Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy

Cell

Volumn 90, Issue 3, 1997, Pages 523-535

  Hanson, Phyllis I ^a,b   Roth, Robyn ^c   Morisaki, Hiroshi ^c   Jahn, Reinhard ^a   Heuser, John E ^a  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c NONE

Author keywords

[No Author keywords available]

Indexed keywords

ADSORPTION; ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; CONFORMATIONAL TRANSITION; HYDROLYSIS; NEUROTRANSMITTER RELEASE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; STEM CELL; SYNAPSE VESICLE; SYNAPTIC MEMBRANE; TEMPERATURE SENSITIVE MUTANT;

MICA;

EID: 0030740252     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80512-7     Document Type: Article

References (49)

1. Barnstable, C.J., Hofstein, R., and Akagawa, K. (1985). A marker of early amacrine cell development in rat retina. Dev. Brain Res. 20, 286-290.
2. Block, M.R., Click, B.S., Wilcox, C.A., Wieland, FT., and Rothman, J.E. (1988). Purification of an N-ethylmaleimide-sensitive protein catalyzing vesicular transport. Proc. Natl. Acad. Sci. USA 85, 7852-7856.
3. Bullough, P.A., Hughson, F.M., Skehel, J.J., and Wiley, D.C. (1994). Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 377, 37-43.
4. Cheney, R.E., O'Shea, M.K., Heuser, J.E., Coelho, M.V., Wolenski, J.S., Espreafico, E.M., Forscher, P., Larson, R.E., and Mooseker, M.S. (1993). Brain myosin-V is a two-headed unconventional myosin with motor activity. Cell 75, 13-23.
5. 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.
6. Confalonieri, F., and Duguet, M. (1995). A 200-amino acid ATPase module in search of a basic function. Bioessays 17, 639-650.
7. Eakle, K.A., Bernstein, M., and Emr, S.D. (1988). Characterization of a component of the yeast secretion machinery: identification of the sec 18 gene product. Mol. Cell. Biol. 8, 4098-4109.
8. 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.
9. Fasshauer, D., Bruns, D., Shen, B., Jahn, R., and Brünger, A.T. (1997). A structural change occurs upon binding of syntaxin to SNAP-25. J. Biol. Chem. 272, 4582-4590.
10. Ferro-Novick, S., and Jahn, R. (1994). Vesicle fusion from yeast to man. Nature 370, 191-193.
11. Click, B.S., and Rothman, J.E. (1987). Possible role for fatty acylcoenzyme A in intracellular protein transport. Nature 326, 309-312.
12. Griff, I.C., Schekman, R., Rothman, J.E., and Kaiser, C.A. (1992). The yeast sec77 gene product is functionally equivalent to mammalian α-SNAP protein. J. Biol. Chem. 267, 12106-12115.
13. Hanson, P.I., Otto, H., Barton, N., and Jahn, R. (1995). The N-ethylmaleimide-sensitive fusion protein and α-SNAP induce aconformational change in syntaxin. J. Biol. Chem. 270, 16955-16961.
14. Hayashi, T., McMahon, H., Yamasaki, S., Binz, T., Hata, Y., Sudhof, T.C., and Niemann, H. (1994). Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly. EMBO J. 13, 5051-5061.
15. 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.
16. Heuser, J.E. (1983). Procedure for freeze-drying molecules adsorbed to mica flakes. J. Mol. Biol. 169, 155-195.
17. Heuser, J. (1989). Procedure for 3-D visualization of molecules on mica via the quick-freeze, deep-etch technique. J. Electron Microsc. Technique 73, 244-263.
18. 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 74, 991-998.
19. Kessel, M., Maurizi, M.R., Kim, B., Kocsis, E., Trus, B.L., Singh, S.K., and Steven, A.C. (1995). Homology in structural organization between E. coliClpAP protease and the eukaryotic 26S proteasome. J. Mol. Biol. 250, 587-594.
20. Levchenko, I., Luo, L., and Baker, T.A. (1995). Disassembly of the Mu transposase tetramer by the ClpX chaperone. Genes Dev. 9, 2399-2408.
21. Malhotra, V., Orci, L, Glick, B.S., Block, M.R., and Rothman, J.E. (1988). Role of an N-ethylmaleimide-sensitive transport component in promoting fusion of transport vesicles with cisternae of the Golgi stack. Cell 54, 221-227.
22. Mayer, A., Wickner, W., and Haas, A. (1996). Sec 18p (NSF)-driven release of Sec 17p (α-SNAP) can precede docking and fusion of yeast vacuoles. Cell 85, 83-94.
23. Nagiec, E.E., Bernstein, A., and Whiteheart, S.W. (1995). Each domain of the N-ethylmaleimide-sensitive fusion protein contributes to its transport activity. J. Biol. Chem. 270, 29182-29188.
24. Nathke, I.S., Heuser, J., Lupas, A., Stock, J., Turck, C.W., and Brodsky, P.M. (1992). Folding and trimerization of the clathrin triskelion hub. Cell 65, 899-910.
25. Nichols, B.J., Ungermann, C., Pelham, H.R.B., Wickner, W.T., and Haas, A. (1997). Homotypic vacuolar fusion mediated by t-and v-SNAREs. Nature 387, 199-202.
26. 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.
27. Pallanck, L., Ordway, R.W., and Ganetzky, B. (1995). A Drosophila NSF mutant. Nature 376, 25.
28. Parsell, D.A., Kowal, A.S., and Lindquist, S. (1994a). Saccharomyces cerevisiae Hsp 104 protein. Purification and characterization of ATP-induced structural changes. J. Biol. Chem. 269, 4480-4487.
29. Parsell, D.A., Kowal, A.S., Singer, M.A., and Lindquist, S. (1994b). Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372, 475-478.
30. Peters, J.-M., Walsh, M.J., and Franke, W.W. (1990). An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec 18p and NSF. EMBO J. 9, 1757-1767.
31. 2+-ATPase complex. A structural study. J. Mol. Biol. 223, 557-571.
32. Rand, R.P., and Parsegian, V.A. (1986). Mimicry and mechanism in phospholipid models of membrane fusion. Ann. Rev. Physiol. 48, 201-212.
33. Rothman, J.E. (1994). Mechanisms of intracellular protein transport. Nature 372, 55-63.
34. Schekman, R., and Orci, L. (1996). Coat proteins and vesicle budding. Science 277, 1526-1533.
35. Scheller, R.H. (1995). Membrane trafficking in the presynaptic nerve terminal. Neuron 14, 893-897.
36. Schirmer, E.C., Glover, J.R., Singer, M.A., and Lindquist, S. (1996). Hsp 100/Clp proteins: a common mechanism explains diverse functions. TIBS 21, 289-296.
37. Scholey, J.M., Heuser, J.E., Yung, J.T., and Goldstein, C.S.B. (1989). Identification of globular mechanochemical heads of kinesin. Nature 338, 355-357.
38. Singh, S.K., and Maurizi, M.R. (1994). Mutational analysis demonstrates different functional roles for the two ATP-binding sites in ClpAP protease from Escherichia coli. J. Biol. Chem. 269, 29537-29545.
39. Söllner, T., Whiteheart, S.W., Brunner, M., Erdjument-Bromage, H., Geromanos, S., Tempst, P., and Rothman, J.E. (1993a). SNAP receptors implicated in vesicle targeting and fusion. Nature 362, 318-324.
40. Söllner, T., Bennett, M .K., Whiteheart, S.W., Scheller, R.H., and Rothman, J.E. (1993b). A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 75, 409-418.
41. Spurlino, J.C., Lu, G.Y., and Quiocho, F.A. (1991). The 2.3-A resolution structure of the maltose-or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J. Biol. Chem. 266, 5202-5219.
42. Südhof, T.C. (1995). The synaptic vesiclecycle: a cascade of protein-protein interactions. Nature 375, 645-653.
43. 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.
44. Weissenhorn, W., Dessen, A., Harrison, S.C., Skehel, J.J., and Wiley, D.C. (1997). Atomic structure of the ectodomain from HIV-1 gp41. Nature 387, 426-430.
45. Whiteheart, S.W., and Kubalek, E.W. (1995). SNAPs and NSF: general members of the fusion apparatus. Trends Cell Biol. 5, 64-68.
46. Whiteheart, S.W., Rossnagel, K., Buhrow, S.A., Brunner, M., Jaenicke, R., and Rothman, J.E. (1994). N-ethylmaleimide-sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion. J. Cell Biol. 126, 945-954.
47. Williams, R.C., and Wyckoff, R.W.G. (1946). Applications of metallic shadow-casting to microscopy. J. Appl. Physics 17, 23-33.
48. Wilson, D.W., Wilcox, C.A., Flynn, G.C., Chen, E., Kuang, W.J., Henzel, W.J., Block, M.R., Ullrich, A., and Rothman, J.E. (1989). A fusion protein required for vesicle-mediated transport in both mammalian cells and yeast. Nature 339, 355-359.
49. 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.