet M. L., Jin Y. and Horvitz H. R. (1995) Defective recycling of synaptic vesicles in synaptotagmin mutants of Caenorhabditis elegans. Nature 378: 196-199
254. 254 Geppert M., Goda Y., Stevens C. F. and Sudhof T. C. (1997) The small GTP-binding protein Rab3A regulates a late step in synaptic vesicle fusion. Nature 387: 810-814
255. 255 Kishida S., Shirataki H., Sasaki T., Kato M., Kaibuchi K. and Takai Y. (1993) Rab3A GTPase-activating protein-inhibiting activity of Rabphilin-3A, a putative Rab3A target protein. J. Biol. Chem. 268: 22259-22261
256. 256 Shirataki H., Yamamoto T., Hagi S., Miura H., Oishi H., Jin-no Y. et al. (1994) Rabphilin-3A is associated with synaptic vesicles through a vesicle protein in a manner independent of Rab3A. J. Biol. Chem. 269: 32717-32720
257. 2 + /phospholipid-binding protein, depends on rab3A/3C. Neuron 13: 885-898
258. 258 Wang Y., Okamoto M., Schmitz F., Hofmann K. and Sudhof T. C. (1997) Rim is a putative Rab3 effector in regulating synaptic-vesicle fusion. Nature 388: 593-598
259. 259 Brondyk W. H., McKiernan C. J., Fortner K. A., Stabila P., Holz R. W. and Macara I. G. (1995) Interaction cloning of Rabin3, a novel protein that associates with the Ras-like GTPase Rab3A. Mol. Cell. Biol. 15: 1137-1143
260. 260 Stahl B., Chou J. H., Li C., Sudhof T. C. and Jahn R. (1996) Rab3 reversibly recruits rabphilin to synaptic vesicles by a mechanism analogous to raf recruitment by ras. EMBO J. 15: 1799-1809
261. 261 Masumoto N., Sasaki T., Tahara M., Mammoto A., Ikebuchi Y., Tasaka K. et al. (1996) Involvement of Rabphilin-3A in cortical granule exocytosis in mouse eggs. J. Cell Biol. 135: 1741-1747
262. 262 Burns M. E., Sasaki T., Takai Y. and Augustine G. J. (1998) Rabphilin-3A: a multifunctional regulator of synaptic vesicle traffic. J. Gen. Physiol. 111: 243-255
263. 263 Arribas M., Regazzi R., Garcia E., Wollheim C. B. and De Camilli P. (1997) The stimulatory effect of rabphilin 3a on regulated exocytosis from insulin-secreting cells does not require an association-dissociation cycle with membranes mediated by Rab 3. Eur. J. Cell Biol. 74: 209-216
264. 264 Johannes L., Doussau F., Clabeeq A., Henry J. P., Darchen F. and Poulain B. (1996) Evidence for a functional link between Rab3 and the SNARE complex. J. Cell Sci. 109: 2875-2884
265. 265 Orita S., Sasaki T., Naito A., Komuro R., Ohtsuka T., Maeda M. et al. (1995) Doc2: a novel brain protein having two repeated C2-like domains. Biochem. Biophys. Res. Commun. 206: 439-448
266. 266 Sakaguchi G., Orita S., Maeda M., Igarashi H. and Takai Y. (1995) Molecular cloning of an isoform of Doc2 having two C2-like domains. Biochem. Biophys. Res. Commun. 217: 1053-1061
267. 267 Verhage M., de Vries K. J., Roshol H., Burbach J. P., Gispen W. H. and Sudhof T. C. (1997) DOC2 proteins in raf brain: complementary distribution and proposed function as vesicular adapter proteins in early stages of secretion. Neuron 18: 453-461
268. 2 + -dependent exocytosis from PC12 cells. J. Biol. Chem. 271: 7257-7260
269. 2 + -dependent exocytotic machinery. J. Biol. Chem. 272: 16081-16084
270. 270 Byrne J. H. and Kandel E. R. (1996) Presynaptic facilitation revisited: state and time dependence. J. Neurosci. 16: 425-435
271. 271 Ktistakis N. T. (1998) Signalling molecules and the regulation of intracellular transport. Bioessays 20: 495-504
272. 272 Fabbri M., Bannykh S. and Balch W. E. (1994) Export of protein from the endoplasmic reticulum is regulated by a diacylglycerol/phorbol ester binding protein. J. Biol. Chem. 269: 26848-26857
273. 273 Redman R. S., Searl T. J., Hirsh J. K. and Silinsky E. M. (1997) Opposing effects of phorbol esters on transmitter release and calcium currents at frog motor nerve endings. J. Physiol. 501: 41-48
274. 2 + acts by two separate pathways to modulate the supply of release-competent vesicles in chromaffin cells. Neuron 20: 1243-1253
275. 275 Maruyama I. N. and Brenner S. (1991) A phorbol ester/diacylglycerol-binding protein encoded by the unc-13 gene of Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA 88: 5729-5733
276. 276 Betz A., Telemenakis I., Hofmann K. and Brose N. (1996) Mammalian Unc-13 homologues as possible regulators of neurotransmitter release. Biochem. Soc. Trans. 24: 661-666
277. 277 Betz A., Ashery U., Rickmann M., Augustin I., Neher E., Sudhof T. C. et al. (1998) Munc13-1 is a presynaptic phorbol ester receptor that enhances neurotransmitter release. Neuron 21: 123-136
278. 278 Hosono R., Sassa T. and Kuno S. (1987) Mutations affecting acetylcholine levels in the nematode Caenorhabditis elegans. J. Neurochem. 49: 1820-1823
279. 279 Hosono R. and Kamiya Y. (1991) Additional genes which result in an elevation of acetylcholine levels by mutations in Caenorhabditis elegans. Neurosci. Lett. 128: 243-244
280. 280 Bean A. J., Seifert R., Chen Y. A., Sacks R. and Scheller R. H. (1997) Hrs-2 is an ATPase implicated in calcium-regulated secretion. Nature 385: 826-829
281. 281 McMahon H. T., Missler M., Li C. and Sudhof T. C. (1995) Complexins: cytosolic proteins that regulate SNAP receptor function. Cell 83: 111-119
282. 282 Feany M. B., Lee S., Edwards R. H. and Buckley K. M. (1992) The synaptic vesicle protein SV2 is a novel type of transmembrane transporter. Cell 70: 861-867
283. 283 Bajjalieh S. M., Peterson K., Shinghal R. and Scheller R. H. (1992) SV2, a brain synaptic vesicle protein homologous to bacterial transporters. Science 257: 1271-1273
284. 284 Bajjalieh S. M., Peterson K., Linial M. and Scheller R. H. (1993) Brain contains two forms of synaptic vesicle protein 2. Proc. Natl. Acad. Sci. USA 90: 2150-2154
285. 285 Walent J. H., Porter B. W. and Martin T. F. (1992) A novel 145 kd brain cytosolic protein reconstitutes Ca(2 + )-regulated secretion in permeable neuroendocrine cells. Cell 70: 765-775
286. 286 Hay J. C. and Martin T. F. (1992) Resolution of regulated secretion into sequential MgATP-dependent and calcium-dependent stages mediated by distinct cytosolic proteins. J. Cell Biol. 119: 139-151
287. 2 + -activated exocytosis. J. Biol. Chem. 272: 19637-19640
288. 2 + -activated exocytosis in a cell-free system. J. Biol. Chem. 272: 14447-14453
289. 289 Loyet K. M., Kowalchyk J. A., Chaudhary A., Chen J., Prestwich G. D. and Martin T. F. J. (1998) Specific binding of phosphatidylinositol 4,5-bisphosphate to calcium-dependent activator protein for secretion (CAPS), a potential phosphoinositide effector protein for regulated exocytosis. J. Biol. Chem. 273: 8337-8343
290. 290 Berwin B., Floor E. and Martin T. F. (1998) CAPS (mammalian UNC-31) protein localizes to membranes involved in dense-core vesicle exocytosis. Neuron 21: 137-145
291. 291 Tandon A., Bannykh S., Kowalchyk J. A., Banerjee A., Martin T. F. and Balch W. E. (1998) Differential regulation of exocytosis by calcium and CAPS in semi-intact synaptosomes. Neuron 21: 147-154
292. 292 Thureson-Klein A. (1983) Exocytosis from large and small dense cored vesicles in noradrenergic nerve terminals. Neuroscience 10: 245-259
293. 293 Verhage M., McMahon H. T., Ghijsen W. E., Boomsma F., Scholten G., Wiegant V. M. et al. (1991) Differential release of amino acids, neuropeptides and catecholamines from isolated nerve terminals. Neuron 6: 517-624
294. 294 Heidelberger R., Heinemann C., Neher E. and Matthews G. (1994) Calcium dependence of the rate of exocytosis in a synaptic terminal. Nature 371: 513-515
295. 295 Bruns D. and Jahn R. (1995) Real-time measurement of transmitter release from single synaptic vesicles. Nature 377: 62-65
296. 296 Skehel P. A., Martin K. C., Kandel E. R. and Bartsch D. (1995) A VAMP-binding protein from Aplysia required for neurotransmitter release. Science 269: 1580-1583
297. 297 Skehel P. A., Armitage B. A., Bartsch D., Hu Y., Kaang B. K., Siegelbaum S. A. et al. (1995) Proteins functioning in synaptic transmission at the sensory to motor synapse of Aplysia. Neuropharmacology 34: 1379-1385
298. 298 Nikawa J., Murakami A., Esumi E. and Hosaka K. (1995) Cloning and sequence of the SCS2 gene, which can suppress the defect of INO1 expression in an inositol auxotrophic mutant of Saccharomyces cerevisiae. J. Biochem. 118: 39-45
299. 299 Kagiwada S., Hosaka K., Murata M., Nikawa J. and Takatsuki A. (1998) The Saccharomyces cerevisiae SCS2 gene product, a homolog of a synaptobrevin-associated protein, is an integral membrane protein of the endoplasmic reticulum and is required for inositol metabolism. J. Bacteriol. 180: 1700-1708
300. 300 Greengard P., Valtorta F., Czernik A. J. and Benfenati F. (1993) Synaptic vesicle phosphoproteins and regulation of synaptic function. Science 259: 780-785
301. 301 Greengard P., Benfenati F. and Valtorta F. (1994) Synapsin I, an actin-binding protein regulating synaptic vesicle traffic in the nerve terminal. Adv. Second Messenger Phosphoprotein Res. 29: 31-45
302. 302 Nishizaki T., Walent J. H., Kowalchyk J. A. and Martin T. F. (1992) A key role for a 145-kDa cytosolic protein in the stimulation of Ca(2 + )-dependent secretion by protein kinase C. J. Biol. Chem. 267: 23972-23981
303. 303 Janz R. and Sudhof T. C. (1998) Cellugyrin, a novel ubiquitous form of synaptogyrin that is phosphorylated by pp60c-src. J. Biol. Chem. 273: 2851-2857
304. 304 Sarafian T., Pradel L. A., Henry J. P., Aunis D. and Bader M. F. (1991) The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kinase C. J. Cell Biol. 114: 1135-1147
305. 305 Johnstone S. A., Hubaishy I. and Waisman D. M. (1992) Phosphorylation of annexin II tetramer by protein kinase C inhibits aggregation of lipid vesicles by the protein. J. Biol. Chem. 267: 25976-25981
306. 306 Wang W. and Creutz C. E. (1992) Regulation of the chromaffin granule aggregating activity of annexin I by phosphorylation. Biochemistry 31: 9934-9939
307. 307 Morgan A. and Burgoyne R. D. (1992) Exo1 and Exo2 proteins stimulate calcium-dependent exocytosis in permeabilized adrenal chromaffin cells. Nature 355: 833-836
308. 2 + trigger. J. Neurochem. 60: 1264-1273
309. 2 + channel which is coupled to glutamate exocylosis. FEBS Lett. 353: 264-268
310. 310 Burgoyne R. D. (1991) Control of exocytosis in adrenal chromaffin cells. Biochim. Biophys. Acta 1071: 174-202
311. 311 Burgoyne R. D. and Morgan A. (1992) Phospholipid-binding proteins in calcium-dependent exocytosis. Biochem. Soc. Trans. 20: 834-836
312. 312 Valtorta E., Benfenati F. and Basudev H. (1996) Role of protein kinases in nerve terminal maturation and function. Biochem. Soc. Trans. 24: 645-653
313. 313 Mellor H. and Parker P. J. (1998) The extended protein kinase C superfamily. Biochem. J. 332: 281-292
314. 314 Foster L. J., Yeung B., Mohtashami M., Ross K., Trimble W. S. and Klip A. (1998) Binary interactions of the SNARE proteins syntaxin-4, SNAP23, and VAMP-2 and their regulation by phosphorylation. Biochemistry 37: 11089-11096
315. 2 + / phospholipid binding. J. Biol. Chem. 268: 26386-26390
316. 2 + /calmodulin protein kinase II in synaptic vesicles. FEBS Lett. 317: 85-88
317. 2 + /calmodulin-dependent protein kinase II is a binding protein for synapsin I. Nature 359: 417-420
318. 2 + / calmodulin and phosphorylation: inhibition of actin binding and bundling. Biochemistry 34: 1912-1920
319. 319 Ceccaldi P. E., Grohovaz F., Benfenati F., Chieregatti E., Greengard P. and Valtorta F. (1995) Dephosphorylated synapsin I anchors synaptic vesicles to actin cytoskeleton: an analysis by videomicroscopy. J. Cell Biol. 128: 905-912
320. 2 + /calmodulin kinasc II inhibitor KN-62. J. Cell Sci. 108: 2619-2628
321. 321 De Camilli P., Emr S. D., McPherson P. S. and Novick P. (1996) Phosphoinositides as regulators in membrane traffic. Science 271: 1533-1539
322. 322 Martin T. F. (1997) Phosphoinositides as spatial regulators of membrane traffic. Curr. Opin. Neurobiol. 7: 331-338
323. 323 Hay J. C., Fisette P. L., Jenkins G. H., Fukami K., Takenawa T., Anderson R. A. et al. (1995) ATP-dependent inositide phosphorylation required for Ca(2 t )-activated secretion. Nature 374: 173-177
324. 324 Martin T. F., Hay J. C., Banerjee A., Barry V. A., Ann K., Yom H. C. et al. (1995) Late ATP-dependent and Ca + + -activated steps of dense core granule exocytosis. Cold Spring Harb. Symp. Quant. Biol. 60: 197-204
325. 2 + -activated exocytosis. J. Biol. Chem. 271: 20223-20226
326. 326 Alter C. A. and Wolf B. A. (1995) Identification of phosphatidylinositol 3,4,5-trisphosphate in pancreatic islets and insulin-secreting beta-cells. Biochem. Biophys. Res. Commun. 208: 190-197
327. 327 Wiedemann C., Schafer T., Burger M. M. and Sihra T. S. (1998) An essential role for a small synaptic vesicle-associated phosphatidylinositol 4-kinase in neurotransmitter release. J. Neurosci. 18: 5594-5602
328. 328 McPherson P. S., Garcia E. P., Slepnev V. I., David C., Zhang X., Grabs D. et al. (1996) A presynaptic inositol-5-phosphatase. Nature 379: 353-357
329. 329 Gaidarov I., Chen Q., Falck J. R., Reddy K. K. and Keen J. H. (1996) A functional phosphatidylinositol 3,4,5-trisphosphate/phosphoinositide binding domain in the clathrin adaptor AP-2 alpha subunit. Implications for the endocytic pathway. J. Biol. Chem. 271: 20922-20929
330. 330 Slepnev V. I., Ochoa G. C., Butler M. H., Grabs D. and Camilli P. D. (1998) Role of phosphorylation in regulation of the assembly of endocytic coat complexes. Science 281: 821-824
331. 331 Liscovitch M. and Cantley L. C. (1995) Signal transduction and membrane traffic: the PITP phosphoinositide connection. Cell 81: 659-662
332. 332 Janmey P. A. (1994) Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly. Ann. Rev. Physiol. 56: 169-191
333. 333 Liscovitch M., Chalifa V., Pertile P., Chen C. S. and Cantley L. C. (1994) Novel function of phosphatidylinositol 4,5-bisphosphate as a cofactor for brain membrane phospholipase D. J. Biol. Chem. 269: 21403-21406
334. 334 Simons K. and Ikonen E. (1997) Functional rafts in cell membranes. Nature 387: 569-572
335. 335 Simons K. and van Meer G. (1988) Lipid sorting in epithelial cells. Biochemistry 27: 6197-6202
336. 336 van Genderen I. L., van Meer G., Slot J. W., Geuze H. J. and Voorhout W. F. (1991) Subcellular localization of Forssman glycolipid in epithelial MDCK cells by immunoelectronmicroscopy after freeze-substitution. J. Cell Biol. 115: 1009-1019
337. 337 Lisanti M. P., Caras I. W., Davitz M. A. and Rodriguez-Boulan E. (1989) A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells. J. Cell Biol. 109: 2145-2156
338. 338 Wandinger-Ness A., Bennett M. K., Antony C. and Simons K. (1990) Distinct transport vesicles mediate the delivery of plasma membrane proteins to the apical and basolateral domains of MDCK cells. J. Cell Biol. 111: 987-1000
339. 339 van Meer G. (1993) Transport and sorting of membrane lipids. Curr. Opin. Cell Biol. 5: 661-673
340. 340 Cerneus D. P., Ueffing E., Posthuma G., Strous G. J. and van der Ende A. (1003) Detergent insolubility of alkaline phosphatase during biosynthetic transport and endocytosis. Role of cholesterol. J. Biol. Chem. 268: 3150-3155
341. 341 Fiedler K., Kobayashi T., Kurzchalia T. V. and Simons K. (1993) Glycosphingolipid-enriched, detergent-insoluble complexes in protein sorting in epithelial cells. Biochemistry 32: 6365-6373
342. 342 Hanada K., Nishijima M., Akamatsu Y. and Pagano R. E. (1995) Both sphingolipids and cholesterol participate in the detergent insolubility of alkaline phosphatase, a glycosylphosphatidylinositol-anchored protein, in mammalian membranes. J. Biol. Chem. 270: 6254-6260
343. 343 Horvath A., Sutterlin C., Manning-Krieg U., Movva N. R. and Riezman H. (1994) Ceramide synthesis enhances transport of GPI-anchored proteins to the Golgi apparatus in yeast. EMBO J. 13: 3687-3695
344. 344 Skrzypek M., Lester R. L. and Dickson R. C. (1097) Suppressor gene analysis reveals an essential role for sphingolipids in transport of glycosylphosphatidylinositol-anchored proteins in Saccharomyces cerevisiae. J. Bacteriol. 179: 1513-1520
345. 345 Harel R. and Futerman A. H. (1993) Inhibition of sphingolipid synthesis affects axonal outgrowth in cultured hippocampal neurons. J. Biol. Chem. 268: 14476-14481
346. 346 Sšllner T. and Rothman J. E. (1994) Neurotransmission: harnessing fusion machinery at the synapse. Trends Neurosci. 17: 344-348
347. 347 Littleton J. T., Chapman E. R., Kreber R., Garment M. B., Carlson S. D. and Ganetzky B. (1998) Temperature-sensitive paralytic mutations demonstrate that synaptic exocytosis requires SNARE complex assembly and disassembly. Neuron 21: 401-413
348. 348 Tagaya M., Furuno A. and Mizushima S. (1996) SNAP prevents Mg(2 + )-ATP-induced release of N-ethylmaleimide-sensitive factor from the Golgi apparatus in digitonin-permeabilized PC12 cells. J. Biol. Chem. 271: 466-470
349. 340 Walch-Solimena C., Blasi J., Edelmann L., Chapman E. R., von Mollard G. F. and Jahn R. (1905) The t-SNAREs syntaxin I and SNAP-25 are present on orpanelles that participate in synaptic vesicle recycling. J. Cell Biol. 128: 637-645
350. 350 Richardson C. J., Jones S., Litt R. J. and Segev N. (1998) GTP hydrolysis is not important for Ypt1 GTPase function in vesicular transport. Mol. Cell. Biol. 18: 827-838
351. 351 Jones S., Richardson C. J., Litt R. J. and Segev N. (1998) Identification of regulators for ypt1 GTPase nucleotide cycling. Mol. Biol. Cell 9: 2810-2837