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Emr1 regulates the number of foci of the endoplasmic reticulum-mitochondria encounter structure complex
The endoplasmic reticulum-mitochondria encounter structure (ERMES) complex creates contact sites between the endoplasmic reticulum and mitochondria, playing crucial roles in interorganelle communication, mitochondrial fission, mtDNA inheritance, lipid transfer, and autophagy. The mechanism regulatin...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7822926/ https://www.ncbi.nlm.nih.gov/pubmed/33483504 http://dx.doi.org/10.1038/s41467-020-20866-x |
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author | Rasul, Faiz Zheng, Fan Dong, Fenfen He, Jiajia Liu, Ling Liu, Wenyue Cheema, Javairia Yousuf Wei, Wenfan Fu, Chuanhai |
author_facet | Rasul, Faiz Zheng, Fan Dong, Fenfen He, Jiajia Liu, Ling Liu, Wenyue Cheema, Javairia Yousuf Wei, Wenfan Fu, Chuanhai |
author_sort | Rasul, Faiz |
collection | PubMed |
description | The endoplasmic reticulum-mitochondria encounter structure (ERMES) complex creates contact sites between the endoplasmic reticulum and mitochondria, playing crucial roles in interorganelle communication, mitochondrial fission, mtDNA inheritance, lipid transfer, and autophagy. The mechanism regulating the number of ERMES foci within the cell remains unclear. Here, we demonstrate that the mitochondrial membrane protein Emr1 contributes to regulating the number of ERMES foci. We show that the absence of Emr1 significantly decreases the number of ERMES foci. Moreover, we find that Emr1 interacts with the ERMES core component Mdm12 and colocalizes with Mdm12 on mitochondria. Similar to ERMES mutant cells, cells lacking Emr1 display defective mitochondrial morphology and impaired mitochondrial segregation, which can be rescued by an artificial tether capable of linking the endoplasmic reticulum and mitochondria. We further demonstrate that the cytoplasmic region of Emr1 is required for regulating the number of ERMES foci. This work thus reveals a crucial regulatory protein necessary for ERMES functions and provides mechanistic insights into understanding the dynamic regulation of endoplasmic reticulum-mitochondria communication. |
format | Online Article Text |
id | pubmed-7822926 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-78229262021-01-29 Emr1 regulates the number of foci of the endoplasmic reticulum-mitochondria encounter structure complex Rasul, Faiz Zheng, Fan Dong, Fenfen He, Jiajia Liu, Ling Liu, Wenyue Cheema, Javairia Yousuf Wei, Wenfan Fu, Chuanhai Nat Commun Article The endoplasmic reticulum-mitochondria encounter structure (ERMES) complex creates contact sites between the endoplasmic reticulum and mitochondria, playing crucial roles in interorganelle communication, mitochondrial fission, mtDNA inheritance, lipid transfer, and autophagy. The mechanism regulating the number of ERMES foci within the cell remains unclear. Here, we demonstrate that the mitochondrial membrane protein Emr1 contributes to regulating the number of ERMES foci. We show that the absence of Emr1 significantly decreases the number of ERMES foci. Moreover, we find that Emr1 interacts with the ERMES core component Mdm12 and colocalizes with Mdm12 on mitochondria. Similar to ERMES mutant cells, cells lacking Emr1 display defective mitochondrial morphology and impaired mitochondrial segregation, which can be rescued by an artificial tether capable of linking the endoplasmic reticulum and mitochondria. We further demonstrate that the cytoplasmic region of Emr1 is required for regulating the number of ERMES foci. This work thus reveals a crucial regulatory protein necessary for ERMES functions and provides mechanistic insights into understanding the dynamic regulation of endoplasmic reticulum-mitochondria communication. Nature Publishing Group UK 2021-01-22 /pmc/articles/PMC7822926/ /pubmed/33483504 http://dx.doi.org/10.1038/s41467-020-20866-x Text en © The Author(s) 2021 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Rasul, Faiz Zheng, Fan Dong, Fenfen He, Jiajia Liu, Ling Liu, Wenyue Cheema, Javairia Yousuf Wei, Wenfan Fu, Chuanhai Emr1 regulates the number of foci of the endoplasmic reticulum-mitochondria encounter structure complex |
title | Emr1 regulates the number of foci of the endoplasmic reticulum-mitochondria encounter structure complex |
title_full | Emr1 regulates the number of foci of the endoplasmic reticulum-mitochondria encounter structure complex |
title_fullStr | Emr1 regulates the number of foci of the endoplasmic reticulum-mitochondria encounter structure complex |
title_full_unstemmed | Emr1 regulates the number of foci of the endoplasmic reticulum-mitochondria encounter structure complex |
title_short | Emr1 regulates the number of foci of the endoplasmic reticulum-mitochondria encounter structure complex |
title_sort | emr1 regulates the number of foci of the endoplasmic reticulum-mitochondria encounter structure complex |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7822926/ https://www.ncbi.nlm.nih.gov/pubmed/33483504 http://dx.doi.org/10.1038/s41467-020-20866-x |
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