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Gene Review

VPS5  -  Vps5p

Saccharomyces cerevisiae S288c

Synonyms: Carboxypeptidase Y-deficient protein 10, GRD2, PEP10, VPT5, Vacuolar protein sorting-associated protein 5, ...
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High impact information on VPS5

  • One includes the Vps5p and Vps17p subunits, which provide mechanical force for vesicle budding [1].
  • Furthermore, gel filtration analysis indicates that Vps35p and Vps5p are present on a population of vesicles and tubules slightly larger than COPI/coatomer-coated vesicles [2].
  • We also show by immunogold EM that Vps5p is localized to discrete regions at the rims of the prevacuolar endosome where vesicles appear to be budding [2].
  • YOR068c, termed VAM10 (altered vacuole morphology), lies within the VPS5 gene on the opposite DNA strand [3].
  • Sorting nexins (SNX) comprise a family of proteins with homology to several yeast proteins, including Vps5p and Mvp1p, that are required for the sorting of proteins to the yeast vacuole [4].

Biological context of VPS5

  • The VPS5 gene is predicted to encode a very hydrophilic protein of 675 amino acids that shows significant sequence homology with mammalian sorting nexin-1 [5].
  • To explore the role of these VPS gene products in vacuole biogenesis, we cloned and sequenced VPS5 and characterized its protein products [5].
  • Gene disruption experiments show that the VPS5 genes product is not essential for cell viability; however, cells carrying the null allele contain fragmented vacuoles and exhibit defects in vacuolar protein-sorting similar to vps17 null mutants [5].
  • A sorting nexin-1 homologue, Vps5p, forms a complex with Vps17p and is required for recycling the vacuolar protein-sorting receptor [5].

Anatomical context of VPS5

  • Subcellular fractionation studies indicate that Vps5p is associated peripherally with a dense membrane fraction distinct from Golgi, endosomal, and vacuolar membranes [5].
  • Immunofluorescence microscopy experiments show that the membrane-associated pool of Vps5p localizes to an endosome-like organelle that accumulates in the class E vps27 mutant [6].

Associations of VPS5 with chemical compounds

  • Polyclonal antiserum directed against the VPS5 gene product detects a single, cytoplasmic protein that is phosphorylated specifically on a serine residue(s) [5].
  • Interestingly, we measured decreased PtdIns3P levels in Deltavps30 and Deltavps38 cells and observed redistribution of Vps5p and Vps17p to the cytoplasm in these mutants [7].

Other interactions of VPS5

  • Additionally, the Vps10p vacuolar protein-sorting receptor is mislocalized to the vacuole in vps5 mutant cells [5].
  • In yeast cells containing a vps5 null mutation the late Golgi membrane proteins A-ALP and Kex2p were rapidly mislocalized to the vacuolar membrane [6].


  1. The mammalian retromer regulates transcytosis of the polymeric immunoglobulin receptor. Vergés, M., Luton, F., Gruber, C., Tiemann, F., Reinders, L.G., Huang, L., Burlingame, A.L., Haft, C.R., Mostov, K.E. Nat. Cell Biol. (2004) [Pubmed]
  2. A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast. Seaman, M.N., McCaffery, J.M., Emr, S.D. J. Cell Biol. (1998) [Pubmed]
  3. Vam10p defines a Sec18p-independent step of priming that allows yeast vacuole tethering. Kato, M., Wickner, W. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  4. Sorting nexin 6, a novel SNX, interacts with the transforming growth factor-beta family of receptor serine-threonine kinases. Parks, W.T., Frank, D.B., Huff, C., Renfrew Haft, C., Martin, J., Meng, X., de Caestecker, M.P., McNally, J.G., Reddi, A., Taylor, S.I., Roberts, A.B., Wang, T., Lechleider, R.J. J. Biol. Chem. (2001) [Pubmed]
  5. A sorting nexin-1 homologue, Vps5p, forms a complex with Vps17p and is required for recycling the vacuolar protein-sorting receptor. Horazdovsky, B.F., Davies, B.A., Seaman, M.N., McLaughlin, S.A., Yoon, S., Emr, S.D. Mol. Biol. Cell (1997) [Pubmed]
  6. The yeast VPS5/GRD2 gene encodes a sorting nexin-1-like protein required for localizing membrane proteins to the late Golgi. Nothwehr, S.F., Hindes, A.E. J. Cell. Sci. (1997) [Pubmed]
  7. Retromer function in endosome-to-Golgi retrograde transport is regulated by the yeast Vps34 PtdIns 3-kinase. Burda, P., Padilla, S.M., Sarkar, S., Emr, S.D. J. Cell. Sci. (2002) [Pubmed]
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