SNAP-24, a Drosophila SNAP-25 homologue on granule membranes, is a putative mediator of secretion and granule-granule fusion in salivary glands

QUICK SEARCH:

[advanced]

	Author:		Keyword(s):

Home Help Feedback Subscriptions Archive Search Table of Contents

This Article

	Summary
	Full Text (PDF)
	Alert me when this article is cited
	Alert me if a correction is posted

Services

	Email this article to a friend
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new issues of the journal
	Download to citation manager


Citing Articles

	Citing Articles via HighWire
	Citing Articles via Google Scholar

Google Scholar

	Articles by Niemeyer, B. A.
	Articles by Schwarz, T. L.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Niemeyer, B. A.
	Articles by Schwarz, T. L.

Adams, M. D., Celniker, S. E., Holt, R. A., Evans, C. A., Gocayne, J. D., Amanatides, P. G., Scherer, S. E., Li, P. W., Hoskins, R. A., Galle, R. F., et al. ( (2000). The genome sequence of Drosophila melanogaster. Science 287, 2185-2195.[Abstract/Free Full Text]

Alvarez de Toledo, G. and Fernandez, J. M (1990). Compound versus multigranular exocytosis in peritoneal mast cells. J. Gen. Physiol 95, 397-409.[Abstract/Free Full Text]

Araki, S., Tamori, Y., Kawanishi, M., Shinoda, H., Masugi, J., Mori, H., Niki, T., Okazawa, H., Kubota, T. and Kasuga, M (1997). Inhibition of the binding of SNAP-23 to syntaxin 4 by Munc18c. Biochem. Biophys. Res. Commun 234, 257-262.[Medline]

Banerjee, A., Kowalchyk, J. A., DasGupta, B. R. and Martin, T. F. J (1996). SNAP-25 is required for a late postdocking step in Ca2+-dependent exocytosis. J. Biol. Chem 271, 20227-20230.[Abstract/Free Full Text]

Beckendorf, S. K. and Kafatos, F. C (1976). Differentiation in the salivary glands of Drosophila melanogaster : characterization of the glue proteins and their developmental appearance. Cell 9, 365-373.[Medline]

Berendes, H. D (1965). Salivary gland function and chromosomal puffing patterns in Drosophila hydei. Chromosoma 17, 35-77.[Medline]

Boulianne, G. L. and Trimble, W. S (1995). Identification of a second homolog of N-ethylmaleimide-sensitive fusion protein that is expressed in the nervous system and secretory tissues of Drosophila. Proc. Natl. Acad. Sci. USA 92, 7095-7099.[Abstract/Free Full Text]

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.[Medline]

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.[Abstract/Free Full Text]

Chandler, D. E. and Heuser, J. E (1980). Arrest of membrane fusion events in mast cells by quick-freezing. J. Cell Biol 86, 666-674.[Abstract/Free Full Text]

Chen, D., Minger, S. L., Honer, W. G. and Whiteheart, S. W (1999). Organization of the secretory machinery in the rodent brain: distribution of the t-SNAREs, SNAP-25 and SNAP-23 [In Process Citation]. Brain Res 831, 11-24.[Medline]

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-L1 adipocytes and cleaves cellubrevin unlike type A toxin which failed to proteolyze the SNAP-23 present. Biochemistry 36, 5719-5728.[Medline]

Chen, Y. A., Scales, S. J., Patel, S. M., Doung, Y. C. and Scheller, R. H (1999). SNARE complex formation is triggered by Ca2+and drives membrane fusion. Cell 97, 165-174.[Medline]

Chin, A. C., Burgess, R. W., Wong, B. R., Schwarz, T. L. and Scheller, R. H (1993). Differential expression of transcripts from syb, a Drosophila melanogaster gene encoding VAMP (synaptobrevin) that is abundant in non-neuronal cells. Gene 131, 175-181.[Medline]

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.[Abstract/Free Full Text]

DiAntonio, A., Burgess, R. W., Chin, A. C., Deitcher, D. L., Scheller, R. H. and Schwarz, T. L (1993). Identification and characterization of Drosophila genes for synaptic vesicle proteins. J. Neurosci 13, 4924-4935.[Abstract]

Fasshauer, D., Antonin, W., Margittai, M., Pabst, S. and Jahn, R (1999). Mixed and non-cognate SNARE complexes. Characterization of assembly and biophysical properties. J. Biol. Chem 274, 15440-15446.[Abstract/Free Full Text]

Fasshauer, D., Sutton, R. B., Brunger, A. T. and Jahn, R (1998). Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q-and R-SNAREs. Proc. Natl. Acad. Sci. USA 95, 15781-15786.[Abstract/Free Full Text]

Flaumenhaft, R., Croce, K., Chen, E., Furie, B. and Furie, B. C (1999). Proteins of the exocytotic core complex mediate platelet alpha-granule secretion. Roles of vesicle-associated membrane protein, SNAP-23, and syntaxin 4. J. Biol. Chem 274, 2492-2501.[Abstract/Free Full Text]

Foster, L. J., Yaworsky, K., Trimble, W. S. and Klip, A (1999). SNAP23 promotes insulin-dependent glucose uptake in 3T3-L1 adipocytes: possible interaction with cytoskeleton. Am. J. Physiol 276, 1108-1114.

Fraenkel, G. and Brookes, V. J (1953). The process by which the puparia of many species of flies become fixed to a substrate. Biol. Bull 105, 442-449.[Abstract/Free Full Text]

Fujita, S. C., Zipursky, S. L., Benzer, S., Ferrus, A. and Shotwell, S. L (1982). Monoclonal antibodies against the Drosophila nervous system. Proc. Natl. Acad. Sci. USA 79, 7929-7233.[Abstract/Free Full Text]

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.[Medline]

Hansen, N. J., Antonin, W. and Edwardson, J. M (1999). Identification of SNAREs involved in regulated exocytosis in the pancreatic acinar cell [In Process Citation]. J. Biol. Chem 274, 22871-22876.[Abstract/Free Full Text]

Hansson, L. and Lambertsson, A (1989). Steroid regulation of glue protein genes in Drosophila melanogaster. Hereditas 110, 61-67.[Medline]

Hepp, R., Perraut, M., Chasserot-Golaz, S., Galli, T., Aunis, D., Langley, K. and Grant, N. J (1999). Cultured glial cells express the SNAP-25 analogue SNAP-23. Glia 27, 181-187.[Medline]

Hunt, J. M., Bommert, K., Charlton, M. P., Kistner, A., Habermann, E., Augustine, G. J. and Betz, H (1994). A post-docking role for synaptobrevin in synaptic vesicle fusion. Neuron 12, 1269-1279.[Medline]

Kawasaki, F., Mattiuz, A. M. and Ordway, R. W (1998). Synaptic physiology and ultrastructure in comatose mutants define an in vivo role for NSF in neurotransmitter release. J. Neurosci 18, 10241-10249.[Abstract/Free Full Text]

Kee, Y. and Scheller, R. H (1996). Localization of synaptotagmin-binding domains on syntaxin. J. Neurosci 16, 1975-1981.[Abstract/Free Full Text]

Lafont, F., Verkade, P., Galli, T., Wimmer, C., Louvard, D. and Simons, K (1999). Raft association of SNAP receptors acting in apical trafficking in Madin-Darby canine kidney cells. Proc. Natl. Acad. Sci. USA 96, 3734-3738.[Abstract/Free Full Text]

Lane, S. R. and Liu, Y (1997). Characterization of the palmitoylation domain of SNAP-25. J. Neurochem 69, 1864-1869.[Medline]

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.[Medline]

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.[Abstract/Free Full Text]

Lloyd, T. E., Verstreken, P., Ostrin, E. J., Phillippi, A., Lichtarge, O. and Bellen, H. J (2000). A genome-wide search for synaptic vesicle cycle proteins in Drosophila. Neuron 26, 45-50.[Medline]

Low, S. H., Roche, P. A., Anderson, H. A., van Ijzendoorn, S. C., Zhang, M., Mostov, K. E. and Weimbs, T (1998). Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells. J. Biol. Chem 273, 3422-3430.[Abstract/Free Full Text]

Mi, H., Deerinck, T. J., Ellisman, M. H. and Schwarz, T. L (1995). Differential distribution of closely related potassium channels in rat Schwann cells. J. Neurosci 15, 376137-74.

Ordway, R. W., Pallanck, L. and Ganetzky, B (1994). Neurally expressed Drosophila genes encoding homologs of the NSF and SNAP secretory proteins. Proc. Natl. Acad. Sci. USA 91, 5715-5719.[Abstract/Free Full Text]

Pallanck, L., Ordway, R. W. and Ganetzky, B (1995). A Drosophila NSF mutant [letter]. Nature 376, 25-.[Medline]

Pallanck, L., Ordway, R. W., Ramaswami, M., Chi, W. Y., Krishnan, K.S. and Ganetzky, B (1995). Distinct roles for N-ethylmaleimide-sensitive fusion protein (NSF) suggested by the identification of a second Drosophila NSF homolog. J. Biol. Chem 270, 18742-18744.[Abstract/Free Full Text]

Parfitt, K., Reist, N., Li, J., Burgess, R., Deitcher, D., DiAntonio, A. and Schwarz, T. L (1995). Drosophila genetics and the functions of synaptic proteins. Cold Spring Harb. Symp. Quant. Biol 60, 371-377.[Abstract/Free Full Text]

Poels, C. L. M (1972). Mucopolysaccharide secretion from Drosophila salivary gland cells as a consequence of hormone induced gene activity. Cell Diff 1, 63-78.[Medline]

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, 13300-13303.[Abstract/Free Full Text]

Risinger, C., Blomqvist, A. G., Lundell, I., Lambertsson, A., Nassel, D., Pieribone, V. A., Brodin, L. and Larhammar, D (1993). Evolutionary conservation of synaptosome-associated protein 25 kDa (SNAP-25) shown by Drosophila and Torpedo cDNA clones. J. Biol. Chem 268, 24408-24414.[Abstract/Free Full Text]

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.[Medline]

Rohlich, P., Anderson, P. and Uvnas, B (1971). Electron microscope observations on compounds 48-80-induced degranulation in rat mast cells. Evidence for sequential exocytosis of storage granules. J. Cell Biol 51, 465-483.

Ross, E. B (1939). The post-embryonic development of the salivary glands of Drosophila melanogaster. J. Morphol 65, 471-496.

Rothman, J. E. and Wieland, F. T (1996). Protein sorting by transport vesicles. Science 272, 227-234.[Abstract]

Scales, S. J., Chen, Y. A., Yoo, B. Y., Patel, S. M., Doung, Y. C. and Scheller, R. H (2000). SNAREs contribute to the specificity of membrane fusion. Neuron 26, 457-464.[Medline]

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.[Medline]

Shi, S. H., Hayashi, Y., Petralia, R. S., Zaman, S. H., Wenthold, R. J., Svoboda, K. and Malinow, R (1999). Rapid spine delivery and redistribution of AMPA receptors after synaptic NMDA receptor activation [see comments]. Science 284, 1811-1816.[Abstract/Free Full Text]

Siddiqi, O. and Benzer, S (1976). Neurophysiological defects in temperature-sensitive paralytic mutants of Drosophila melanogaster. Proc. Natl. Acad. Sci. USA 73, 3253-3257.[Abstract/Free Full Text]

Sollner, T., Whiteheart, S. W., Brunner, M., Erdjument-Bromage, H., Geromanos, S., Tempst, P. and Rothman, J. E (1993). SNAP receptors implicated in vesicle targeting and fusion [see comments]. Nature 362, 318-324.[Medline]

Steegmaier, M., Yang, B., Yoo, J. S., Huang, B., Shen, M., Yu, S., Luo, Y. and Scheller, R. H (1998). Three novel proteins of the syntaxin/SNAP-25 family. J. Biol. Chem 273, 34171-34179.[Abstract/Free Full Text]

Stowell, J. N. and Craig, A. M (1999). Axon/dendrite targeting of metabotropic glutamate receptors by their cytoplasmic carboxy-terminal domains [see comments]. Neuron 22, 525-536.[Medline]

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.[Medline]

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.[Medline]

Vogel, K. and Roche, P. A (1999). SNAP-23 and SNAP-25 are palmitoylated in vivo. Biochem. Biophys. Res. Commun 258, 407-410.[Medline]

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.[Medline]

Yang, B., Gonzalez, L., Jr., Prekeris, R., Steegmaier, M., Advani, R. J. and Scheller, R. H (1999). SNARE interactions are not selective. Implications for membrane fusion specificity. J. Biol. Chem 274, 5649-5653.[Abstract/Free Full Text]

Yoshihara, M., Ueda, A., Zhang, D., Deitcher, D. L., Schwarz, T. L. and Kidokoro, Y (1999). Selective effects of neuronal-synaptobrevin mutations on transmitter release evoked by sustained versus transient Ca2+ increases and by cAMP. J. Neurosci 19, 2432-2441.[Abstract/Free Full Text]

This article has been cited by other articles:

T. H. Kloepper, C. N. Kienle, and D. Fasshauer
SNAREing the Basis of Multicellularity: Consequences of Protein Family Expansion during Evolution
Mol. Biol. Evol., September 1, 2008; 25(9): 2055 - 2068.
[Abstract] [Full Text] [PDF]

P. Bronk, F. Deak, M. C. Wilson, X. Liu, T. C. Sudhof, and E. T. Kavalali
Differential Effects of SNAP-25 Deletion on Ca2+-Dependent and Ca2+-Independent Neurotransmission
J Neurophysiol, August 1, 2007; 98(2): 794 - 806.
[Abstract] [Full Text] [PDF]

I. Hafez, A. Stolpe, and M. Lindau
Compound Exocytosis and Cumulative Fusion in Eosinophils
J. Biol. Chem., November 7, 2003; 278(45): 44921 - 44928.
[Abstract] [Full Text] [PDF]

R. M. Weimer and E. M. Jorgensen
Controversies in synaptic vesicle exocytosis
J. Cell Sci., September 15, 2003; 116(18): 3661 - 3666.
[Full Text] [PDF]

S. Bhattacharya, B. A. Stewart, B. A. Niemeyer, R. W. Burgess, B. D. McCabe, P. Lin, G. Boulianne, C. J. O'Kane, and T. L. Schwarz
From the Cover: Members of the synaptobrevin/vesicle-associated membrane protein (VAMP) family in Drosophila are functionally interchangeable in vivo for neurotransmitter release and cell viability
PNAS, October 15, 2002; 99(21): 13867 - 13872.
[Abstract] [Full Text] [PDF]

I. Vilinsky, B. A. Stewart, J. Drummond, I. Robinson, and D. L. Deitcher
A Drosophila SNAP-25 Null Mutant Reveals Context-Dependent Redundancy With SNAP-24 in Neurotransmission
Genetics, September 1, 2002; 162(1): 259 - 271.
[Abstract] [Full Text] [PDF]

This Article

Summary

Full Text (PDF)

Alert me when this article is cited

Alert me if a correction is posted

Services

Email this article to a friend

Similar articles in this journal

Similar articles in PubMed

Alert me to new issues of the journal

Download to citation manager

Citing Articles

Citing Articles via HighWire

Citing Articles via Google Scholar

Google Scholar

Articles by Niemeyer, B. A.

Articles by Schwarz, T. L.

Search for Related Content

PubMed

PubMed Citation

Articles by Niemeyer, B. A.

Articles by Schwarz, T. L.

				P. Bronk, F. Deak, M. C. Wilson, X. Liu, T. C. Sudhof, and E. T. Kavalali Differential Effects of SNAP-25 Deletion on Ca2+-Dependent and Ca2+-Independent Neurotransmission J Neurophysiol, August 1, 2007; 98(2): 794 - 806. [Abstract] [Full Text] [PDF]

				I. Hafez, A. Stolpe, and M. Lindau Compound Exocytosis and Cumulative Fusion in Eosinophils J. Biol. Chem., November 7, 2003; 278(45): 44921 - 44928. [Abstract] [Full Text] [PDF]

				R. M. Weimer and E. M. Jorgensen Controversies in synaptic vesicle exocytosis J. Cell Sci., September 15, 2003; 116(18): 3661 - 3666. [Full Text] [PDF]

				S. Bhattacharya, B. A. Stewart, B. A. Niemeyer, R. W. Burgess, B. D. McCabe, P. Lin, G. Boulianne, C. J. O'Kane, and T. L. Schwarz From the Cover: Members of the synaptobrevin/vesicle-associated membrane protein (VAMP) family in Drosophila are functionally interchangeable in vivo for neurotransmitter release and cell viability PNAS, October 15, 2002; 99(21): 13867 - 13872. [Abstract] [Full Text] [PDF]

				I. Vilinsky, B. A. Stewart, J. Drummond, I. Robinson, and D. L. Deitcher A Drosophila SNAP-25 Null Mutant Reveals Context-Dependent Redundancy With SNAP-24 in Neurotransmission Genetics, September 1, 2002; 162(1): 259 - 271. [Abstract] [Full Text] [PDF]