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The C-terminal region of ATG101 bridges ULK1 and PtdIns3K complex in autophagy initiation

Authors
Kim, Byeong-WonJin, YunjungKim, JiyeaKim, Jun HoeJung, JuneyoungKang, SeongmanKim, Ick YoungKim, JoungmokCheong, HeesunSong, Hyun Kyu
Issue Date
2-12월-2018
Publisher
TAYLOR & FRANCIS INC
Keywords
ATG13; ATG101; C-terminal region; PtdIns3K complex; structure; ULK1 complex
Citation
AUTOPHAGY, v.14, no.12, pp.2104 - 2116
Indexed
SCIE
SCOPUS
Journal Title
AUTOPHAGY
Volume
14
Number
12
Start Page
2104
End Page
2116
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/71250
DOI
10.1080/15548627.2018.1504716
ISSN
1554-8627
Abstract
The initiation of macroautophagy/autophagy is tightly regulated by the upstream ULK1 kinase complex, which affects many downstream factors including the PtdIns3K complex. The phosphorylation of the right position at the right time on downstream molecules is governed by proper complex formation. One component of the ULK1 complex, ATG101, known as an accessory protein, is a stabilizer of ATG13 in cells. The WF finger region of ATG101 plays an important role in the recruitment of WIPI1 (WD repeat domain, phosphoinositide interacting protein 1) and ZFYVE1 (zinc finger FYVE-type containing 1). Here, we report that the C-terminal region identified in the structure of the human ATG101-ATG13(HORMA) complex is responsible for the binding of the PtdIns3K complex. This region adopts a beta-strand conformation in free ATG101, but either an alpha-helix or random coil in our ATG101-ATG13(HORMA) complex, which protrudes from the core and interacts with other molecules. The C-terminal deletion of ATG101 shows a significant defect in the interaction with PtdIns3K components and subsequently impairs autophagosome formation. This result clearly presents an additional role of ATG101 for bridging the ULK1 and PtdIns3K complexes in the mammalian autophagy process.
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