RNF185, a novel mitochondrial ubiquitin E3 ligase, regulates autophagy through interaction with BNIP1.

Autophagy is an evolutionarily conserved catabolic process that allows recycling of cytoplasmic organelles, such as mitochondria, to offer a bioenergetically efficient pathway for cell survival. Considerable progress has been made in characterizing mitochondrial autophagy. However, the dedicated ubi...

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Autores principales:	Fei Tang, Bin Wang, Na Li, Yanfang Wu, Junying Jia, Talin Suo, Quan Chen, Yong-Jun Liu, Jie Tang
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/482315bc867649658105ff720b051591
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spelling	oai:doaj.org-article:482315bc867649658105ff720b0515912021-11-04T06:08:56ZRNF185, a novel mitochondrial ubiquitin E3 ligase, regulates autophagy through interaction with BNIP1.1932-620310.1371/journal.pone.0024367https://doaj.org/article/482315bc867649658105ff720b0515912011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21931693/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Autophagy is an evolutionarily conserved catabolic process that allows recycling of cytoplasmic organelles, such as mitochondria, to offer a bioenergetically efficient pathway for cell survival. Considerable progress has been made in characterizing mitochondrial autophagy. However, the dedicated ubiquitin E3 ligases targeting mitochondria for autophagy have not been revealed. Here we show that human RNF185 is a mitochondrial ubiquitin E3 ligase that regulates selective mitochondrial autophagy in cultured cells. The two C-terminal transmembrane domains of human RNF185 mediate its localization to mitochondrial outer membrane. RNF185 stimulates LC3II accumulation and the formation of autophagolysosomes in human cell lines. We further identified the Bcl-2 family protein BNIP1 as one of the substrates for RNF185. Human BNIP1 colocalizes with RNF185 at mitochondria and is polyubiquitinated by RNF185 through K63-based ubiquitin linkage in vivo. The polyubiquitinated BNIP1 is capable of recruiting autophagy receptor p62, which simultaneously binds both ubiquitin and LC3 to link ubiquitination and autophagy. Our study might reveal a novel RNF185-mediated mechanism for modulating mitochondrial homeostasis through autophagy.Fei TangBin WangNa LiYanfang WuJunying JiaTalin SuoQuan ChenYong-Jun LiuJie TangPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 9, p e24367 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Fei Tang Bin Wang Na Li Yanfang Wu Junying Jia Talin Suo Quan Chen Yong-Jun Liu Jie Tang RNF185, a novel mitochondrial ubiquitin E3 ligase, regulates autophagy through interaction with BNIP1.
description	Autophagy is an evolutionarily conserved catabolic process that allows recycling of cytoplasmic organelles, such as mitochondria, to offer a bioenergetically efficient pathway for cell survival. Considerable progress has been made in characterizing mitochondrial autophagy. However, the dedicated ubiquitin E3 ligases targeting mitochondria for autophagy have not been revealed. Here we show that human RNF185 is a mitochondrial ubiquitin E3 ligase that regulates selective mitochondrial autophagy in cultured cells. The two C-terminal transmembrane domains of human RNF185 mediate its localization to mitochondrial outer membrane. RNF185 stimulates LC3II accumulation and the formation of autophagolysosomes in human cell lines. We further identified the Bcl-2 family protein BNIP1 as one of the substrates for RNF185. Human BNIP1 colocalizes with RNF185 at mitochondria and is polyubiquitinated by RNF185 through K63-based ubiquitin linkage in vivo. The polyubiquitinated BNIP1 is capable of recruiting autophagy receptor p62, which simultaneously binds both ubiquitin and LC3 to link ubiquitination and autophagy. Our study might reveal a novel RNF185-mediated mechanism for modulating mitochondrial homeostasis through autophagy.
format	article
author	Fei Tang Bin Wang Na Li Yanfang Wu Junying Jia Talin Suo Quan Chen Yong-Jun Liu Jie Tang
author_facet	Fei Tang Bin Wang Na Li Yanfang Wu Junying Jia Talin Suo Quan Chen Yong-Jun Liu Jie Tang
author_sort	Fei Tang
title	RNF185, a novel mitochondrial ubiquitin E3 ligase, regulates autophagy through interaction with BNIP1.
title_short	RNF185, a novel mitochondrial ubiquitin E3 ligase, regulates autophagy through interaction with BNIP1.
title_full	RNF185, a novel mitochondrial ubiquitin E3 ligase, regulates autophagy through interaction with BNIP1.
title_fullStr	RNF185, a novel mitochondrial ubiquitin E3 ligase, regulates autophagy through interaction with BNIP1.
title_full_unstemmed	RNF185, a novel mitochondrial ubiquitin E3 ligase, regulates autophagy through interaction with BNIP1.
title_sort	rnf185, a novel mitochondrial ubiquitin e3 ligase, regulates autophagy through interaction with bnip1.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/482315bc867649658105ff720b051591
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RNF185, a novel mitochondrial ubiquitin E3 ligase, regulates autophagy through interaction with BNIP1.

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