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A semisynthetic Atg3 reveals that acetylation promotes Atg3 membrane binding and Atg8 lipidation
Acetylation of Atg3 regulates the lipidation of the protein Atg8 in autophagy. The molecular mechanism behind this important biochemical event remains to be elucidated. We describe the first semi-synthesis of homogeneous K19/K48-diacetylated Atg3 through sequential hydrazide-based native chemical li...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5473643/ https://www.ncbi.nlm.nih.gov/pubmed/28327644 http://dx.doi.org/10.1038/ncomms14846 |
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author | Li, Yi-Tong Yi, Cong Chen, Chen-Chen Lan, Huan Pan, Man Zhang, Shao-Jin Huang, Yi-Chao Guan, Chao-Jian Li, Yi-Ming Yu, Li Liu, Lei |
author_facet | Li, Yi-Tong Yi, Cong Chen, Chen-Chen Lan, Huan Pan, Man Zhang, Shao-Jin Huang, Yi-Chao Guan, Chao-Jian Li, Yi-Ming Yu, Li Liu, Lei |
author_sort | Li, Yi-Tong |
collection | PubMed |
description | Acetylation of Atg3 regulates the lipidation of the protein Atg8 in autophagy. The molecular mechanism behind this important biochemical event remains to be elucidated. We describe the first semi-synthesis of homogeneous K19/K48-diacetylated Atg3 through sequential hydrazide-based native chemical ligation. In vitro reconstitution experiments with the semi-synthetic proteins confirm that Atg3 acetylation can promote the lipidation of Atg8. We find that acetylation of Atg3 enhances its binding to phosphatidylethanolamine-containing liposomes and to endoplasmic reticulum, through which it promotes the lipidation process. |
format | Online Article Text |
id | pubmed-5473643 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-54736432017-06-28 A semisynthetic Atg3 reveals that acetylation promotes Atg3 membrane binding and Atg8 lipidation Li, Yi-Tong Yi, Cong Chen, Chen-Chen Lan, Huan Pan, Man Zhang, Shao-Jin Huang, Yi-Chao Guan, Chao-Jian Li, Yi-Ming Yu, Li Liu, Lei Nat Commun Article Acetylation of Atg3 regulates the lipidation of the protein Atg8 in autophagy. The molecular mechanism behind this important biochemical event remains to be elucidated. We describe the first semi-synthesis of homogeneous K19/K48-diacetylated Atg3 through sequential hydrazide-based native chemical ligation. In vitro reconstitution experiments with the semi-synthetic proteins confirm that Atg3 acetylation can promote the lipidation of Atg8. We find that acetylation of Atg3 enhances its binding to phosphatidylethanolamine-containing liposomes and to endoplasmic reticulum, through which it promotes the lipidation process. Nature Publishing Group 2017-03-22 /pmc/articles/PMC5473643/ /pubmed/28327644 http://dx.doi.org/10.1038/ncomms14846 Text en Copyright © 2017, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Li, Yi-Tong Yi, Cong Chen, Chen-Chen Lan, Huan Pan, Man Zhang, Shao-Jin Huang, Yi-Chao Guan, Chao-Jian Li, Yi-Ming Yu, Li Liu, Lei A semisynthetic Atg3 reveals that acetylation promotes Atg3 membrane binding and Atg8 lipidation |
title | A semisynthetic Atg3 reveals that acetylation promotes Atg3 membrane binding and Atg8 lipidation |
title_full | A semisynthetic Atg3 reveals that acetylation promotes Atg3 membrane binding and Atg8 lipidation |
title_fullStr | A semisynthetic Atg3 reveals that acetylation promotes Atg3 membrane binding and Atg8 lipidation |
title_full_unstemmed | A semisynthetic Atg3 reveals that acetylation promotes Atg3 membrane binding and Atg8 lipidation |
title_short | A semisynthetic Atg3 reveals that acetylation promotes Atg3 membrane binding and Atg8 lipidation |
title_sort | semisynthetic atg3 reveals that acetylation promotes atg3 membrane binding and atg8 lipidation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5473643/ https://www.ncbi.nlm.nih.gov/pubmed/28327644 http://dx.doi.org/10.1038/ncomms14846 |
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