دورية أكاديمية
أعرض في EDS

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

التفاصيل البيبلوغرافية
العنوان: Different effects of Atg2 and Atg18 mutations on Atg8a and Atg9 trafficking during starvation in Drosophila.
المؤلفون: Nagy P; Department of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest H-1117, Hungary., Hegedűs K; Department of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest H-1117, Hungary., Pircs K; Department of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest H-1117, Hungary., Varga Á; Department of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest H-1117, Hungary., Juhász G; Department of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest H-1117, Hungary. Electronic address: szmrt@elte.hu.
المصدر: FEBS letters [FEBS Lett] 2014 Jan 31; Vol. 588 (3), pp. 408-13. Date of Electronic Publication: 2013 Dec 24.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: John Wiley & Sons Ltd Country of Publication: England NLM ID: 0155157 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-3468 (Electronic) Linking ISSN: 00145793 NLM ISO Abbreviation: FEBS Lett Subsets: MEDLINE
أسماء مطبوعة: Publication: Jan. 2016- : West Sussex : John Wiley & Sons Ltd.
Original Publication: Amsterdam, North-Holland on behalf of the Federation of European Biochemical Societies.
مواضيع طبية MeSH: Autophagy*, Carrier Proteins/*genetics , Drosophila Proteins/*genetics , Membrane Proteins/*genetics, Animals ; Autophagy-Related Proteins ; Drosophila/genetics ; Drosophila/metabolism ; Drosophila Proteins/metabolism ; Membrane Proteins/metabolism ; Mutation ; Protein Transport ; Proteolysis ; Starvation/genetics ; Ubiquitinated Proteins/genetics ; Ubiquitinated Proteins/metabolism
مستخلص: 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.
(Copyright © 2013 The Authors. Published by Elsevier B.V. All rights reserved.)
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معلومات مُعتمدة: United Kingdom Wellcome Trust; 087518 United Kingdom Wellcome Trust
فهرسة مساهمة: Keywords: Atg; Atg18; Atg2; Atg7; Atg8a; Atg9; PAS; PI3P; Ref(2)P; Ref(2)P/p62; ULK; Vps; WD40 repeat domain phosphoinositide-interacting protein; WIPI; autophagy-related; phagophore assembly site; phosphatidylinositol 3-phosphate; refractory to Sigma P; uncoordinated-51 like autophagy kinase; vacuolar protein sorting
المشرفين على المادة: 0 (Atg18a protein, Drosophila)
0 (Atg2 protein, Drosophila)
0 (Atg8a protein, Drosophila)
0 (Atg9 protein, Drosophila)
0 (Autophagy-Related Proteins)
0 (Carrier Proteins)
0 (Drosophila Proteins)
0 (Membrane Proteins)
0 (Ubiquitinated Proteins)
تواريخ الأحداث: Date Created: 20131231 Date Completed: 20140327 Latest Revision: 20211021
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC3928829
DOI: 10.1016/j.febslet.2013.12.012
PMID: 24374083
قاعدة البيانات: MEDLINE
الوصف
تدمد:1873-3468
DOI:10.1016/j.febslet.2013.12.012