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

Péter Nagy, Krisztina Hegedus, Karolina Pircs, Ágnes Varga, G. Juhász

Research output: Contribution to journalArticle

25 Citations (Scopus)

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 ubiquitinated protein aggregates by autophagy.

Original languageEnglish
Pages (from-to)408-413
Number of pages6
JournalFEBS Letters
Volume588
Issue number3
DOIs
Publication statusPublished - Jan 31 2014

Fingerprint

Ubiquitinated Proteins
Autophagy
Starvation
Drosophila
Degradation
Mutation
Recycling
Refractory materials
Yeast
Phosphotransferases
Yeasts
Lipids
Proteins
Protein Aggregates

Keywords

  • Atg18
  • Atg2
  • Atg7
  • Atg8a
  • Atg9
  • Ref(2)P/p62

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

Cite this

Different effects of Atg2 and Atg18 mutations on Atg8a and Atg9 trafficking during starvation in Drosophila. / Nagy, Péter; Hegedus, Krisztina; Pircs, Karolina; Varga, Ágnes; Juhász, G.

In: FEBS Letters, Vol. 588, No. 3, 31.01.2014, p. 408-413.

Research output: Contribution to journalArticle

Nagy, Péter ; Hegedus, Krisztina ; Pircs, Karolina ; Varga, Ágnes ; Juhász, G. / Different effects of Atg2 and Atg18 mutations on Atg8a and Atg9 trafficking during starvation in Drosophila. In: FEBS Letters. 2014 ; Vol. 588, No. 3. pp. 408-413.
@article{eff4eb169d3140709abb72d3f40f8867,
title = "Different effects of Atg2 and Atg18 mutations on Atg8a and Atg9 trafficking during starvation in Drosophila",
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 ubiquitinated protein aggregates by autophagy.",
keywords = "Atg18, Atg2, Atg7, Atg8a, Atg9, Ref(2)P/p62",
author = "P{\'e}ter Nagy and Krisztina Hegedus and Karolina Pircs and {\'A}gnes Varga and G. Juh{\'a}sz",
year = "2014",
month = "1",
day = "31",
doi = "10.1016/j.febslet.2013.12.012",
language = "English",
volume = "588",
pages = "408--413",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "3",

}

TY - JOUR

T1 - Different effects of Atg2 and Atg18 mutations on Atg8a and Atg9 trafficking during starvation in Drosophila

AU - Nagy, Péter

AU - Hegedus, Krisztina

AU - Pircs, Karolina

AU - Varga, Ágnes

AU - Juhász, G.

PY - 2014/1/31

Y1 - 2014/1/31

N2 - 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.

AB - 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.

KW - Atg18

KW - Atg2

KW - Atg7

KW - Atg8a

KW - Atg9

KW - Ref(2)P/p62

UR - http://www.scopus.com/inward/record.url?scp=84892810375&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84892810375&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2013.12.012

DO - 10.1016/j.febslet.2013.12.012

M3 - Article

C2 - 24374083

AN - SCOPUS:84892810375

VL - 588

SP - 408

EP - 413

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 3

ER -