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Gene Review

VPS17  -  Vps17p

Saccharomyces cerevisiae S288c

Synonyms: Carboxypeptidase Y-deficient protein 21, O3314, PEP21, VPT3, Vacuolar protein sorting-associated protein 17, ...
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High impact information on VPS17

  • One includes the Vps5p and Vps17p subunits, which provide mechanical force for vesicle budding [1].
  • Density gradient fractionation of Golgi/endosomal/vesicular membranes reveals that Vps35p cofractionates with Vps5p/Vps17p in a vesicle-enriched dense membrane fraction [2].
  • The yeast sorting nexins Vps5p and Vps17p form a dimer and are also components of the retromer complex that mediates endosome-to-Golgi transport of the carboxypeptidase Y receptor Vps10p [3].
  • A sorting nexin-1 homologue, Vps5p, forms a complex with Vps17p and is required for recycling the vacuolar protein-sorting receptor [4].
  • The DNA sequence of the VPS17 clone indicates that the gene encodes a 551-amino-acid protein with a calculated molecular mass of 63.1 kDa [5].

Biological context of VPS17

  • To analyze the role of the VPS17 gene in vacuolar protein delivery, we have cloned this gene by complementation of the vacuolar protein sorting defects of a vps17-5 mutant [5].
  • Disruption of the VPS17 gene had no effect on the viability of haploid yeast cells, although they show an obvious defect in vacuolar morphology. vps17-disrupted cells contain numerous small vacuole-like compartments and also exhibit a severe defect in the sorting of carboxypeptidase Y (CPY), a soluble vacuolar hydrolase [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 [4].
  • Using a Vps17p-specific polyclonal antiserum, we have demonstrated that the Vps17 protein is not modified with N-linked carbohydrates at any of its four potential N-linked glycosylation sites [5].

Anatomical context of VPS17

  • Based on these results, we propose that the Vps17p functions on the cytoplasmic surface of some intracellular organelle, possibly the Golgi complex or an intermediate in Golgi to vacuole transport, to facilitate the sorting and delivery of soluble vacuolar hydrolases [5].

Associations of VPS17 with chemical compounds

  • Vps17p can be released from this particulate fraction by treatment with either Triton X-100 or urea, indicating that the Vps17p is peripherally associated with a crude membrane fraction [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 [6].

Physical interactions of VPS17

  • On the basis of these and other observations, we propose that the Vps17p protein complex may participate in the intracellular trafficking of the Vps10p-sorting receptor, as well as other later-Golgi proteins [4].

Other interactions of VPS17

  • In contrast, the sequences essential for the transcription of EFT1 were localized to the region between the start ATG and the stop codon of the VPS17 gene that terminates 267 nt upstream on the same strand [7].

Analytical, diagnostic and therapeutic context of VPS17


  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. Identification of the functional domains of yeast sorting nexins Vps5p and Vps17p. Seaman, M.N., Williams, H.P. Mol. Biol. Cell (2002) [Pubmed]
  4. 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]
  5. The yeast VPS17 gene encodes a membrane-associated protein required for the sorting of soluble vacuolar hydrolases. Köhrer, K., Emr, S.D. J. Biol. Chem. (1993) [Pubmed]
  6. 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]
  7. Differential transcription of the two Saccharomyces cerevisiae genes encoding elongation factor 2. Veldman, S., Rao, S., Bodley, J.W. Gene (1994) [Pubmed]
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