Yme1l1, a mitochondrial metalloproteinase, is an ATP-dependent metalloproteinase located in the mitochondrial inner membrane. Its protease domain faces the mitochondrial intermembrane space and modulates the processing of mitochondrial GTPase optic atrophy type 1 (OPA1), playing a crucial role in mitochondrial biogenesis, function, and quality control [2,3]. It is involved in pathways related to mitochondrial dynamics, energy metabolism, and apoptosis, which are of great biological importance in processes like embryonic development, cell survival, and response to stress [2,4]. Genetic models, especially gene knockout models, are valuable for studying Yme1l1.

In Sirt3 knockout mice injected with LPS, Sirt3 deficiency exacerbated LPS-induced renal pathological damage, apoptosis, and mitochondrial function and dynamics disturbances. Sirt3 overexpression alleviated these lesions by promoting OPA1-mediated mitochondrial fusion through deacetylating Yme1l1, an upstream regulatory molecule of OPA1 [1]. In early porcine embryonic development, knockdown of Yme1l1 led to decreased blastocyst rate and quality, mitochondrial fragmentation, excessive ROS production, lower mitochondrial membrane potential, and lower ATP levels. It also induced OPA1 cleavage, which was prevented by double knockdown of Yme1l1 and OMA1, and released cytochrome c, indicating its role in regulating mitochondrial fission, function, and apoptosis during preimplantation development [2].

In conclusion, Yme1l1 is essential for regulating mitochondrial fission, function, and apoptosis. The study of Yme1l1 knockout mouse models has contributed to understanding its role in acute kidney injury and early embryonic development, providing insights into the underlying mechanisms of these biological processes and potential disease-related mechanisms [1,2].