A rare human mitofusin (MFN) 2 mutation that uniquely impaired Parkin-mediated mitophagy evoked developmental heart disease and increased myocardial sensitivity to doxorubicin in mice, differentiating it from mitophagy-competent MFN2 mutations that cause neuropathy and implicating mitophagy in clinical cardiomyopathy.

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.

Specific human mitofusin 2 mutations induce selective upper body obesity with suppressed leptin expression and severe adipose mitochondrial dysfunction.

A trial of mitofusin activation shows neuron regeneration and phenotype reversal in vitro and in vivo in experimental Charcot–Marie–Tooth disease type 2A caused by mitofusin 2 mutations.

The maintenance of proper mitochondrial-associated endoplasmic reticulum membranes is crucial for preventing skeletal muscle atrophy to interact with the Notch signaling pathway.

Mitochondrial fusion enables a metabolic transition during spermatogenesis.

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

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.

The dual role of Drosophila Mitofusin in steroid hormone production and cholesterol ester storage, which is evolutionary conserved by the combined expression of the two mammalian Mitofusins, ensures proper synaptic development.

In addition to increasing glycolysis, some proliferating cells exhibiting the Warburg effect also increase oxidative phosphorylation through mitochondrial fusion.