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内质网-线粒体接触结构及其调节蛋白

The Endoplasmic Reticulum-Mitochondria Encounter Structure and its Regulatory Proteins.

作者信息

Cheema Javairia Y, He Jiajia, Wei Wenfan, Fu Chuanhai

机构信息

Ministry of Education Key Laboratory for Cellular Dynamics, CAS Center for Excellence in Molecular Cell Sciences, Hefei National Laboratory for Physical Sciences at the Microscale, School of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, P.R. China.

出版信息

Contact (Thousand Oaks). 2021 Dec 6;4:25152564211064491. doi: 10.1177/25152564211064491. eCollection 2021 Jan-Dec.

DOI:10.1177/25152564211064491
PMID:37366373
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10243566/
Abstract

In fungi, the endoplasmic reticulum-mitochondria encounter structure (ERMES) is present between the endoplasmic reticulon (ER) and mitochondria to promote the formation of the ER-mitochondria contact sites. Four constitutive components (Mmm1, Mdm12, Mdm34, and Mdm10) assemble to form the ERMES complex while regulator proteins are required for regulating the organization and function of the ERMES complex. Multiple regulator proteins, including Gem1, Lam6, Tom7, and Emr1, of the ERMES complex, have been identified recently. In this review, we discuss the organization of the ERMES complex and the roles of the regulator proteins of the ERMES complex.

摘要

在真菌中,内质网-线粒体接触结构(ERMES)存在于内质网(ER)和线粒体之间,以促进内质网-线粒体接触位点的形成。四个组成成分(Mmm1、Mdm12、Mdm34和Mdm10)组装形成ERMES复合物,而调节蛋白对于调节ERMES复合物的组织和功能是必需的。最近已鉴定出ERMES复合物的多种调节蛋白,包括Gem1、Lam6、Tom7和Emr1。在本综述中,我们讨论了ERMES复合物的组织以及ERMES复合物调节蛋白的作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d1c5/10243566/cccdb64bad2c/10.1177_25152564211064491-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d1c5/10243566/2b1ec69ed25d/10.1177_25152564211064491-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d1c5/10243566/cccdb64bad2c/10.1177_25152564211064491-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d1c5/10243566/2b1ec69ed25d/10.1177_25152564211064491-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d1c5/10243566/cccdb64bad2c/10.1177_25152564211064491-fig2.jpg

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