An autophagy assay reveals the ESCRT-III component CHMP2A as a regulator of phagophore closure

During autophagy, phagophores elongate to form double-membrane vesicles but the mechanism behind their closure is unknown. Here, the authors develop an autophagy assay and find a role for the endosomal sorting complexes required for transport component CHMP2A as a phagophore closure regulator.

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Autores principales: Yoshinori Takahashi, Haiyan He, Zhenyuan Tang, Tatsuya Hattori, Ying Liu, Megan M. Young, Jacob M. Serfass, Longgui Chen, Melat Gebru, Chong Chen, Carson A. Wills, Jennifer M. Atkinson, Han Chen, Thomas Abraham, Hong-Gang Wang
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Publicado: Nature Portfolio 2018
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Acceso en línea:https://doaj.org/article/dc0bd3a5e9b64caca02caa285ccc24af
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spelling oai:doaj.org-article:dc0bd3a5e9b64caca02caa285ccc24af2021-12-02T15:34:24ZAn autophagy assay reveals the ESCRT-III component CHMP2A as a regulator of phagophore closure10.1038/s41467-018-05254-w2041-1723https://doaj.org/article/dc0bd3a5e9b64caca02caa285ccc24af2018-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-05254-whttps://doaj.org/toc/2041-1723During autophagy, phagophores elongate to form double-membrane vesicles but the mechanism behind their closure is unknown. Here, the authors develop an autophagy assay and find a role for the endosomal sorting complexes required for transport component CHMP2A as a phagophore closure regulator.Yoshinori TakahashiHaiyan HeZhenyuan TangTatsuya HattoriYing LiuMegan M. YoungJacob M. SerfassLonggui ChenMelat GebruChong ChenCarson A. WillsJennifer M. AtkinsonHan ChenThomas AbrahamHong-Gang WangNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Yoshinori Takahashi
Haiyan He
Zhenyuan Tang
Tatsuya Hattori
Ying Liu
Megan M. Young
Jacob M. Serfass
Longgui Chen
Melat Gebru
Chong Chen
Carson A. Wills
Jennifer M. Atkinson
Han Chen
Thomas Abraham
Hong-Gang Wang
An autophagy assay reveals the ESCRT-III component CHMP2A as a regulator of phagophore closure
description During autophagy, phagophores elongate to form double-membrane vesicles but the mechanism behind their closure is unknown. Here, the authors develop an autophagy assay and find a role for the endosomal sorting complexes required for transport component CHMP2A as a phagophore closure regulator.
format article
author Yoshinori Takahashi
Haiyan He
Zhenyuan Tang
Tatsuya Hattori
Ying Liu
Megan M. Young
Jacob M. Serfass
Longgui Chen
Melat Gebru
Chong Chen
Carson A. Wills
Jennifer M. Atkinson
Han Chen
Thomas Abraham
Hong-Gang Wang
author_facet Yoshinori Takahashi
Haiyan He
Zhenyuan Tang
Tatsuya Hattori
Ying Liu
Megan M. Young
Jacob M. Serfass
Longgui Chen
Melat Gebru
Chong Chen
Carson A. Wills
Jennifer M. Atkinson
Han Chen
Thomas Abraham
Hong-Gang Wang
author_sort Yoshinori Takahashi
title An autophagy assay reveals the ESCRT-III component CHMP2A as a regulator of phagophore closure
title_short An autophagy assay reveals the ESCRT-III component CHMP2A as a regulator of phagophore closure
title_full An autophagy assay reveals the ESCRT-III component CHMP2A as a regulator of phagophore closure
title_fullStr An autophagy assay reveals the ESCRT-III component CHMP2A as a regulator of phagophore closure
title_full_unstemmed An autophagy assay reveals the ESCRT-III component CHMP2A as a regulator of phagophore closure
title_sort autophagy assay reveals the escrt-iii component chmp2a as a regulator of phagophore closure
publisher Nature Portfolio
publishDate 2018
url https://doaj.org/article/dc0bd3a5e9b64caca02caa285ccc24af
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