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

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 pro...

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Autores principales: Nagy, Péter, Hegedűs, Krisztina, Pircs, Karolina, Varga, Ágnes, Juhász, Gábor
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons Ltd 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3928829/
https://www.ncbi.nlm.nih.gov/pubmed/24374083
http://dx.doi.org/10.1016/j.febslet.2013.12.012
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author Nagy, Péter
Hegedűs, Krisztina
Pircs, Karolina
Varga, Ágnes
Juhász, Gábor
author_facet Nagy, Péter
Hegedűs, Krisztina
Pircs, Karolina
Varga, Ágnes
Juhász, Gábor
author_sort Nagy, Péter
collection PubMed
description 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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spelling pubmed-39288292014-03-12 Different effects of Atg2 and Atg18 mutations on Atg8a and Atg9 trafficking during starvation in Drosophila() Nagy, Péter Hegedűs, Krisztina Pircs, Karolina Varga, Ágnes Juhász, Gábor FEBS Lett Article 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. John Wiley & Sons Ltd 2014-01-31 /pmc/articles/PMC3928829/ /pubmed/24374083 http://dx.doi.org/10.1016/j.febslet.2013.12.012 Text en © 2013 The Authors https://creativecommons.org/licenses/by/3.0/This is an open access article under the CC BY license (https://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Nagy, Péter
Hegedűs, Krisztina
Pircs, Karolina
Varga, Ágnes
Juhász, Gábor
Different effects of Atg2 and Atg18 mutations on Atg8a and Atg9 trafficking during starvation in Drosophila()
title Different effects of Atg2 and Atg18 mutations on Atg8a and Atg9 trafficking during starvation in Drosophila()
title_full Different effects of Atg2 and Atg18 mutations on Atg8a and Atg9 trafficking during starvation in Drosophila()
title_fullStr Different effects of Atg2 and Atg18 mutations on Atg8a and Atg9 trafficking during starvation in Drosophila()
title_full_unstemmed Different effects of Atg2 and Atg18 mutations on Atg8a and Atg9 trafficking during starvation in Drosophila()
title_short Different effects of Atg2 and Atg18 mutations on Atg8a and Atg9 trafficking during starvation in Drosophila()
title_sort different effects of atg2 and atg18 mutations on atg8a and atg9 trafficking during starvation in drosophila()
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3928829/
https://www.ncbi.nlm.nih.gov/pubmed/24374083
http://dx.doi.org/10.1016/j.febslet.2013.12.012
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