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 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. Interorganelle membrane contact sites between the endoplasmic reticulum and mitochondria can be mediated with the ER-mitochondria encounter structure (ERMES) complex, though precise regulation is unclear. Here, the authors report that the number of ERMES foci is regulated by the previously uncharacterized mitochondrial membrane protein Emr1.

Automated summary

This study reveals the crucial role of the previously uncharacterized mitochondrial membrane protein Emr1 in regulating the number of ERMES foci, with its absence significantly decreasing the foci number, affecting mitochondrial morphology and segregation. Emr1 interacts with the ERMES core component Mdm12 and is essential for ERMES functions, shedding light on the dynamic regulation of endoplasmic reticulum-mitochondria communication.