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Gene Review

VTI1  -  Vti1p

Saccharomyces cerevisiae S288c

Synonyms: Qb-SNARE VTI1, VPS10-interacting protein 1, Vesicle transport v-SNARE protein VTI1, YM9646.10C, YMR197C, ...
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High impact information on VTI1

  • Furthermore, temperature-conditional mutations in the Class C VPS genes destabilized Vam3-Vti1-Vam7 pairing [1].
  • Vam3 pairs with the SNAP-25 homolog Vam7 and VAMP homolog Vti1 to form SNARE complexes during vesicle docking/fusion with the vacuole [1].
  • In 'bypass fusion', without ATP but with added rVam7p, there are sufficient unpaired vacuolar SNAREs Vam3p, Vti1p, and Nyv1p to interact with Vam7p and support fusion [2].
  • Antibody inhibition experiments coupled with antigen competition indicated a requirement for soluble NSF attachment protein receptor (SNARE) proteins Tlg1p, Tlg2p, and Vti1p in this reaction [3].
  • We now identify the v-SNAREs Vti1p and Ykt6p by mass spectrometry as additional components of the immunoisolated vacuolar SNARE complex [4].

Biological context of VTI1


Anatomical context of VTI1

  • VTI1 interacts genetically with the vacuolar t-SNARE VAM3, which is required for transport of both alkaline phosphatase and aminopeptidase I to the vacuole [6].
  • Here we identify Vti1p as the first v-SNARE protein found to be required for biosynthetic traffic into the yeast vacuole, the equivalent of the mammalian lysosome [6].
  • The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p [5].

Associations of VTI1 with chemical compounds

  • First, we showed that Sec18p (N-ethylmaleimide-sensitive fusion protein, NSF) and Vti1p (soluble N-ethylmaleimide-sensitive fusion protein attachment protein, SNARE), and soluble N-ethylmaleimide-sensitive fusion protein receptor are required for fusion of the autophagosome to the vacuole but are not involved in autophagosome formation [7].

Physical interactions of VTI1

  • However, Vti1p also functions in two additional membrane traffic pathways: Vti1p interacts with the t-SNAREs Pep12p in traffic from the TGN to the prevacuolar compartment and with Sed5p in retrograde traffic to the cis-Golgi [6].

Other interactions of VTI1

  • Genetic interactions with the yeast Q-SNARE VTI1 reveal novel functions for the R-SNARE YKT6 [8].

Analytical, diagnostic and therapeutic context of VTI1

  • This paper describes circular dichroism, Fourier transform infrared spectroscopy, and dynamic light scattering data for a set of yeast v- and t-SNARE proteins, Vti1p and Pep12p, that are Q-SNAREs involved in intracellular trafficking [9].


  1. Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion. Sato, T.K., Rehling, P., Peterson, M.R., Emr, S.D. Mol. Cell (2000) [Pubmed]
  2. A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion. Thorngren, N., Collins, K.M., Fratti, R.A., Wickner, W., Merz, A.J. EMBO J. (2004) [Pubmed]
  3. The Tlg SNARE complex is required for TGN homotypic fusion. Brickner, J.H., Blanchette, J.M., Sipos, G., Fuller, R.S. J. Cell Biol. (2001) [Pubmed]
  4. Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion. Ungermann, C., von Mollard, G.F., Jensen, O.N., Margolis, N., Stevens, T.H., Wickner, W. J. Cell Biol. (1999) [Pubmed]
  5. The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p. von Mollard, G.F., Nothwehr, S.F., Stevens, T.H. J. Cell Biol. (1997) [Pubmed]
  6. The Saccharomyces cerevisiae v-SNARE Vti1p is required for multiple membrane transport pathways to the vacuole. Fischer von Mollard, G., Stevens, T.H. Mol. Biol. Cell (1999) [Pubmed]
  7. Autophagosome requires specific early Sec proteins for its formation and NSF/SNARE for vacuolar fusion. Ishihara, N., Hamasaki, M., Yokota, S., Suzuki, K., Kamada, Y., Kihara, A., Yoshimori, T., Noda, T., Ohsumi, Y. Mol. Biol. Cell (2001) [Pubmed]
  8. Genetic interactions with the yeast Q-SNARE VTI1 reveal novel functions for the R-SNARE YKT6. Dilcher, M., Köhler, B., von Mollard, G.F. J. Biol. Chem. (2001) [Pubmed]
  9. Structures of yeast vesicle trafficking proteins. Tishgarten, T., Yin, F.F., Faucher, K.M., Dluhy, R.A., Grant, T.R., Fischer von Mollard, G., Stevens, T.H., Lipscomb, L.A. Protein Sci. (1999) [Pubmed]
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