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Gene Review

ATG7  -  Atg7p

Saccharomyces cerevisiae S288c

Synonyms: APG11, APG7, ATG12-activating enzyme E1 ATG7, Autophagy-related protein 7, CVT2, ...
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High impact information on ATG7

  • Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice [1].
  • Here, we generated conditional knockout mice of Atg7, an essential gene for autophagy in yeast [1].
  • Furthermore, Atg7 deficiency led to multiple cellular abnormalities, such as appearance of concentric membranous structure and deformed mitochondria, and accumulation of ubiquitin-positive aggregates [1].
  • Atg7 was essential for ATG conjugation systems and autophagosome formation, amino acid supply in neonates, and starvation-induced bulk degradation of proteins and organelles in mice [1].
  • This modification requires the carboxy-terminal Gly residue of Apg8FG and Apg7, a ubiquitin E1-like enzyme [2].

Biological context of ATG7

  • Similar to plants missing ATG7, those missing ATG5 display early senescence and are hypersensitive to either nitrogen or carbon starvation, which is accompanied by a more rapid loss of organellar and cytoplasmic proteins [3].
  • Apg7p/Cvt2p: A novel protein-activating enzyme essential for autophagy [4].
  • Evidence is presented here that Apg7p forms a homodimer with two active-site cysteine residues via the C-terminal region [5].
  • The C-terminal 123 amino acids of Apg7p (residues 508 to 630 out of 630 amino acids) are sufficient for its dimerization, where there is neither an ATP binding domain nor an active-site cysteine essential for its E1 activity [5].
  • Apg7p exhibits a considerable similarity to ubiquitin-activating enzyme (E1) and is found to activate Apg12p with ATP hydrolysis [6].

Anatomical context of ATG7

  • Finally, we demonstrate that the Pichia pastoris homologue Gsa7p that is required for peroxisome degradation is functionally similar to Apg7p, indicating that this novel conjugation system may represent a general nonclassical targeting mechanism that is conserved across species [7].
  • We also report here on the ubiquitous expression of human APG7 mRNA in human adult and fetal tissues and of rat Apg7p in adult tissues [8].

Associations of ATG7 with chemical compounds

  • Following induction of peroxisomes by a 2-week treatment with phthalate esters in control and Atg7-deficient livers, peroxisomal degradation was monitored within 1 week after discontinuation of phthalate esters [9].
  • We performed a differential screen on wild-type and Deltaatg7/apg7 autophagy-deficient cells and found that cytosolic acetaldehyde dehydrogenase (Ald6p) decreased under nitrogen starvation [10].
  • Cross-linking experiments and glycerol-gradient centrifugation analysis showed that the mammalian Apg7p homolog forms a homodimer as in yeast Apg7p [11].

Physical interactions of ATG7

  • These results indicated that Apg12p interacts with Apg7p via a thioester bond [4].

Regulatory relationships of ATG7

  • Cells expressing mutant Apg7ps, Apg7pG333A, or Apg7pC507A showed defects in autophagy and cytoplasm-to-vacuole targeting of aminopeptidase I. These results indicated that Apg7p functions as a novel protein-activating enzyme necessary for Apg12p-Apg5p conjugation [4].

Other interactions of ATG7

  • We have generated mutations in apg5 and apg7 that produce defects typically associated with an abrogation of autophagy [12].
  • In this article, we investigated the function of Apg7p as an Apg12p-activating enzyme [4].
  • These reactions require the action of the E1-like enzyme, Apg7p, and the E2-like enzymes, Apg3p and Apg10p [12].
  • Using an Arabidopsis (Arabidopsis thaliana) atg7 mutant unable to ligate either tag, we previously showed that the ATG8/12 conjugation system is important for survival under nitrogen-limiting growth conditions [3].
  • The conjugation reaction was demonstrated to be dependent on Apg7p, which shares homology with the E1 family of ubiquitin-activating enzymes [7].


  1. Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice. Komatsu, M., Waguri, S., Ueno, T., Iwata, J., Murata, S., Tanida, I., Ezaki, J., Mizushima, N., Ohsumi, Y., Uchiyama, Y., Kominami, E., Tanaka, K., Chiba, T. J. Cell Biol. (2005) [Pubmed]
  2. The reversible modification regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway. Kirisako, T., Ichimura, Y., Okada, H., Kabeya, Y., Mizushima, N., Yoshimori, T., Ohsumi, M., Takao, T., Noda, T., Ohsumi, Y. J. Cell Biol. (2000) [Pubmed]
  3. Autophagic nutrient recycling in Arabidopsis directed by the ATG8 and ATG12 conjugation pathways. Thompson, A.R., Doelling, J.H., Suttangkakul, A., Vierstra, R.D. Plant Physiol. (2005) [Pubmed]
  4. Apg7p/Cvt2p: A novel protein-activating enzyme essential for autophagy. Tanida, I., Mizushima, N., Kiyooka, M., Ohsumi, M., Ueno, T., Ohsumi, Y., Kominami, E. Mol. Biol. Cell (1999) [Pubmed]
  5. The C-terminal region of an Apg7p/Cvt2p is required for homodimerization and is essential for its E1 activity and E1-E2 complex formation. Komatsu, M., Tanida, I., Ueno, T., Ohsumi, M., Ohsumi, Y., Kominami, E. J. Biol. Chem. (2001) [Pubmed]
  6. Apg10p, a novel protein-conjugating enzyme essential for autophagy in yeast. Shintani, T., Mizushima, N., Ogawa, Y., Matsuura, A., Noda, T., Ohsumi, Y. EMBO J. (1999) [Pubmed]
  7. Apg7p/Cvt2p is required for the cytoplasm-to-vacuole targeting, macroautophagy, and peroxisome degradation pathways. Kim, J., Dalton, V.M., Eggerton, K.P., Scott, S.V., Klionsky, D.J. Mol. Biol. Cell (1999) [Pubmed]
  8. Murine Apg12p has a substrate preference for murine Apg7p over three Apg8p homologs. Tanida, I., Tanida-Miyake, E., Nishitani, T., Komatsu, M., Yamazaki, H., Ueno, T., Kominami, E. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  9. Excess peroxisomes are degraded by autophagic machinery in mammals. Iwata, J., Ezaki, J., Komatsu, M., Yokota, S., Ueno, T., Tanida, I., Chiba, T., Tanaka, K., Kominami, E. J. Biol. Chem. (2006) [Pubmed]
  10. Ald6p is a preferred target for autophagy in yeast, Saccharomyces cerevisiae. Onodera, J., Ohsumi, Y. J. Biol. Chem. (2004) [Pubmed]
  11. The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3. Tanida, I., Tanida-Miyake, E., Ueno, T., Kominami, E. J. Biol. Chem. (2001) [Pubmed]
  12. Macroautophagy is required for multicellular development of the social amoeba Dictyostelium discoideum. Otto, G.P., Wu, M.Y., Kazgan, N., Anderson, O.R., Kessin, R.H. J. Biol. Chem. (2003) [Pubmed]
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