Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion

Ungermann C, Fischer von Mollard G, Jensen ON, Margolis N, Stevens TH, Wickner W (1999)
JOURNAL OF CELL BIOLOGY 145(7): 1435-1442.

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DOI
Autor*in
Ungermann, C; Fischer von Mollard, GabrieleUniBi ; Jensen, ON; Margolis, N; Stevens, TH; Wickner, W
Einrichtung
Fakultät für Chemie > Biochemie III
Abstract / Bemerkung
Vacuole SNAREs, including the t-SNAREs Vam3p and Vam7p and the V-SNARE Nyv1p, are found in a multisubunit ``cis'' complex on isolated organelles. We now identify the v-SNAREs Vti1p and Ykt6p by mass spectrometry as additional components of the immunoisolated vacuolar SNARE complex. Immunodepletion of detergent extracts with anti-Vti1p removes all the Ykt6p that is in a complex with Vam3p, immunodepletion with anti-Ykt6p removes all the Vti1p that is complexed with Vam3p, and immunodepletion with anti-Nyv1p removes all the Ykt6p in complex with other SNAREs, demonstrating that they are all together in the same cis multi-SNARE complex. After priming, which disassembles the cis-SNARE complex, antibodies to any of the five SNARE proteins still inhibit the fusion assay until the docking stage is completed, suggesting that each SNARE plays a role in docking. Furthermore, vti1 temperature-sensitive alleles cause a synthetic fusion-defective phenotype in our reaction. Our data show that vacuole-vacuole fusion requires a cis-SNARE complex of five SNAREs, the t-SNAREs Vam3p and Vam7p and the v-SNAREs Nyv1p, Vti1p, and Ykt6p.
Erscheinungsjahr
1999
Zeitschriftentitel
JOURNAL OF CELL BIOLOGY
Band
145
Ausgabe
7
Seite(n)
1435-1442
ISSN
0021-9525
Page URI
https://pub.uni-bielefeld.de/record/2374363

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Ungermann C, Fischer von Mollard G, Jensen ON, Margolis N, Stevens TH, Wickner W. Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion. JOURNAL OF CELL BIOLOGY. 1999;145(7):1435-1442.
Ungermann, C., Fischer von Mollard, G., Jensen, O. N., Margolis, N., Stevens, T. H., & Wickner, W. (1999). Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion. JOURNAL OF CELL BIOLOGY, 145(7), 1435-1442. https://doi.org/10.1083/jcb.145.7.1435
Ungermann, C, Fischer von Mollard, Gabriele, Jensen, ON, Margolis, N, Stevens, TH, and Wickner, W. 1999. “Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion”. JOURNAL OF CELL BIOLOGY 145 (7): 1435-1442.
Ungermann, C., Fischer von Mollard, G., Jensen, O. N., Margolis, N., Stevens, T. H., and Wickner, W. (1999). Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion. JOURNAL OF CELL BIOLOGY 145, 1435-1442.
Ungermann, C., et al., 1999. Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion. JOURNAL OF CELL BIOLOGY, 145(7), p 1435-1442.
C. Ungermann, et al., “Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion”, JOURNAL OF CELL BIOLOGY, vol. 145, 1999, pp. 1435-1442.
Ungermann, C., Fischer von Mollard, G., Jensen, O.N., Margolis, N., Stevens, T.H., Wickner, W.: Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion. JOURNAL OF CELL BIOLOGY. 145, 1435-1442 (1999).
Ungermann, C, Fischer von Mollard, Gabriele, Jensen, ON, Margolis, N, Stevens, TH, and Wickner, W. “Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion”. JOURNAL OF CELL BIOLOGY 145.7 (1999): 1435-1442.

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Identification of the components of simple protein mixtures by high-accuracy peptide mass mapping and database searching.
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AUTHOR UNKNOWN, 0
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.
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Lowe M, Nakamura N, Warren G., Trends Cell Biol. 8(1), 1998
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Characterization of a novel yeast SNARE protein implicated in Golgi retrograde traffic.
Lupashin VV, Pokrovskaya ID, McNew JA, Waters MG., Mol. Biol. Cell 8(12), 1997
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Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles.
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Ca2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion.
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The membrane protein alkaline phosphatase is delivered to the vacuole by a route that is distinct from the VPS-dependent pathway.
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Functional reconstitution of ypt7p GTPase and a purified vacuole SNARE complex.
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Vam7p, a SNAP-25-like molecule, and Vam3p, a syntaxin homolog, function together in yeast vacuolar protein trafficking.
Sato TK, Darsow T, Emr SD., Mol. Cell. Biol. 18(9), 1998
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Srivastava A, Jones EW., Genetics 148(1), 1998
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A syntaxin homolog encoded by VAM3 mediates down-regulation of a yeast G protein-coupled receptor.
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Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion.
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Calcium can disrupt the SNARE protein complex on sea urchin egg secretory vesicles without irreversibly blocking fusion.
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Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion.
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A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion.
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Defining the functions of trans-SNARE pairs.
Ungermann C, Sato K, Wickner W., Nature 396(6711), 1998
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Vam3p, a new member of syntaxin related protein, is required for vacuolar assembly in the yeast Saccharomyces cerevisiae.
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AUTHOR UNKNOWN, 0
SNAREpins: minimal machinery for membrane fusion.
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PMID: 9529252
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Thioredoxin is required for vacuole inheritance in Saccharomyces cerevisiae.
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LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion.
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