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Dual roles of Atg8−PE deconjugation by Atg4 in autophagy

Modification of target molecules by ubiquitin or ubiquitin-like (Ubl) proteins is generally reversible. Little is known, however, about the physiological function of the reverse reaction, deconjugation. Atg8 is a unique Ubl protein whose conjugation target is the lipid phosphatidylethanolamine (PE)....

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Autores principales: Yu, Zhong-Qiu, Ni, Tao, Hong, Bing, Wang, Hai-Yan, Jiang, Fen-Jun, Zou, Shenshen, Chen, Yong, Zheng, Xi-Long, Klionsky, Daniel J., Liang, Yongheng, Xie, Zhiping
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3427254/
https://www.ncbi.nlm.nih.gov/pubmed/22652539
http://dx.doi.org/10.4161/auto.19652
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author Yu, Zhong-Qiu
Ni, Tao
Hong, Bing
Wang, Hai-Yan
Jiang, Fen-Jun
Zou, Shenshen
Chen, Yong
Zheng, Xi-Long
Klionsky, Daniel J.
Liang, Yongheng
Xie, Zhiping
author_facet Yu, Zhong-Qiu
Ni, Tao
Hong, Bing
Wang, Hai-Yan
Jiang, Fen-Jun
Zou, Shenshen
Chen, Yong
Zheng, Xi-Long
Klionsky, Daniel J.
Liang, Yongheng
Xie, Zhiping
author_sort Yu, Zhong-Qiu
collection PubMed
description Modification of target molecules by ubiquitin or ubiquitin-like (Ubl) proteins is generally reversible. Little is known, however, about the physiological function of the reverse reaction, deconjugation. Atg8 is a unique Ubl protein whose conjugation target is the lipid phosphatidylethanolamine (PE). Atg8 functions in the formation of double-membrane autophagosomes, a central step in the well-conserved intracellular degradation pathway of macroautophagy (hereafter autophagy). Here we show that the deconjugation of Atg8−PE by the cysteine protease Atg4 plays dual roles in the formation of autophagosomes. During the early stage of autophagosome formation, deconjugation releases Atg8 from non-autophagosomal membranes to maintain a proper supply of Atg8. At a later stage, the release of Atg8 from intermediate autophagosomal membranes facilitates the maturation of these structures into fusion-capable autophagosomes. These results provide new insights into the functions of Atg8−PE and its deconjugation.
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spelling pubmed-34272542012-08-27 Dual roles of Atg8−PE deconjugation by Atg4 in autophagy Yu, Zhong-Qiu Ni, Tao Hong, Bing Wang, Hai-Yan Jiang, Fen-Jun Zou, Shenshen Chen, Yong Zheng, Xi-Long Klionsky, Daniel J. Liang, Yongheng Xie, Zhiping Autophagy Basic Brief Report Modification of target molecules by ubiquitin or ubiquitin-like (Ubl) proteins is generally reversible. Little is known, however, about the physiological function of the reverse reaction, deconjugation. Atg8 is a unique Ubl protein whose conjugation target is the lipid phosphatidylethanolamine (PE). Atg8 functions in the formation of double-membrane autophagosomes, a central step in the well-conserved intracellular degradation pathway of macroautophagy (hereafter autophagy). Here we show that the deconjugation of Atg8−PE by the cysteine protease Atg4 plays dual roles in the formation of autophagosomes. During the early stage of autophagosome formation, deconjugation releases Atg8 from non-autophagosomal membranes to maintain a proper supply of Atg8. At a later stage, the release of Atg8 from intermediate autophagosomal membranes facilitates the maturation of these structures into fusion-capable autophagosomes. These results provide new insights into the functions of Atg8−PE and its deconjugation. Landes Bioscience 2012-06-01 /pmc/articles/PMC3427254/ /pubmed/22652539 http://dx.doi.org/10.4161/auto.19652 Text en Copyright © 2012 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Basic Brief Report
Yu, Zhong-Qiu
Ni, Tao
Hong, Bing
Wang, Hai-Yan
Jiang, Fen-Jun
Zou, Shenshen
Chen, Yong
Zheng, Xi-Long
Klionsky, Daniel J.
Liang, Yongheng
Xie, Zhiping
Dual roles of Atg8−PE deconjugation by Atg4 in autophagy
title Dual roles of Atg8−PE deconjugation by Atg4 in autophagy
title_full Dual roles of Atg8−PE deconjugation by Atg4 in autophagy
title_fullStr Dual roles of Atg8−PE deconjugation by Atg4 in autophagy
title_full_unstemmed Dual roles of Atg8−PE deconjugation by Atg4 in autophagy
title_short Dual roles of Atg8−PE deconjugation by Atg4 in autophagy
title_sort dual roles of atg8−pe deconjugation by atg4 in autophagy
topic Basic Brief Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3427254/
https://www.ncbi.nlm.nih.gov/pubmed/22652539
http://dx.doi.org/10.4161/auto.19652
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