Vesicle trafficking: Pleasure and pain from SM genes

Trends in Cell Biology

Volumn 13, Issue 4, 2003, Pages 177-186

  Toonen, Ruud F G ^a   Verhage, Matthijs ^a  

^a VU UNIVERSITY AMSTERDAM   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; PROTEIN SM; SNARE PROTEIN; SYNAPTOBREVIN; SYNTAXIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; CELLULAR DISTRIBUTION; COMPLEX FORMATION; GENE FUNCTION; GENE OVEREXPRESSION; INTRACELLULAR TRANSPORT; MOLECULAR BIOLOGY; MULTIGENE FAMILY; NONHUMAN; NULL ALLELE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; REVIEW; SEQUENCE HOMOLOGY; TRANSPORT VESICLE;

EID: 0037377234     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0962-8924(03)00031-X     Document Type: Review

References (105)

1. Chen Y.A., Scheller R.H. SNARE-mediated membrane fusion. Nat. Rev. Mol. Cell Biol. 2:2001;98-106.
2. Bruns D., Jahn R. Molecular determinants of exocytosis. Pflugers Arch. 443:2002;333-338.
3. Rizo J., Sudhof T.C. Snares and munc18 in synaptic vesicle fusion. Nat. Rev. Neurosci. 3:2002;641-653.
4. Broadie K., et al. Syntaxin and synaptobrevin function downstream of vesicle docking in Drosophila. Neuron. 15:1995;663-673.
5. O'Connor V., et al. Disruption of syntaxin-mediated protein interactions blocks neurotransmitter secretion. Proc. Natl. Acad. Sci. U. S. A. 94:1997;12186-12191.
6. Fasshauer D., et al. Mixed and non-cognate SNARE complexes. Characterization of assembly and biophysical properties. J. Biol. Chem. 274:1999;15440-15446.
7. Yang B., et al. SNARE interactions are not selective. Implications for membrane fusion specificity. J. Biol. Chem. 274:1999;5649-5653.
8. Gengyo-Ando K., et al. A murine neural-specific homolog corrects cholinergic defects in Caenorhabditis elegans unc-18 mutants. J. Neurosci. 16:1996;6695-6702.
9. Khan A.H., et al. Munc18c regulates insulin-stimulated glut4 translocation to the transverse tubules in skeletal muscle. J. Biol. Chem. 276:2001;4063-4069.
10. Verhage M., et al. Synaptic assembly of the brain in the absence of neurotransmitter secretion. Science. 287:2000;864-869.
11. Bhattacharya S., et al. Members of the synaptobrevin/vesicle-associated membrane protein (VAMP) family in Drosophila are functionally interchangeable in vivo for neurotransmitter release and cell viability. Proc. Natl. Acad. Sci. U. S. A. 99:2002;13867-13872.
12. Schoch S., et al. SNARE function analyzed in synaptobrevin/VAMP knockout mice. Science. 294:2001;1117-1122.
13. Washbourne P., et al. Genetic ablation of the t-SNARE SNAP-25 distinguishes mechanisms of neuroexocytosis. Nat. Neurosci. 5:2002;19-26.
14. Vilinsky I., et al. A Drosophila SNAP-25 Null Mutant Reveals Context-Dependent Redundancy With SNAP-24 in Neurotransmission. Genetics. 162:2002;259-271.
15. Pevsner J., et al. Specificity and regulation of a synaptic vesicle docking complex. Neuron. 13:1994;353-361.
16. De Vries K.J., et al. Dynamics of munc18-1 phosphorylation/dephosphorylation in rat brain nerve terminals. Eur. J. Neurosci. 12:2000;385-390.
17. Betz A., et al. Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin. J. Biol. Chem. 272:1997;2520-2526.
18. Fernandez I., et al. Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A. Cell. 94:1998;841-849.
19. Dulubova I., et al. A conformational switch in syntaxin during exocytosis: role of munc18. EMBO J. 18:1999;4372-4382.
20. Misura K.M., et al. Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex. Nature. 404:2000;355-362.
21. Munson M., et al. Interactions within the yeast t-SNARE Sso1p that control SNARE complex assembly. Nat. Struct. Biol. 7:2000;894-902.
22. Carr C.M., et al. Sec1p binds to SNARE complexes and concentrates at sites of secretion. J. Cell Biol. 146:1999;333-344.
23. Dulubova I., et al. How Tlg2p/syntaxin 16 'snares' Vps45. EMBO J. 21:2002;3620-3631.
24. Yamaguchi T., et al. Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif. Dev. Cell. 2:2002;295-305.
25. Bryant N.J., James D.E. Vps45p stabilizes the syntaxin homologue Tlg2p and positively regulates SNARE complex formation. EMBO J. 20:2001;3380-3388.
26. Peng R., Gallwitz D. Sly1 protein bound to Golgi syntaxin Sed5p allows assembly and contributes to specificity of SNARE fusion complexes. J. Cell Biol. 157:2002;645-655.
27. Sato T.K., et al. Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion. Mol. Cell. 6:2000;661-671.
28. Sevrioukov E.A., et al. A role for the deep orange and carnation eye color genes in lysosomal delivery in Drosophila. Mol. Cell. 4:1999;479-486.
29. Price A., et al. The docking stage of yeast vacuole fusion requires the transfer of proteins from a cis-SNARE complex to a Rab/Ypt protein. J. Cell Biol. 148:2000;1231-1238.
30. Dulubova I., et al. Vam3p structure reveals conserved and divergent properties of syntaxins. Nat. Struct. Biol. 8:2001;258-264.
31. Kosodo Y., et al. Binding of Sly1 to Sed5 enhances formation of the yeast early Golgi SNARE complex. J. Cell Sci. 115:2002;3683-3691.
32. Yang C., et al. Syntaxin 4 heterozygous knockout mice develop muscle insulin resistance. J. Clin. Invest. 107:2001;1311-1318.
33. Rowe J., et al. Blockade of membrane transport and disassembly of the Golgi complex by expression of syntaxin 1A in neurosecretion-incompetent cells: prevention by rbSEC1. J. Cell Sci. 112:1999;1865-1877.
34. Rowe J., et al. Syntaxin 1A is delivered to the apical and basolateral domains of epithelial cells: the role of munc-18 proteins. J. Cell Sci. 114:2001;3323-3332.
35. Wu M.N., et al. ROP, the Drosophila Sec1 homolog, interacts with syntaxin and regulates neurotransmitter release in a dosage-dependent manner. EMBO J. 17:1998;127-139.
36. Novick P., Schekman R. Secretion and cell-surface growth are blocked in a temperature- sensitive mutant of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 76:1979;1858-1862.
37. Riento K., et al. Munc18-2, a functional partner of syntaxin 3, controls apical membrane trafficking in epithelial cells. J. Biol. Chem. 275:2000;13476-13483.
38. Richmond J.E., et al. An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming. Nature. 412:2001;338-341.
39. Graham M.E., et al. Evidence against an acute inhibitory role of nSec-1 (munc-18) in late steps of regulated exocytosis in chromaffin and PC12 cells. J. Neurochem. 69:1997;2369-2377.
40. Voets T., et al. Munc18-1 promotes large dense-core vesicle docking. Neuron. 31:2001;581-591.
41. Riento K., et al. Interaction of Munc-18-2 with syntaxin 3 controls the association of apical SNAREs in epithelial cells. J. Cell Sci. 111:1998;2681-2688.
42. Thurmond D.C., et al. Regulation of insulin-stimulated GLUT4 translocation by Munc18c in 3T3L1 adipocytes. J. Biol. Chem. 273:1998;33876-33883.
43. Thurmond D.C., et al. Munc18c function is required for insulin-stimulated plasma membrane fusion of GLUT4 and insulin-responsive amino peptidase storage vesicles. Mol. Cell. Biol. 20:2000;379-388.
44. Dresbach T., et al. A neuronal Sec1 homolog regulates neurotransmitter release at the squid giant synapse. J. Neurosci. 18:1998;2923-2932.
45. Schulze K.L., et al. rop, a Drosophila homolog of yeast Sec1 and vertebrate n-Sec1/Munc-18 proteins, is a negative regulator of neurotransmitter release in vivo. Neuron. 13:1994;1099-1108.
46. Fisher R.J., et al. Control of fusion pore dynamics during exocytosis by Munc18. Science. 291:2001;875-878.
47. Sudhof T.C. The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature. 375:1995;645-653.
48. Augustin I., et al. Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles. Nature. 400:1999;457-461.
49. Ashery U., et al. Munc13-1 acts as a priming factor for large dense-core vesicles in bovine chromaffin cells. EMBO J. 19:2000;3586-3596.
50. Cowles C.R., et al. Mutations in the VPS45 gene, a SEC1 homologue, result in vacuolar protein sorting defects and accumulation of membrane vesicles. J. Cell Sci. 107:1994;3449-3459.
51. Cao X., et al. Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins. EMBO J. 17:1998;2156-2165.
52. Ossig R., et al. The yeast SLY gene products, suppressors of defects in the essential GTP-binding Ypt1 protein, may act in endoplasmic reticulum-to-Golgi transport. Mol. Cell. Biol. 11:1991;2980-2993.
53. Finger F.P., Novick P. Synthetic interactions of the post-Golgi sec mutations of Saccharomyces cerevisiae. Genetics. 156:2000;943-951.
54. Salminen A., Novick P.J. A ras-like protein is required for a post-Golgi event in yeast secretion. Cell. 49:1987;527-538.
55. Dascher C., et al. 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. 11:1991;872-885.
56. Grote E., et al. Ordering the final events in yeast exocytosis. J. Cell Biol. 151:2000;439-452.
57. Lerman J.C., et al. Structural analysis of the neuronal SNARE protein syntaxin-1A. Biochemistry. 39:2000;8470-8479.
58. Laage R., Langosch D. Dimerization of the synaptic vesicle protein synaptobrevin (vesicle- associated membrane protein) II depends on specific residues within the transmembrane segment. Eur. J. Biochem. 249:1997;540-546.
59. Margittai M., et al. A stable interaction between syntaxin 1a and synaptobrevin 2 mediated by their transmembrane domains. FEBS Lett. 446:1999;40-44.
60. Lang T., et al. SNAREs in native plasma membranes are active and readily form core complexes with endogenous and exogenous SNAREs. J. Cell Biol. 158:2002;751-760.
61. Fujita Y., et al. Tomosyn: a syntaxin-1-binding protein that forms a novel complex in the neurotransmitter release process. Neuron. 20:1998;905-915.
62. Lehman K., et al. Yeast homologues of tomosyn and lethal giant larvae function in exocytosis and are associated with the plasma membrane SNARE, Sec9. J. Cell Biol. 146:1999;125-140.
63. Sassa T., et al. Regulation of the UNC-18-Caenorhabditis elegans syntaxin complex by UNC- 13. J. Neurosci. 19:1999;4772-4777.
64. Tall G.G., et al. The phosphatidylinositol 3-phosphate binding protein Vac1p interacts with a Rab GTPase and a Sec1p homologue to facilitate vesicle-mediated vacuolar protein sorting. Mol. Biol. Cell. 10:1999;1873-1889.
65. Nielsen E., et al. Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain. J. Cell Biol. 151:2000;601-612.
66. Coppola T., et al. Pancreatic beta-cell protein granuphilin binds Rab3 and Munc-18 and controls exocytosis. Mol. Biol. Cell. 13:2002;1906-1915.
67. Lupashin V.V., Waters M.G. t-SNARE activation through transient interaction with a rab-like guanosine triphosphatase. Science. 276:1997;1255-1258.
68. Banta L.M., et al. Characterization of yeast Vps33p, a protein required for vacuolar protein sorting and vacuole biogenesis. Mol. Cell. Biol. 10:1990;4638-4649.
69. Nichols B.J., et al. The Sec1p homologue Vps45p binds to the syntaxin Tlg2p. Eur. J. Cell Biol. 77:1998;263-268.
70. Abeliovich H., et al. Cytoplasm to vacuole trafficking of aminopeptidase I requires a t-SNARE- Sec1p complex composed of Tlg2p and Vps45p. EMBO J. 18:1999;6005-6016.
71. Webb G.C., et al. Genetic interactions between a pep7 mutation and the PEP12 and VPS45 genes: evidence for a novel SNARE component in transport between the Saccharomyces cerevisiae Golgi complex and endosome. Genetics. 147:1997;467-478.
72. Harrison S.D., et al. Mutations in the Drosophila Rop gene suggest a function in general secretion and synaptic transmission. Neuron. 13:1994;555-566.
73. Wu M.N., et al. The ROP-syntaxin interaction inhibits neurotransmitter release. Eur. J. Cell Biol. 80:2001;196-199.
74. Littleton J.T. A genomic analysis of membrane trafficking and neurotransmitter release in Drosophila. J. Cell Biol. 150:2000;F77-F82.
75. Hosono R., et al. The unc-18 gene encodes a novel protein affecting the kinetics of acetylcholine metabolism in the nematode Caenorhabditis elegans. J. Neurochem. 58:1992;1517-1525.
76. Hata Y., et al. Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin. Nature. 366:1993;347-351.
77. Riento K., et al. A sec1-related vesicle-transport protein that is expressed predominantly in epithelial cells. Eur. J. Biochem. 239:1996;638-646.
78. Tellam J.T., et al. Identification of a mammalian Golgi Sec1p-like protein, mVps45. J. Biol. Chem. 272:1997;6187-6193.
79. Dascher C., Balch W.E. Mammalian Sly1 regulates syntaxin 5 function in endoplasmic reticulum to Golgi transport. J. Biol. Chem. 271:1996;15866-15869.
80. Pevsner J., et al. Mammalian homologues of yeast vacuolar protein sorting (vps) genes implicated in Golgi-to-lysosome trafficking. Gene. 183:1996;7-14.
81. Swanson D.A., et al. Identification and characterization of the human ortholog of rat STXBP1, a protein implicated in vesicle trafficking and neurotransmitter release. Genomics. 48:1998;373-376.
82. Aalto M.K., et al. Yeast syntaxins Sso1p and Sso2p belong to a family of related membrane proteins that function in vesicular transport. EMBO J. 12:1993;4095-4104.
83. Sollner T., et al. A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell. 75:1993;409-418.
84. Sudhof T.C., et al. Membrane fusion machinery: insights from synaptic proteins. Cell. 75:1993;1-4.
85. Schiavo G., et al. Neurotoxins affecting neuroexocytosis. Physiol. Rev. 80:2000;717-766.
86. Jahn R., Sudhof T.C. Membrane fusion and exocytosis. Annu. Rev. Biochem. 68:1999;863-911.
87. Chen Y.A., et al. SNARE complex formation is triggered by Ca2+ and drives membrane fusion. Cell. 97:1999;165-174.
88. Hanson P.I., et al. Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell. 90:1997;523-535.
89. Sutton R.B., et al. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature. 395:1998;347-353.
90. Mayer A., et al. Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles. Cell. 85:1996;83-94.
91. McNew J.A., et al. Compartmental specificity of cellular membrane fusion encoded in SNARE proteins. Nature. 407:2000;153-159.
92. Pevsner J., et al. n-Sec1: a neural-specific syntaxin-binding protein. Proc. Natl. Acad. Sci. U. S. A. 91:1994;1445-1449.
93. Verhage M., et al. DOC2 proteins in rat brain: complementary distribution and proposed function as vesicular adapter proteins in early stages of secretion. Neuron. 18:1997;453-461.
94. Orita S., et al. Doc2: a novel brain protein having two repeated C2-like domains. Biochem. Biophys. Res. Commun. 206:1995;439-448.
95. Borg J.P., et al. Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting. J. Biol. Chem. 273:1998;31633-31636.
96. Borg J.P., et al. Molecular analysis of the X11-mLin-2/CASK complex in brain. J. Neurosci. 19:1999;1307-1316.
97. Butz S., et al. A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Cell. 94:1998;773-782.
98. Rongo C., et al. LIN-10 is a shared component of the polarized protein localization pathways in neurons and epithelia. Cell. 94:1998;751-759.
99. Okamoto M., Sudhof T.C. Mints, Munc18-interacting proteins in synaptic vesicle exocytosis. J. Biol. Chem. 272:1997;31459-31464.
100. Biederer T., Sudhof T.C. Mints as adaptors. Direct binding to neurexins and recruitment of munc18. J. Biol. Chem. 275:2000;39803-39806.
101. Mochida S., et al. Role of the Doc2 alpha-Munc13-1 interaction in the neurotransmitter release process. Proc. Natl. Acad. Sci. U. S. A. 95:1998;11418-11422.
102. Sakaguchi G., et al. Doc2alpha is an activity-dependent modulator of excitatory synaptic transmission. Eur. J. Neurosci. 11:1999;4262-4268.
103. Aalto M.K., et al. Mso1p: a yeast protein that functions in secretion and interacts physically and genetically with Sec1p. Proc. Natl. Acad. Sci. U. S. A. 94:1997;7331-7336.
104. Brose N., et al. Regulation of transmitter release by Unc-13 and its homologues. Curr. Opin. Neurobiol. 10:2000;303-311.
105. 2+-dependent exocytosis. Curr. Opin. Neurobiol. 10:2000;293-302.