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Gene Review

VPS30  -  Vps30p

Saccharomyces cerevisiae S288c

Synonyms: APG6, ATG6, Autophagy-related protein 6, LPH7, VPT30, ...
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High impact information on VPS30

  • Here we show that plant BECLIN 1, an ortholog of the yeast and mammalian autophagy gene ATG6/VPS30/beclin 1, functions to restrict HR PCD to infection sites [1].
  • These results indicate that Vps30p functions as a subunit of a Vps34 PtdIns 3-kinase complex(es) [2].
  • Although Vps30p is known to interact with Apg14p, its precise role remains unclear [2].
  • The sequences of the VPS29, VPS30, and VPS35 genes do not yet give any clues to the functions of their products [3].
  • Vps34p and Vps30p, components shared by the two complexes, localized to the PAS, vacuolar membranes, and several punctate structures that included endosomes [4].

Biological context of VPS30

  • We observed that mutations in the VPS30 and VPS38 genes led to a selective sorting and maturation phenotype of the soluble vacuolar protease CPY [5].
  • Apg14p and Apg6/Vps30p form a protein complex essential for autophagy in the yeast, Saccharomyces cerevisiae [6].
  • These results imply that Apg6/Vps30p has two distinct functions in the autophagic process and the vacuolar protein sorting pathway [6].
  • Using nematodes with a loss-of-function mutation in the insulin-like signaling pathway, we show that bec-1, the C. elegans ortholog of the yeast and mammalian autophagy gene APG6/VPS30/beclin1, is essential for normal dauer morphogenesis and life-span extension [7].

Associations of VPS30 with chemical compounds

  • The defect in one of these mutants, add3, was complemented by VPS30/ATG6, a gene that encodes a component of two phosphatidylinositol 3-kinase (PtdIns 3-kinase) complexes: complex I is required for autophagy, whereas complex II is required for the carboxypeptidase Y (CPY)-to-vacuole pathway [8].

Physical interactions of VPS30

  • Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex [6].

Other interactions of VPS30

  • Subcellular fractionation indicated that Apg14p and Apg6p peripherally associated with a membrane structure(s) [6].
  • The distribution of a green fluorescent protein fusion of the autophagosome marker, Atg8, is aberrant in both atg1-1 and atg6(-) mutants [9].


  1. Autophagy regulates programmed cell death during the plant innate immune response. Liu, Y., Schiff, M., Czymmek, K., Tallóczy, Z., Levine, B., Dinesh-Kumar, S.P. Cell (2005) [Pubmed]
  2. Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae. Kihara, A., Noda, T., Ishihara, N., Ohsumi, Y. J. Cell Biol. (2001) [Pubmed]
  3. Endosome to Golgi retrieval of the vacuolar protein sorting receptor, Vps10p, requires the function of the VPS29, VPS30, and VPS35 gene products. Seaman, M.N., Marcusson, E.G., Cereghino, J.L., Emr, S.D. J. Cell Biol. (1997) [Pubmed]
  4. Assortment of phosphatidylinositol 3-kinase complexes--Atg14p directs association of complex i to the pre-autophagosomal structure in Saccharomyces cerevisiae. Obara, K., Sekito, T., Ohsumi, Y. Mol. Biol. Cell (2006) [Pubmed]
  5. 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]
  6. Apg14p and Apg6/Vps30p form a protein complex essential for autophagy in the yeast, Saccharomyces cerevisiae. Kametaka, S., Okano, T., Ohsumi, M., Ohsumi, Y. J. Biol. Chem. (1998) [Pubmed]
  7. Autophagy genes are essential for dauer development and life-span extension in C. elegans. Meléndez, A., Tallóczy, Z., Seaman, M., Eskelinen, E.L., Hall, D.H., Levine, B. Science (2003) [Pubmed]
  8. Characterization of an ERAD gene as VPS30/ATG6 reveals two alternative and functionally distinct protein quality control pathways: one for soluble Z variant of human alpha-1 proteinase inhibitor (A1PiZ) and another for aggregates of A1PiZ. Kruse, K.B., Brodsky, J.L., McCracken, A.A. Mol. Biol. Cell (2006) [Pubmed]
  9. Dictyostelium macroautophagy mutants vary in the severity of their developmental defects. Otto, G.P., Wu, M.Y., Kazgan, N., Anderson, O.R., Kessin, R.H. J. Biol. Chem. (2004) [Pubmed]
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