A human homolog can functionally replace the yeast vesicle-associated SNARE Vti1p in two vesicle transport pathways

Fischer von Mollard G, Stevens TH (1998)
JOURNAL OF BIOLOGICAL CHEMISTRY 273(5): 2624-2630.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Abstract / Bemerkung
Membrane traffic in eukaryotic cells requires the interaction of a vesicle-associated soluble NSF attachment protein receptor (v-SNARE) on transport vesicles with a SNARE on the target membrane (t-SNARE). Recently, we identified the yeast protein Vti1p as a v-SNARE that is involved in two transport reactions. Vti1p interacts with the prevacuolar t-SNARE Pep12p in Golgi to prevacuolar transport and with the cis-Golgi t-SNARE Sed5p in traffic to the cis-Golgi. Here we describe a human Vti1p homolog, hVti1, Whereas vti1 Delta cells are inviable, expression of hVti1 allows vti1 Delta cells to grow at nearly the wild-type growth rate. When expressed in yeast hVti1 can replace Vti1p in both Golgi to prevacuolar transport and in traffic to the cis-Golgi, Sequence comparisons with a Schizosaccharomyces pombe and two different mouse Vti1 homologs led to the identification of a very conserved predicted alpha-helix. Amino acid exchanges in vti1 mutant alleles defective either in one or both trafficking steps cluster in this domain, suggesting that this structure is probably the binding site for effector proteins.
Erscheinungsjahr
1998
Zeitschriftentitel
JOURNAL OF BIOLOGICAL CHEMISTRY
Band
273
Ausgabe
5
Seite(n)
2624-2630
ISSN
0021-9258
Page URI
https://pub.uni-bielefeld.de/record/2374378

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Fischer von Mollard G, Stevens TH. A human homolog can functionally replace the yeast vesicle-associated SNARE Vti1p in two vesicle transport pathways. JOURNAL OF BIOLOGICAL CHEMISTRY. 1998;273(5):2624-2630.
Fischer von Mollard, G., & Stevens, T. H. (1998). A human homolog can functionally replace the yeast vesicle-associated SNARE Vti1p in two vesicle transport pathways. JOURNAL OF BIOLOGICAL CHEMISTRY, 273(5), 2624-2630. https://doi.org/10.1074/jbc.273.5.2624
Fischer von Mollard, Gabriele, and Stevens, TH. 1998. “A human homolog can functionally replace the yeast vesicle-associated SNARE Vti1p in two vesicle transport pathways”. JOURNAL OF BIOLOGICAL CHEMISTRY 273 (5): 2624-2630.
Fischer von Mollard, G., and Stevens, T. H. (1998). A human homolog can functionally replace the yeast vesicle-associated SNARE Vti1p in two vesicle transport pathways. JOURNAL OF BIOLOGICAL CHEMISTRY 273, 2624-2630.
Fischer von Mollard, G., & Stevens, T.H., 1998. A human homolog can functionally replace the yeast vesicle-associated SNARE Vti1p in two vesicle transport pathways. JOURNAL OF BIOLOGICAL CHEMISTRY, 273(5), p 2624-2630.
G. Fischer von Mollard and T.H. Stevens, “A human homolog can functionally replace the yeast vesicle-associated SNARE Vti1p in two vesicle transport pathways”, JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 273, 1998, pp. 2624-2630.
Fischer von Mollard, G., Stevens, T.H.: A human homolog can functionally replace the yeast vesicle-associated SNARE Vti1p in two vesicle transport pathways. JOURNAL OF BIOLOGICAL CHEMISTRY. 273, 2624-2630 (1998).
Fischer von Mollard, Gabriele, and Stevens, TH. “A human homolog can functionally replace the yeast vesicle-associated SNARE Vti1p in two vesicle transport pathways”. JOURNAL OF BIOLOGICAL CHEMISTRY 273.5 (1998): 2624-2630.

32 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Vti1a/b regulate synaptic vesicle and dense core vesicle secretion via protein sorting at the Golgi.
Emperador-Melero J, Huson V, van Weering J, Bollmann C, Fischer von Mollard G, Toonen RF, Verhage M., Nat Commun 9(1), 2018
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Mutations in Membrin/GOSR2 Reveal Stringent Secretory Pathway Demands of Dendritic Growth and Synaptic Integrity.
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Synaptotagmin 11 interacts with components of the RNA-induced silencing complex RISC in clonal pancreatic β-cells.
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The SNARE protein vti1a functions in dense-core vesicle biogenesis.
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Truckenbrodt S, Rizzoli SO., Front Cell Neurosci 8(), 2014
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ER-associated SNAREs and Sey1p mediate nuclear fusion at two distinct steps during yeast mating.
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PMID: 22243751
Lack of the endosomal SNAREs vti1a and vti1b led to significant impairments in neuronal development.
Kunwar AJ, Rickmann M, Backofen B, Browski SM, Rosenbusch J, Schöning S, Fleischmann T, Krieglstein K, Fischer von Mollard G., Proc Natl Acad Sci U S A 108(6), 2011
PMID: 21262811
Syntaxin 16: unraveling cellular physiology through a ubiquitous SNARE molecule.
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Divergent functions of VTI12 and VTI11 in trafficking to storage and lytic vacuoles in Arabidopsis.
Sanmartín M, Ordóñez A, Sohn EJ, Robert S, Sánchez-Serrano JJ, Surpin MA, Raikhel NV, Rojo E., Proc Natl Acad Sci U S A 104(9), 2007
PMID: 17360696
The yeast protein sorting pathway as an experimental model for lysosomal trafficking.
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PMID: 20477111
Extracting sequence motifs and the phylogenetic features of SNARE-dependent membrane traffic.
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i-SNAREs: inhibitory SNAREs that fine-tune the specificity of membrane fusion.
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Syntaxin-6 SNARE involvement in secretory and endocytic pathways of cultured pancreatic beta-cells.
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PMID: 14742717
Deletion of the SNARE vti1b in mice results in the loss of a single SNARE partner, syntaxin 8.
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PMID: 12861006
Yeast Vps55p, a functional homolog of human obesity receptor gene-related protein, is involved in late endosome to vacuole trafficking.
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PMID: 12006663
Exocytosis requires asymmetry in the central layer of the SNARE complex.
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PMID: 11080147
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Jahn R, Südhof TC., Annu Rev Biochem 68(), 1999
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SNAREs and the secretory pathway-lessons from yeast.
Pelham HR., Exp Cell Res 247(1), 1999
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Sanderfoot AA, Raikhel NV., Plant Cell 11(4), 1999
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The plant vesicle-associated SNARE AtVTI1a likely mediates vesicle transport from the trans-Golgi network to the prevacuolar compartment.
Zheng H, von Mollard GF, Kovaleva V, Stevens TH, Raikhel NV., Mol Biol Cell 10(7), 1999
PMID: 10397763
Structures of yeast vesicle trafficking proteins.
Tishgarten T, Yin FF, Faucher KM, Dluhy RA, Grant TR, Fischer von Mollard G, Stevens TH, Lipscomb LA., Protein Sci 8(11), 1999
PMID: 10595551
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Fasshauer D, Sutton RB, Brunger AT, Jahn R., Proc Natl Acad Sci U S A 95(26), 1998
PMID: 9861047

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