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, 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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Lack of the endosomal SNAREs vti1a and vti1b led to significant impairments in neuronal development.
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Deletion of the SNARE vti1b in mice results in the loss of a single SNARE partner, syntaxin 8.
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The plant vesicle-associated SNARE AtVTI1a likely mediates vesicle transport from the trans-Golgi network to the prevacuolar compartment.
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Structures of yeast vesicle trafficking proteins.
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