Open AccessMolecular Regulations of FUNDC1 at ER-Mitochondria Contacts Under Hypoxic Stress
Author(s) -
Yi Zhang,
Haixia Zhuang,
Hao Líu,
Du Feng
Publication year - 2022
Publication title -
contact
Language(s) - English
Resource type - Journals
ISSN - 2515-2564
DOI - 10.1177/25152564221092487
Subject(s) - endoplasmic reticulum , mitochondrion , microbiology and biotechnology , deubiquitinating enzyme , unfolded protein response , inner mitochondrial membrane , biology , chemistry , ubiquitin , biochemistry , gene
A recent research paper published in Journal of Cell Biology by Chen and colleagues describes a novel mechanism by which the MAM (Mitochondrial-associated endoplasmic reticulum membrane) protein FUNDC1 (FUN14 domain-containing protein 1) regulates mitochondrial division through altered protein post-translational modifications under hypoxic stress. The authors found that in a hypoxic environment, the endoplasmic reticulum-localized deubiquitinating enzyme USP19 accumulates at the MAM and interacts with the enriched mitochondrial outer membrane protein FUNDC1, which subsequently induces its deubiquitination and promotes the oligomerization and activity of DRP1, and mitochondria eventually divide in the presence of DRP1. This article provides new insights into the regulation of mitochondrial dynamics by FUNDC1 under hypoxic condition.