Sites at which mitochondria contact the endoplasmic reticulum co-localize the replication of mitochondria and their DNA to help ensure that DNA is distributed appropriately between the newly formed organelles in cells.

One minute biotinylation with APEX2 peroxidase in living cells identifies established and new components of mitochondrial and ER membranes; dataset intersection and overexpression screen identifies SYNJ2BP overexpression as inducing mitochondria-rough ER contacts.

A crucial step during the mitophagy cascade involves the disassembly of connections between mitochondria and the endoplasmic reticulum via the retrotranslocation of Mfn2 tethering complexes by the Parkinson's disease genes PARKIN and PINK1, as well as the ATPase VCP/p97.

Mfn2 depletion upregulates cytosolic Ca²⁺ in mouse fibroblast cells, leading to RhoA and nonmuscle myosin II overactivation and a prominent peripheral actin band structure, which is dependent on the contractile force on the cell–substrate interface.

An actin nucleating protein, Spire1C, localizes to the mitochondrial outer membrane and interacts with the endoplasmic reticulum-anchored formin protein INF2 to drive mitochondrial fission.

An extracellular modulator of IGF1 signaling, Pappaa, regulates endoplasmic reticulum–mitochondria connections, which are critical for metabolic homeostasis and hair cell survival.

ABHD16A is a phospholipid-modifying endoplasmic reticulum (ER) membrane protein required for both mitochondrial fission and fusion machinery recruitment to ER-associated mitochondrial constrictions.

Mechanically stimulating mitochondria causes them to divide via the recruitment of the mitochondrial fission machinery to the mechanically strained site, showing that intracellular organelles can be mechanoresponsive.

The p.Arg707Trp mutation in Mfn2 causes adipose-specific activation of the integrated stress response, which lowers secretion of adipokines.

An immunofluorescent analysis of 465 protein kinases revealed a substantial role of liquid-liquid phase separation in kinase localization and identified new kinase localizations to mitochondria and other organelles.