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Gene Review

VPS8  -  Vps8p

Saccharomyces cerevisiae S288c

Synonyms: FUN15, VPL8, VPT8, Vacuolar protein sorting-associated protein 8, Vacuolar protein-targeting protein 8, ...
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High impact information on VPS8

  • Additional alleles in each of the eight previously identified vpt complementation groups (vpt1 through vpt8) were also obtained [1].
  • At the endosome, Vps33p and other class C members exist as a complex with Vps8p, a protein previously known to act in transport between the late Golgi and the endosome [2].
  • In both vps1 and vps8 cells, newly synthesized mutant Pma1 appears in small punctate structures before arrival at the cell surface [3].
  • Furthermore, a defect in endocytic delivery to the vacuole was revealed in vps8 (and vps36) but not vps1 by endocytosis of the bulk membrane marker FM 4-64 [3].
  • In this study, we have analyzed trafficking in the endosomal system by monitoring the movement of Pma1-7 in vps36, vps1, and vps8 mutants [3].

Biological context of VPS8

  • This sorting is not blocked by a temperature-sensitive mutation in SEC12, which inhibits ER to Golgi transport, a null mutation in VPS8, which inhibits Golgi to PVC transport, or temperature-sensitive and null mutations in END4, which inhibit endocytosis from the plasma membrane [4].
  • To better understand the process of protein sorting to the yeast vacuole, the VPS8 gene was identified and characterized [5].
  • Moreover, in vps8 cells, there is defective down-regulation from the cell surface of the mating receptor Ste3, consistent with persistent receptor recycling from an endosomal compartment to the plasma membrane [3].

Anatomical context of VPS8

  • PEP5 interacts genetically with VPS8, implicating Pep5p in the earlier Golgi to endosome step and/or in recycling from the endosome to the Golgi [6].
  • These observations indicate that ALP is sorted to the vacuole in a Vps8p-independent manner, possibly via an alternative vesicle carrier [7].
  • In vps21 null mutant cells, Vps8p is found in the cytosol [7].
  • This genetic interaction was unexpected, since Pep5p was thought to interact more directly with the vacuole, and Vps8p is thought to play a role in transport between the Golgi complex and the prevacuolar compartment [8].
  • Based on our findings, we propose that Vps8p is part of a protein complex that associates with Golgi and post-Golgi membranes and functions in the retrieval of Golgi membrane proteins from the prevacuolar compartment [5].

Associations of VPS8 with chemical compounds

  • Vps8p contains a C-terminal cysteine-rich region that conforms to the H2 variant of the RING finger Zn2+ binding motif [7].

Other interactions of VPS8

  • This approach identified the VPS3, VPS8 and PEP7 genes that function in vesicular trafficking between the endosome and the yeast vacuole via the carboxypeptidase Y (CpY) pathway [9].
  • We suggest that the ability of the VPS3, VPS8 and PEP7 genes to rescue lethal effects of oxidative damage resulted from the overexpression of these genes [9].
  • The data are consistent with Pep5p functioning both at the site of Vps8p function and more closely proximal to the vacuole [8].


  1. Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases. Robinson, J.S., Klionsky, D.J., Banta, L.M., Emr, S.D. Mol. Cell. Biol. (1988) [Pubmed]
  2. The Sec1/Munc18 protein, Vps33p, functions at the endosome and the vacuole of Saccharomyces cerevisiae. Subramanian, S., Woolford, C.A., Jones, E.W. Mol. Biol. Cell (2004) [Pubmed]
  3. An endosome-to-plasma membrane pathway involved in trafficking of a mutant plasma membrane ATPase in yeast. Luo, W., Chang, A. Mol. Biol. Cell (2000) [Pubmed]
  4. NBD-labeled phosphatidylcholine enters the yeast vacuole via the pre-vacuolar compartment. Hanson, P.K., Grant, A.M., Nichols, J.W. J. Cell. Sci. (2002) [Pubmed]
  5. The VPS8 gene is required for localization and trafficking of the CPY sorting receptor in Saccharomyces cerevisiae. Chen, Y.J., Stevens, T.H. Eur. J. Cell Biol. (1996) [Pubmed]
  6. Pep3p/Pep5p complex: a putative docking factor at multiple steps of vesicular transport to the vacuole of Saccharomyces cerevisiae. Srivastava, A., Woolford, C.A., Jones, E.W. Genetics (2000) [Pubmed]
  7. A novel RING finger protein, Vps8p, functionally interacts with the small GTPase, Vps21p, to facilitate soluble vacuolar protein localization. Horazdovsky, B.F., Cowles, C.R., Mustol, P., Holmes, M., Emr, S.D. J. Biol. Chem. (1996) [Pubmed]
  8. Genetic interaction with vps8-200 allows partial suppression of the vestigial vacuole phenotype caused by a pep5 mutation in Saccharomyces cerevisiae. Woolford, C.A., Bounoutas, G.S., Frew, S.E., Jones, E.W. Genetics (1998) [Pubmed]
  9. Overexpression of genes involved in vesicular trafficking to the vacuole defends against lethal effects of oxidative damage. Martinez, M., Pramanik, A., Moto-Ndje, S., Moore, C.W. Cell. Mol. Biol. (Noisy-le-grand) (2003) [Pubmed]
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