A semisynthetic Atg3 reveals that acetylation promotes Atg3 membrane binding and Atg8 lipidation-Reference-Cited by-同舟云学术

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A semisynthetic Atg3 reveals that acetylation promotes Atg3 membrane binding and Atg8 lipidation

Published:2017-03-22 Issue:1 Volume:8 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

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

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/ncomms14846.pdf

Reference33 articles.

1. Mizushima, N. & Komatsu, M. Autophagy: renovation of cells and tissues. Cell 147, 728–741 (2011).

2. Levine, B., Mizushima, N. & Virgin, H. W. Autophagy in immunity and inflammation. Nature 469, 323–335 (2011).

3. Kaiser, S. E. et al. Noncanonical E2 recruitment by the autophagy E1 revealed by Atg7-Atg3 and Atg7-Atg10 structures. Nat. Struct. Mol. Biol. 19, 1242–1249 (2012).

4. Sakoh-Nakatogawa, M. et al. Atg12-Atg5 conjugate enhances E2 activity of Atg3 by rearranging its catalytic site. Nat. Struct. Mol. Biol. 20, 433–439 (2013).

5. Hanada, T. et al. The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy. J. Biol. Chem. 282, 37298–37302 (2007).

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