Insights on autophagosome–lysosome tethering from structural and biochemical characterization of human autophagy factor EPG5

Nam and Cheung et al. describe the structural and biochemical characterization of human autophagy factor EPG5 that functions in autophagosome–lysosome tethering. They show that hEPG5 adopts an extended shepherd’s staff architecture, binds preferentially to GABARAP proteins, and is recruited to mitoc...

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Autores principales:	Sung-Eun Nam, Yiu Wing Sunny Cheung, Thanh Ngoc Nguyen, Michael Gong, Samuel Chan, Michael Lazarou, Calvin K. Yip
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/ac50183ec2794e35b04eadd21d872781
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spelling	oai:doaj.org-article:ac50183ec2794e35b04eadd21d8727812021-12-02T13:33:50ZInsights on autophagosome–lysosome tethering from structural and biochemical characterization of human autophagy factor EPG510.1038/s42003-021-01830-x2399-3642https://doaj.org/article/ac50183ec2794e35b04eadd21d8727812021-03-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-01830-xhttps://doaj.org/toc/2399-3642Nam and Cheung et al. describe the structural and biochemical characterization of human autophagy factor EPG5 that functions in autophagosome–lysosome tethering. They show that hEPG5 adopts an extended shepherd’s staff architecture, binds preferentially to GABARAP proteins, and is recruited to mitochondria during mitophagy.Sung-Eun NamYiu Wing Sunny CheungThanh Ngoc NguyenMichael GongSamuel ChanMichael LazarouCalvin K. YipNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Sung-Eun Nam Yiu Wing Sunny Cheung Thanh Ngoc Nguyen Michael Gong Samuel Chan Michael Lazarou Calvin K. Yip Insights on autophagosome–lysosome tethering from structural and biochemical characterization of human autophagy factor EPG5
description	Nam and Cheung et al. describe the structural and biochemical characterization of human autophagy factor EPG5 that functions in autophagosome–lysosome tethering. They show that hEPG5 adopts an extended shepherd’s staff architecture, binds preferentially to GABARAP proteins, and is recruited to mitochondria during mitophagy.
format	article
author	Sung-Eun Nam Yiu Wing Sunny Cheung Thanh Ngoc Nguyen Michael Gong Samuel Chan Michael Lazarou Calvin K. Yip
author_facet	Sung-Eun Nam Yiu Wing Sunny Cheung Thanh Ngoc Nguyen Michael Gong Samuel Chan Michael Lazarou Calvin K. Yip
author_sort	Sung-Eun Nam
title	Insights on autophagosome–lysosome tethering from structural and biochemical characterization of human autophagy factor EPG5
title_short	Insights on autophagosome–lysosome tethering from structural and biochemical characterization of human autophagy factor EPG5
title_full	Insights on autophagosome–lysosome tethering from structural and biochemical characterization of human autophagy factor EPG5
title_fullStr	Insights on autophagosome–lysosome tethering from structural and biochemical characterization of human autophagy factor EPG5
title_full_unstemmed	Insights on autophagosome–lysosome tethering from structural and biochemical characterization of human autophagy factor EPG5
title_sort	insights on autophagosome–lysosome tethering from structural and biochemical characterization of human autophagy factor epg5
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/ac50183ec2794e35b04eadd21d872781
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Insights on autophagosome–lysosome tethering from structural and biochemical characterization of human autophagy factor EPG5

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