Multi-site-mediated entwining of the linear WIR-motif around WIPI β-propellers for autophagy

WIPI proteins are mammalian PROPPIN family phosphoinositide effectors that recognize a WIPI-interacting-region (WIR)-motif to recruit other regulators during autophagosome formation. Here, the authors combine structural and functional studies and present the crystal structure of human WIPI3 with a b...

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Autores principales: Jinqi Ren, Ruobing Liang, Wenjuan Wang, Dachuan Zhang, Li Yu, Wei Feng
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/db704a1b9bd64094a44afc4f6fbb4ddb
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spelling oai:doaj.org-article:db704a1b9bd64094a44afc4f6fbb4ddb2021-12-02T15:57:09ZMulti-site-mediated entwining of the linear WIR-motif around WIPI β-propellers for autophagy10.1038/s41467-020-16523-y2041-1723https://doaj.org/article/db704a1b9bd64094a44afc4f6fbb4ddb2020-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16523-yhttps://doaj.org/toc/2041-1723WIPI proteins are mammalian PROPPIN family phosphoinositide effectors that recognize a WIPI-interacting-region (WIR)-motif to recruit other regulators during autophagosome formation. Here, the authors combine structural and functional studies and present the crystal structure of human WIPI3 with a bound ATG2A WIR-peptide and observe that the WIR-motif binds to three sites in blades 1-3 of WIPI3 and mutating these binding sites impairs the ATG2A-mediated autophagic process.Jinqi RenRuobing LiangWenjuan WangDachuan ZhangLi YuWei FengNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Jinqi Ren
Ruobing Liang
Wenjuan Wang
Dachuan Zhang
Li Yu
Wei Feng
Multi-site-mediated entwining of the linear WIR-motif around WIPI β-propellers for autophagy
description WIPI proteins are mammalian PROPPIN family phosphoinositide effectors that recognize a WIPI-interacting-region (WIR)-motif to recruit other regulators during autophagosome formation. Here, the authors combine structural and functional studies and present the crystal structure of human WIPI3 with a bound ATG2A WIR-peptide and observe that the WIR-motif binds to three sites in blades 1-3 of WIPI3 and mutating these binding sites impairs the ATG2A-mediated autophagic process.
format article
author Jinqi Ren
Ruobing Liang
Wenjuan Wang
Dachuan Zhang
Li Yu
Wei Feng
author_facet Jinqi Ren
Ruobing Liang
Wenjuan Wang
Dachuan Zhang
Li Yu
Wei Feng
author_sort Jinqi Ren
title Multi-site-mediated entwining of the linear WIR-motif around WIPI β-propellers for autophagy
title_short Multi-site-mediated entwining of the linear WIR-motif around WIPI β-propellers for autophagy
title_full Multi-site-mediated entwining of the linear WIR-motif around WIPI β-propellers for autophagy
title_fullStr Multi-site-mediated entwining of the linear WIR-motif around WIPI β-propellers for autophagy
title_full_unstemmed Multi-site-mediated entwining of the linear WIR-motif around WIPI β-propellers for autophagy
title_sort multi-site-mediated entwining of the linear wir-motif around wipi β-propellers for autophagy
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/db704a1b9bd64094a44afc4f6fbb4ddb
work_keys_str_mv AT jinqiren multisitemediatedentwiningofthelinearwirmotifaroundwipibpropellersforautophagy
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AT wenjuanwang multisitemediatedentwiningofthelinearwirmotifaroundwipibpropellersforautophagy
AT dachuanzhang multisitemediatedentwiningofthelinearwirmotifaroundwipibpropellersforautophagy
AT liyu multisitemediatedentwiningofthelinearwirmotifaroundwipibpropellersforautophagy
AT weifeng multisitemediatedentwiningofthelinearwirmotifaroundwipibpropellersforautophagy
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