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Different effects of Atg2 and Atg18 mutations on Atg8a and Atg9 trafficking during starvation in Drosophila

Nagy, Péter; Hegedűs, Krisztina; Pircs, Karolina LU ; Varga, Ágnes and Juhász, Gábor (2014) In FEBS Letters 588(3). p.13-408
Abstract

The Atg2-Atg18 complex acts in parallel to Atg8 and regulates Atg9 recycling from phagophore assembly site (PAS) during autophagy in yeast. Here we show that in Drosophila, both Atg9 and Atg18 are required for Atg8a puncta formation, unlike Atg2. Selective autophagic degradation of ubiquitinated proteins is mediated by Ref(2)P/p62. The transmembrane protein Atg9 accumulates on refractory to Sigma P (Ref(2)P) aggregates in Atg7, Atg8a and Atg2 mutants. No accumulation of Atg9 is seen on Ref(2)P in cells lacking Atg18 or Vps34 lipid kinase function, while the Atg1 complex subunit FIP200 is recruited. The simultaneous interaction of Atg18 with both Atg9 and Ref(2)P raises the possibility that Atg18 may facilitate selective degradation of... (More)

The Atg2-Atg18 complex acts in parallel to Atg8 and regulates Atg9 recycling from phagophore assembly site (PAS) during autophagy in yeast. Here we show that in Drosophila, both Atg9 and Atg18 are required for Atg8a puncta formation, unlike Atg2. Selective autophagic degradation of ubiquitinated proteins is mediated by Ref(2)P/p62. The transmembrane protein Atg9 accumulates on refractory to Sigma P (Ref(2)P) aggregates in Atg7, Atg8a and Atg2 mutants. No accumulation of Atg9 is seen on Ref(2)P in cells lacking Atg18 or Vps34 lipid kinase function, while the Atg1 complex subunit FIP200 is recruited. The simultaneous interaction of Atg18 with both Atg9 and Ref(2)P raises the possibility that Atg18 may facilitate selective degradation of ubiquitinated protein aggregates by autophagy.

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author
publishing date
type
Contribution to journal
publication status
published
keywords
Animals, Autophagy, Autophagy-Related Proteins, Carrier Proteins, Drosophila, Drosophila Proteins, Membrane Proteins, Mutation, Protein Transport, Proteolysis, Starvation, Ubiquitinated Proteins, Journal Article, Research Support, Non-U.S. Gov't
in
FEBS Letters
volume
588
issue
3
pages
6 pages
publisher
Wiley-Blackwell
external identifiers
  • scopus:84892810375
ISSN
1873-3468
DOI
10.1016/j.febslet.2013.12.012
language
English
LU publication?
no
id
8182a17d-9fa6-4d8b-9f88-8ea48b0a857f
date added to LUP
2017-03-16 15:27:16
date last changed
2017-08-06 05:19:21
@article{8182a17d-9fa6-4d8b-9f88-8ea48b0a857f,
  abstract     = {<p>The Atg2-Atg18 complex acts in parallel to Atg8 and regulates Atg9 recycling from phagophore assembly site (PAS) during autophagy in yeast. Here we show that in Drosophila, both Atg9 and Atg18 are required for Atg8a puncta formation, unlike Atg2. Selective autophagic degradation of ubiquitinated proteins is mediated by Ref(2)P/p62. The transmembrane protein Atg9 accumulates on refractory to Sigma P (Ref(2)P) aggregates in Atg7, Atg8a and Atg2 mutants. No accumulation of Atg9 is seen on Ref(2)P in cells lacking Atg18 or Vps34 lipid kinase function, while the Atg1 complex subunit FIP200 is recruited. The simultaneous interaction of Atg18 with both Atg9 and Ref(2)P raises the possibility that Atg18 may facilitate selective degradation of ubiquitinated protein aggregates by autophagy.</p>},
  author       = {Nagy, Péter and Hegedűs, Krisztina and Pircs, Karolina and Varga, Ágnes and Juhász, Gábor},
  issn         = {1873-3468},
  keyword      = {Animals,Autophagy,Autophagy-Related Proteins,Carrier Proteins,Drosophila,Drosophila Proteins,Membrane Proteins,Mutation,Protein Transport,Proteolysis,Starvation,Ubiquitinated Proteins,Journal Article,Research Support, Non-U.S. Gov't},
  language     = {eng},
  month        = {01},
  number       = {3},
  pages        = {13--408},
  publisher    = {Wiley-Blackwell},
  series       = {FEBS Letters},
  title        = {Different effects of Atg2 and Atg18 mutations on Atg8a and Atg9 trafficking during starvation in Drosophila},
  url          = {http://dx.doi.org/10.1016/j.febslet.2013.12.012},
  volume       = {588},
  year         = {2014},
}