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ATG18  -  Atg18p

Saccharomyces cerevisiae S288c

Synonyms: AUT10, Autophagy-related protein 18, CVT18, Cytoplasm to vacuole targeting protein 18, NMR1, ...
 
 
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High impact information on ATG18

  • Atg18p is the most recently identified candidate for a Fab1p effector mediating the largely uncharacterized processes of vesicle fission and membrane recycling at the vacuole [1].
  • To isolate PtdIns(3,5)P2 effectors, we identified Saccharomyces cerevisiae mutants that display fab1delta-like vacuole enlargement, one of which lacked the SVP1/YFR021w/ATG18 gene [2].
  • The activity of Atg18 is vital for all forms of autophagy, whereas Atg21 is required for the Cvt pathway but not for nitrogen starvation-induced autophagy [3].
  • Atg18 is essential for biogenesis of Cvt vesicles and autophagosomes, while Atg21 is only essential for Cvt vesicle formation [4].
  • A biologically active Ha-tagged Aut10p, chromosomally expressed from its endogenous promoter, localizes in indirect immunofluorescence microscopy in the cytosol and on granulated structures, which appear clustered around the vacuolar membrane [5].
 

Biological context of ATG18

  • We have identified a small gene family in Arabidopsis thaliana, members of which show sequence similarity to the yeast autophagy gene ATG18 [6].
 

Anatomical context of ATG18

  • These observations identify Svp1p as a PtdIns(3,5)P2 effector required for PtdIns(3,5)P2-dependent membrane recycling from the vacuole [2].
 

Associations of ATG18 with chemical compounds

  • Atg18 and Atg21 are proteins essential to vesicle formation and together with Ygr223c form a novel family of phosphoinositide binding proteins that are associated with the vacuole and perivacuolar structures [3].
  • In a previous paper [Serrani, F., Rossi, B. and Berardi, E (2001) Nitrogen metabolite repression in Hansenula polymorpha: the nmrl-l mutation. Curr. Genet. 40, 243-250], we identified five loci (NMR1-NMR5) involved in NMR, and characterised one of them (NMR1), which likely identifies a regulatory factor [7].
 

Regulatory relationships of ATG18

  • Rescue is independent of PtdIns(3,5)P(2), as mutation of the phospholipid-binding site in Atg18 does not prevent vacuole fission and properly regulates Fab1p activity [8].
 

Other interactions of ATG18

  • Svp1p is not involved in the contributions of FAB1/PtdIns(3,5)P2 to MVB sorting or to vacuole acidification and so additional PtdIns(3,5)P2 effectors must exist [2].

References

  1. The Fab1 phosphatidylinositol kinase pathway in the regulation of vacuole morphology. Efe, J.A., Botelho, R.J., Emr, S.D. Curr. Opin. Cell Biol. (2005) [Pubmed]
  2. Svp1p defines a family of phosphatidylinositol 3,5-bisphosphate effectors. Dove, S.K., Piper, R.C., McEwen, R.K., Yu, J.W., King, M.C., Hughes, D.C., Thuring, J., Holmes, A.B., Cooke, F.T., Michell, R.H., Parker, P.J., Lemmon, M.A. EMBO J. (2004) [Pubmed]
  3. Atg21 is a phosphoinositide binding protein required for efficient lipidation and localization of Atg8 during uptake of aminopeptidase I by selective autophagy. Strømhaug, P.E., Reggiori, F., Guan, J., Wang, C.W., Klionsky, D.J. Mol. Biol. Cell (2004) [Pubmed]
  4. The relevance of the phosphatidylinositolphosphat-binding motif FRRGT of Atg18 and Atg21 for the Cvt pathway and autophagy. Krick, R., Tolstrup, J., Appelles, A., Henke, S., Thumm, M. FEBS Lett. (2006) [Pubmed]
  5. Autophagy and the cytoplasm to vacuole targeting pathway both require Aut10p. Barth, H., Meiling-Wesse, K., Epple, U.D., Thumm, M. FEBS Lett. (2001) [Pubmed]
  6. AtATG18a is required for the formation of autophagosomes during nutrient stress and senescence in Arabidopsis thaliana. Xiong, Y., Contento, A.L., Bassham, D.C. Plant J. (2005) [Pubmed]
  7. Hansenula polymorpha NMR2 and NMR4, two new loci involved in nitrogen metabolite repression. Rossi, B., Manasse, S., Serrani, F., Berardi, E. FEMS Yeast Res. (2005) [Pubmed]
  8. Atg18 regulates organelle morphology and Fab1 kinase activity independent of its membrane recruitment by phosphatidylinositol 3,5-bisphosphate. Efe, J.A., Botelho, R.J., Emr, S.D. Mol. Biol. Cell (2007) [Pubmed]
 
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