The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

ATG4  -  Atg4p

Saccharomyces cerevisiae S288c

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

High impact information on ATG4

 

Biological context of ATG4

  • Atg4B, a mammalian homologue of yeast Atg4, has been shown to play an important role in the processing of LC3, a mammalian homologue of yeast Atg8, but the tissue distribution of Atg4B remains unknown [5].
 

Anatomical context of ATG4

  • After synthesis in the cytosol, Aut7p is proteolytically cleaved in an Aut2p-dependent manner [2].
  • Using a cell-free system, we found that HsAtg4B, one of the human Atg4 homologues, cleaves the carboxyl termini of these three Atg8 homologues [6].
 

Associations of ATG4 with chemical compounds

  • First, the carboxy-terminal Arg residue of newly synthesized Apg8 is removed by Apg4/Aut2, a novel cysteine protease, and a Gly residue becomes the carboxy-terminal residue of the protein that is now designated Apg8FG [7].
 

Analytical, diagnostic and therapeutic context of ATG4

References

  1. A ubiquitin-like system mediates protein lipidation. Ichimura, Y., Kirisako, T., Takao, T., Satomi, Y., Shimonishi, Y., Ishihara, N., Mizushima, N., Tanida, I., Kominami, E., Ohsumi, M., Noda, T., Ohsumi, Y. Nature (2000) [Pubmed]
  2. Membrane recruitment of Aut7p in the autophagy and cytoplasm to vacuole targeting pathways requires Aut1p, Aut2p, and the autophagy conjugation complex. Kim, J., Huang, W.P., Klionsky, D.J. J. Cell Biol. (2001) [Pubmed]
  3. Aut2p and Aut7p, two novel microtubule-associated proteins are essential for delivery of autophagic vesicles to the vacuole. Lang, T., Schaeffeler, E., Bernreuther, D., Bredschneider, M., Wolf, D.H., Thumm, M. EMBO J. (1998) [Pubmed]
  4. Human autophagins, a family of cysteine proteinases potentially implicated in cell degradation by autophagy. Mariño, G., Uría, J.A., Puente, X.S., Quesada, V., Bordallo, J., López-Otín, C. J. Biol. Chem. (2003) [Pubmed]
  5. Effects of RNA Interference of Atg4B on the Limited Proteolysis of LC3 in PC12 Cells and Expression of Atg4B in Various Rat Tissues. Yoshimura, K., Shibata, M., Koike, M., Gotoh, K., Fukaya, M., Watanabe, M., Uchiyama, Y. Autophagy. (2006) [Pubmed]
  6. HsAtg4B/HsApg4B/autophagin-1 cleaves the carboxyl termini of three human Atg8 homologues and delipidates microtubule-associated protein light chain 3- and GABAA receptor-associated protein-phospholipid conjugates. Tanida, I., Sou, Y.S., Ezaki, J., Minematsu-Ikeguchi, N., Ueno, T., Kominami, E. J. Biol. Chem. (2004) [Pubmed]
  7. 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]
  8. Arabidopsis homologues of the autophagy protein Atg8 are a novel family of microtubule binding proteins. Ketelaar, T., Voss, C., Dimmock, S.A., Thumm, M., Hussey, P.J. FEBS Lett. (2004) [Pubmed]
 
WikiGenes - Universities