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Gene Review

YKT6  -  palmitoyltransferase YKT6

Saccharomyces cerevisiae S288c

Synonyms: Synaptobrevin homolog YKT6, YKL196C
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Disease relevance of YKT6


High impact information on YKT6

  • Other v-SNAREs, Sec22p and Ykt6p, might interact more weakly with the COPII coat or interact indirectly by binding to Bet1p or Bos1p [3].
  • High concentrations of rVam7p allow the R-SNARE Ykt6p to substitute for Nyv1p for fusion; this functional redundancy among vacuole SNAREs may explain why nyv1delta strains lack the vacuole fragmentation seen with mutants in other fusion catalysts [4].
  • We now identify the v-SNAREs Vti1p and Ykt6p by mass spectrometry as additional components of the immunoisolated vacuolar SNARE complex [5].
  • Weaker suppression is evident upon overexpression of genes encoding the vesicle tethering factor Uso1p or the vesicle-SNAREs Sec22p, Bet1p, or Ykt6p [6].
  • In contrast, we found that the longin domains of Sec22p and Ykt6p were not sufficient to direct their localization [7].

Biological context of YKT6


Anatomical context of YKT6

  • To investigate the role of Ykt6p in membrane traffic to the vacuole we generated temperature-sensitive mutations in YKT6 [13].
  • Using antibodies specific for mammalian Ykt6, it is revealed that it is found mainly in Golgi-enriched membranes [1].
  • It is concluded that Ykt6 functions in a late step of ER-Golgi transport, and this role may be important for the integrity of the Golgi complex [1].
  • The yeast SNARE Ykt6p has been implicated in several trafficking steps, including vesicular transport from the endoplasmic reticulum (ER) to the Golgi, intra-Golgi transport, and homotypic vacuole fusion [1].
  • Ykt6 is localized equally to membranes and the cytosol, although it is unclear how this distribution is mediated [12].

Associations of YKT6 with chemical compounds

  • SNARE complexes to which Ykt6p contributed a fourth glutamine residue in the 0 layer were nonfunctional, suggesting an essential function for arginine in the 0 layer of these complexes. vti1-Q158R cells had severe defects in several transport steps, indicating that the second arginine in the 0 layer interfered with function [14].

Other interactions of YKT6

  • Here we identified a previously uncharacterized gene, VTS1, and the R-SNARE YKT6 both as multicopy and as low copy suppressors of the growth and vacuolar transport defect in vti1-2 cells [14].
  • A second set of mutations in YKT6 specifically affects post-Golgi membrane traffic to the vacuole, and the effects of these mutations are not suppressed by Sft1p overexpression [13].
  • This rescue is attributed to the involvement of Sed5p and Ykt6p in a different SNARE complex that functions in intra-Golgi trafficking [15].
  • Recently, we discovered that Ykt6 mediates the amino-terminal acylation of the fusion protein Vac8 [16].
  • We now know of three proteins in Saccharomyces cerevisiae that promote palmitoylation: effector of Ras function (Erf2), ankyrin-repeat-containing protein (Akr1) and the SNARE protein Ykt6 [16].

Analytical, diagnostic and therapeutic context of YKT6


  1. Ykt6 forms a SNARE complex with syntaxin 5, GS28, and Bet1 and participates in a late stage in endoplasmic reticulum-Golgi transport. Zhang, T., Hong, W. J. Biol. Chem. (2001) [Pubmed]
  2. Chromatographic purification of an insoluble histidine tag recombinant Ykt6p SNARE from Arabidopsis thaliana over-expressed in E. coli. Vincent, P., Dieryck, W., Maneta-Peyret, L., Moreau, P., Cassagne, C., Santarelli, X. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. (2004) [Pubmed]
  3. Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs. Springer, S., Schekman, R. Science (1998) [Pubmed]
  4. 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]
  5. 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]
  6. Sec34p, a protein required for vesicle tethering to the yeast Golgi apparatus, is in a complex with Sec35p. VanRheenen, S.M., Cao, X., Sapperstein, S.K., Chiang, E.C., Lupashin, V.V., Barlowe, C., Waters, M.G. J. Cell Biol. (1999) [Pubmed]
  7. Identification of the Yeast R-SNARE Nyv1p as a Novel Longin Domain-containing Protein. Wen, W., Chen, L., Wu, H., Sun, X., Zhang, M., Banfield, D.K. Mol. Biol. Cell (2006) [Pubmed]
  8. Yeast Golgi SNARE interactions are promiscuous. Tsui, M.M., Banfield, D.K. J. Cell. Sci. (2000) [Pubmed]
  9. YKT6 is a core constituent of membrane fusion machineries at the Arabidopsis trans-Golgi network. Chen, Y., Shin, Y.K., Bassham, D.C. J. Mol. Biol. (2005) [Pubmed]
  10. ATP-independent control of Vac8 palmitoylation by a SNARE subcomplex on yeast vacuoles. Dietrich, L.E., LaGrassa, T.J., Rohde, J., Cristodero, M., Meiringer, C.T., Ungermann, C. J. Biol. Chem. (2005) [Pubmed]
  11. Ric1p and the Ypt6p GTPase function in a common pathway required for localization of trans-Golgi network membrane proteins. Bensen, E.S., Yeung, B.G., Payne, G.S. Mol. Biol. Cell (2001) [Pubmed]
  12. The SNARE Ykt6 is released from yeast vacuoles during an early stage of fusion. Dietrich, L.E., Peplowska, K., LaGrassa, T.J., Hou, H., Rohde, J., Ungermann, C. EMBO Rep. (2005) [Pubmed]
  13. Ykt6p is a multifunctional yeast R-SNARE that is required for multiple membrane transport pathways to the vacuole. Kweon, Y., Rothe, A., Conibear, E., Stevens, T.H. Mol. Biol. Cell (2003) [Pubmed]
  14. 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]
  15. Identification of functionally interacting SNAREs by using complementary substitutions in the conserved '0' layer. Graf, C.T., Riedel, D., Schmitt, H.D., Jahn, R. Mol. Biol. Cell (2005) [Pubmed]
  16. On the mechanism of protein palmitoylation. Dietrich, L.E., Ungermann, C. EMBO Rep. (2004) [Pubmed]
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