Phosphorylation regulates the binding of autophagy receptors to FIP200 Claw domain for selective autophagy initiation

Cooperation between the ULK complex and autophagy receptors mediates targeting cargoes to autophagosomes. Here, the authors show that interactions of ULK subunit FIP200 with autophagy receptors CCPG1 and Optineurin can be regulated by phosphorylation, suggesting a general binding mode shared by auto...

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Autores principales:	Zixuan Zhou, Jianping Liu, Tao Fu, Ping Wu, Chao Peng, Xinyu Gong, Yingli Wang, Mingfang Zhang, Ying Li, Yaru Wang, Xiaolong Xu, Miao Li, Lifeng Pan
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/7866f28ceca14b898aab485fec664bfc
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spelling	oai:doaj.org-article:7866f28ceca14b898aab485fec664bfc2021-12-02T13:15:06ZPhosphorylation regulates the binding of autophagy receptors to FIP200 Claw domain for selective autophagy initiation10.1038/s41467-021-21874-12041-1723https://doaj.org/article/7866f28ceca14b898aab485fec664bfc2021-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21874-1https://doaj.org/toc/2041-1723Cooperation between the ULK complex and autophagy receptors mediates targeting cargoes to autophagosomes. Here, the authors show that interactions of ULK subunit FIP200 with autophagy receptors CCPG1 and Optineurin can be regulated by phosphorylation, suggesting a general binding mode shared by autophagy receptors.Zixuan ZhouJianping LiuTao FuPing WuChao PengXinyu GongYingli WangMingfang ZhangYing LiYaru WangXiaolong XuMiao LiLifeng PanNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Zixuan Zhou Jianping Liu Tao Fu Ping Wu Chao Peng Xinyu Gong Yingli Wang Mingfang Zhang Ying Li Yaru Wang Xiaolong Xu Miao Li Lifeng Pan Phosphorylation regulates the binding of autophagy receptors to FIP200 Claw domain for selective autophagy initiation
description	Cooperation between the ULK complex and autophagy receptors mediates targeting cargoes to autophagosomes. Here, the authors show that interactions of ULK subunit FIP200 with autophagy receptors CCPG1 and Optineurin can be regulated by phosphorylation, suggesting a general binding mode shared by autophagy receptors.
format	article
author	Zixuan Zhou Jianping Liu Tao Fu Ping Wu Chao Peng Xinyu Gong Yingli Wang Mingfang Zhang Ying Li Yaru Wang Xiaolong Xu Miao Li Lifeng Pan
author_facet	Zixuan Zhou Jianping Liu Tao Fu Ping Wu Chao Peng Xinyu Gong Yingli Wang Mingfang Zhang Ying Li Yaru Wang Xiaolong Xu Miao Li Lifeng Pan
author_sort	Zixuan Zhou
title	Phosphorylation regulates the binding of autophagy receptors to FIP200 Claw domain for selective autophagy initiation
title_short	Phosphorylation regulates the binding of autophagy receptors to FIP200 Claw domain for selective autophagy initiation
title_full	Phosphorylation regulates the binding of autophagy receptors to FIP200 Claw domain for selective autophagy initiation
title_fullStr	Phosphorylation regulates the binding of autophagy receptors to FIP200 Claw domain for selective autophagy initiation
title_full_unstemmed	Phosphorylation regulates the binding of autophagy receptors to FIP200 Claw domain for selective autophagy initiation
title_sort	phosphorylation regulates the binding of autophagy receptors to fip200 claw domain for selective autophagy initiation
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/7866f28ceca14b898aab485fec664bfc
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Phosphorylation regulates the binding of autophagy receptors to FIP200 Claw domain for selective autophagy initiation

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