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The 1:2 complex between RavZ and LC3 reveals a mechanism for deconjugation of LC3 on the phagophore membrane

Authors
Kwon, Do HoonKim, SulheeJung, Yang OukRoh, Kyung-HyeKim, LeehyeonKim, Byeong-WonHong, Seung BeomLee, In YoungSong, Ju HanLee, Woo CheolChoi, Eui-JuHwang, Kwang YeonSong, Hyun Kyu
Issue Date
2017
Publisher
TAYLOR & FRANCIS INC
Keywords
ATG4B; crystal structure; LC3; Legionella pneumophila; RavZ; SAXS; xenophagy
Citation
AUTOPHAGY, v.13, no.1, pp.70 - 81
Indexed
SCIE
SCOPUS
Journal Title
AUTOPHAGY
Volume
13
Number
1
Start Page
70
End Page
81
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/86248
DOI
10.1080/15548627.2016.1243199
ISSN
1554-8627
Abstract
Hosts utilize macroautophagy/autophagy to clear invading bacteria; however, bacteria have also developed a specific mechanism to survive by manipulating the host cell autophagy mechanism. One pathogen, Legionella pneumophila, can hinder host cell autophagy by using the specific effector protein RavZ that cleaves phosphatidylethanolamine-conjugated LC3 on the phagophore membrane. However, the detailed molecular mechanisms associated with the function of RavZ have hitherto remained unclear. Here, we report on the biochemical characteristics of the RavZ-LC3 interaction, the solution structure of the 1:2 complex between RavZ and LC3, and crystal structures of RavZ showing different conformations of the active site loop without LC3. Based on our biochemical, structural, and cell-based analyses of RavZ and LC3, both distant flexible N- and C-terminal regions containing LC3-interacting region (LIR) motifs are important for substrate recognition. These results suggest a novel mechanism of RavZ action on the phagophore membrane and lay the groundwork for understanding how bacterial pathogens can survive autophagy.
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