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NYV1  -  Nyv1p

Saccharomyces cerevisiae S288c

Synonyms: MAM2, New v-SNARE 1, R-SNARE NYV1, Synaptobrevin NYV1, Vacuolar v-SNARE NYV1, ...
 
 
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High impact information on NYV1

  • Homotypic vacuole fusion requires many membrane proteins, including the Ypt7p guanosine triphosphatase and a "SNARE complex" with Vam3p and Nyv1p [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].
  • 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 [2].
  • The Vtc complex associates with the R-SNARE Nyv1p and with V(0) [3].
  • A YXXPhi-like adaptin-dependent sorting signal (Y(31)GTI(34)) unique to the longin domain of Nyv1p mediates interactions with the AP3 complex in vivo and in vitro [4].
 

Biological context of NYV1

  • We show that amino acid substitutions to Y(31)GTI(34) (Y31Q;I34Q) resulted in mislocalization of Nyv1p as well as reduced binding of the mutant protein to the AP3 complex [4].
  • Development of a semi-quantitative plate-based alpha-galactosidase gene reporter for Schizosaccharomyces pombe and its use to isolate a constitutively active Mam2 [5].
 

Anatomical context of NYV1

  • Vacuole SNAREs, including the t-SNAREs Vam3p and Vam7p and the v-SNARE Nyv1p, are found in a multisubunit "cis" complex on isolated organelles [6].
  • Aut7p interacts physically with the following two v-SNAREs: Bet1p, which is involved in endoplasmic reticulum to Golgi vesicular transport, and Nyv1p, implicated in vacuolar inheritance [7].
  • The vacuolar SNAREs Nyv1p and Vam3p avoid this fate by using the AP-3-dependent pathway, which bypasses late endosomes, but the endosomal SNARE Pep12p must avoid it more directly [8].
 

Associations of NYV1 with chemical compounds

 

Other interactions of NYV1

  • Even in the absence of the vacuolar v-SNARE Nyv1p, a subcomplex which includes Vam7p and the t-SNARE Vam3p is preserved [11].
  • Inhibition of the Ca(2+)-ATPase Pmc1p by the v-SNARE protein Nyv1p [9].
  • We speculate that during vacuole fusion, Nyv1 is the classical R-SNARE, whereas the Ykt6-containing complex has a novel function in Vac8 palmitoylation [12].
  • Although the sorting of Nyv1p to the limiting membrane of the vacuole is dependent upon the Y(31)GTI(34) motif, and Y31 in particular, our findings with structure-based amino acid substitutions in the mu chain (Apm3p) of yeast AP3 suggest a mechanistically distinct role for this subunit in the recognition of YXXPhi-like sorting signals [4].

References

  1. Functional reconstitution of ypt7p GTPase and a purified vacuole SNARE complex. Sato, K., Wickner, W. Science (1998) [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 Vtc proteins in vacuole fusion: coupling NSF activity to V(0) trans-complex formation. Müller, O., Bayer, M.J., Peters, C., Andersen, J.S., Mann, M., Mayer, A. EMBO J. (2002) [Pubmed]
  4. 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]
  5. Development of a semi-quantitative plate-based alpha-galactosidase gene reporter for Schizosaccharomyces pombe and its use to isolate a constitutively active Mam2. Goddard, A., Ladds, G., Davey, J. Yeast (2005) [Pubmed]
  6. 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]
  7. Aut7p, a soluble autophagic factor, participates in multiple membrane trafficking processes. Legesse-Miller, A., Sagiv, Y., Glozman, R., Elazar, Z. J. Biol. Chem. (2000) [Pubmed]
  8. Polar transmembrane domains target proteins to the interior of the yeast vacuole. Reggiori, F., Black, M.W., Pelham, H.R. Mol. Biol. Cell (2000) [Pubmed]
  9. Inhibition of the Ca(2+)-ATPase Pmc1p by the v-SNARE protein Nyv1p. Takita, Y., Engstrom, L., Ungermann, C., Cunningham, K.W. J. Biol. Chem. (2001) [Pubmed]
  10. Acyl-CoA-binding protein, Acb1p, is required for normal vacuole function and ceramide synthesis in Saccharomyces cerevisiae. Faergeman, N.J., Feddersen, S., Christiansen, J.K., Larsen, M.K., Schneiter, R., Ungermann, C., Mutenda, K., Roepstorff, P., Knudsen, J. Biochem. J. (2004) [Pubmed]
  11. Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion. Ungermann, C., Wickner, W. EMBO J. (1998) [Pubmed]
  12. 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]
 
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